NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034608882|ref|XP_016882599|]
View 

B-cell lymphoma 3 protein isoform X2 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
81-309 8.93e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 8.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  81 LSADIAMATRADEDGDTPLHIAVVQGNLpavhRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMA 160
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDL----LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 161 LDRHGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPL 240
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGA----DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034608882 241 IHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVA 309
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
81-309 8.93e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 8.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  81 LSADIAMATRADEDGDTPLHIAVVQGNLpavhRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMA 160
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDL----LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 161 LDRHGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPL 240
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGA----DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034608882 241 IHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVA 309
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 97-294 1.47e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.26  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  97 TPLHIAVvQGNLPAVhrLVNLFQQGGReLDIYNNLRQTPLHL-----AVITTLPSVVRLLVTAGASPMALDRHGQTAAHL 171
Cdd:PHA03100   37 LPLYLAK-EARNIDV--VKILLDNGAD-INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 172 ACEHR--SPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQET--VQLLLERGADIDA-------------VDIK 234
Cdd:PHA03100  113 AISKKsnSYSIVEYLLDNGA----NVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAknrvnyllsygvpINIK 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034608882 235 S--GRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGAD 294
Cdd:PHA03100  189 DvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
136-232 3.72e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 3.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 136 LHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAapgtlDLEARNYdGLTALHVAVNTECQ 215
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-----DVNLKDN-GRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 1034608882 216 ETVQLLLERGADIDAVD 232
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 134-274 4.58e-11

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.88  E-value: 4.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 134 TPLHLAVITT-LPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDsAAPGTLDLEARN--YDGLTALHVAV 210
Cdd:cd22192    19 SPLLLAAKENdVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPELVNEPMTSdlYQGETALHIAV 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034608882 211 NTECQETVQLLLERGADIDAVD-------------IKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALH 274
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRatgtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 200-274 5.29e-08

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 54.70  E-value: 5.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 200 YDGLTALHVAVNTECQETVQLLLERGADIDA------------VD-IKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQM 266
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsFYHGESPLNAAACLGSPSIVALLSEDPADILTAD 205


                  ....*...
gi 1034608882 267 YSGSSALH 274
Cdd:TIGR00870 206 SLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 236-264 5.50e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 5.50e-06
                           10        20
                   ....*....|....*....|....*....
gi 1034608882  236 GRSPLIHAVENNSLSMVQLLLQHGANVNA 264
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
81-309 8.93e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.50  E-value: 8.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  81 LSADIAMATRADEDGDTPLHIAVVQGNLpavhRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMA 160
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDL----LVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 161 LDRHGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPL 240
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGA----DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPL 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034608882 241 IHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVA 309
Cdd:COG0666   191 HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
129-312 2.07e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 2.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 129 NNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHV 208
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGA----DVNARDKDGETPLHL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 209 AVNTECQETVQLLLERGADIDAVDiKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTL 288
Cdd:COG0666   127 AAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205

                         170       180
                  ....*....|....*....|....
gi 1034608882 289 VRSGADSSLKNCHNDTPLMVARSR 312
Cdd:COG0666   206 LEAGADVNAKDNDGKTALDLAAEN 229
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
81-306 2.16e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 2.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  81 LSADIAMATRADEDGDTPLHIAVVQGNLPAVHRLVNLfqqgGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMA 160
Cdd:COG0666    73 LLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA----GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 161 LDRHGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPL 240
Cdd:COG0666   149 QDNDGNTPLHLAAANGNLEIVKLLLEAGA----DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD-NDGKTAL 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034608882 241 IHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPL 306
Cdd:COG0666   224 DLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
181-309 1.30e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.40  E-value: 1.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 181 LRALLDSAAPGTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHAVENNSLSMVQLLLQHGA 260
Cdd:COG0666    33 LLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD-DGGNTLLHAAARNGDLEIVKLLLEAGA 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034608882 261 NVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVA 309
Cdd:COG0666   112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 97-294 1.47e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.26  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  97 TPLHIAVvQGNLPAVhrLVNLFQQGGReLDIYNNLRQTPLHL-----AVITTLPSVVRLLVTAGASPMALDRHGQTAAHL 171
Cdd:PHA03100   37 LPLYLAK-EARNIDV--VKILLDNGAD-INSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 172 ACEHR--SPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQET--VQLLLERGADIDA-------------VDIK 234
Cdd:PHA03100  113 AISKKsnSYSIVEYLLDNGA----NVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAknrvnyllsygvpINIK 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034608882 235 S--GRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGAD 294
Cdd:PHA03100  189 DvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
136-232 3.72e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 3.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 136 LHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAapgtlDLEARNYdGLTALHVAVNTECQ 215
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-----DVNLKDN-GRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 1034608882 216 ETVQLLLERGADIDAVD 232
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
206-299 4.41e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 4.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 206 LHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHAVENNSLSMVQLLLQHgANVNAQMYsGSSALHSASGRGLLPLV 285
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 1034608882 286 RTLVRSGADSSLKN 299
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
170-265 4.69e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 4.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 170 HLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERgADIDAVDikSGRSPLIHAVENNSL 249
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGA----DANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD--NGRTALHYAARSGHL 74

                          90
                  ....*....|....*.
gi 1034608882 250 SMVQLLLQHGANVNAQ 265
Cdd:pfam12796  75 EIVKLLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 94-263 8.39e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.11  E-value: 8.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  94 DGDTPLHIAVVQGNLPAVHRLVNLfqqGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLAC 173
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDL---GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 174 EHRSPTCLRALLDSAApgTLDLEarNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQ 253
Cdd:PHA02875  144 MMGDIKGIELLIDHKA--CLDIE--DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVR 219

                         170
                  ....*....|
gi 1034608882 254 LLLQHGANVN 263
Cdd:PHA02875  220 LFIKRGADCN 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 92-309 1.62e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  92 DEDGDTPLHIAVvqgNLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSV-VRLLVTAGASPMALDRHGQTAAH 170
Cdd:PHA02876  270 DDCKNTPLHHAS---QAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDTEnIRTLIMLGADVNAADRLYITPLH 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 171 LACE-HRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSL 249
Cdd:PHA02876  347 QASTlDRNKDIVITLLELGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPY 422

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034608882 250 SMVQLLLQHGANVNAQMYSGSSALHSASGRGLLP-LVRTLVRSGADSSLKNCHNDTPLMVA 309
Cdd:PHA02876  423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA03095 PHA03095
ankyrin-like protein; Provisional
 83-310 1.21e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.68  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  83 ADIAMATRAdedGDTPLHIAVVQGNlpaVHRLVNLFQQGGRELDIYNNLRQTPLH--LAVITTLPSVVRLLVTAGASPMA 160
Cdd:PHA03095   74 ADVNAPERC---GFTPLHLYLYNAT---TLDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 161 LDRHGQTAahLACEHRSPTC----LRALLDSAApgtlDLEARNYDGLTALHV-AVNTECQETV-QLLLERGADIDAVDIk 234
Cdd:PHA03095  148 LDLYGMTP--LAVLLKSRNAnvelLRLLIDAGA----DVYAVDDRFRSLLHHhLQSFKPRARIvRELIRAGCDPAATDM- 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 235 SGRSPLIHAVENNSL--SMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPL--MVAR 310
Cdd:PHA03095  221 LGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLslMVRN 300
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 90-309 4.18e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.99  E-value: 4.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  90 RADEDGDTPLHIAVVQGNLPAV------------------------HRLVNLFQ-------QGGRELDIYNnLRQTPLHL 138
Cdd:PHA02878   65 QPDHRDLTPLHIICKEPNKLGMkemirsinkcsvfytlvaikdafnNRNVEIFKiiltnryKNIQTIDLVY-IDKKSKDD 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 139 AVITtlpSVVRLLVTAGASPMALDRH-GQTAAHLACEHRSPTCLRALLDSAA-PGTLDlEARNYdgltALHVAVNTECQE 216
Cdd:PHA02878  144 IIEA---EITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGAnVNIPD-KTNNS----PLHHAVKHYNKP 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 217 TVQLLLERGADIDAVDiKSGRSPLIHAVEN-NSLSMVQLLLQHGANVNAQMY-SGSSALHSA--SGRGLlplvRTLVRSG 292
Cdd:PHA02878  216 IVHILLENGASTDARD-KCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALHSSikSERKL----KLLLEYG 290

                         250
                  ....*....|....*..
gi 1034608882 293 ADSSLKNCHNDTPLMVA 309
Cdd:PHA02878  291 ADINSLNSYKLTPLSSA 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
 199-315 4.83e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 4.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 199 NYDGL---TALHVAVNTECQ---ETVQLLLERGADIDAVDIkSGRSPLIHAVENNS-LSMVQLLLQHGANVNAQMYSGSS 271
Cdd:PHA03095   41 NFRGEygkTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPER-CGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRT 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034608882 272 ALHS-ASGRGLLP-LVRTLVRSGADSSLKNCHNDTPLMVA-RSRRVS 315
Cdd:PHA03095  120 PLHVyLSGFNINPkVIRLLLRKGADVNALDLYGMTPLAVLlKSRNAN 166
PHA03095 PHA03095
ankyrin-like protein; Provisional
 134-309 7.75e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 7.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 134 TPLHLAVITTLP---SVVRLLVTAGASPMALDRHGQTAAHLACEHRS-PTCLRALLDSAApgtlDLEARNYDGLTALHVA 209
Cdd:PHA03095   49 TPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGA----DVNAKDKVGRTPLHVY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 210 VNTEC--QETVQLLLERGADIDAVDiKSGRSPLIHAVENN--SLSMVQLLLQHGANVNAQMYSGSSALHS--ASGRGLLP 283
Cdd:PHA03095  125 LSGFNinPKVIRLLLRKGADVNALD-LYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDRFRSLLHHhlQSFKPRAR 203

                         170       180
                  ....*....|....*....|....*.
gi 1034608882 284 LVRTLVRSGADSSLKNCHNDTPLMVA 309
Cdd:PHA03095  204 IVRELIRAGCDPAATDMLGNTPLHSM 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 93-309 1.64e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.15  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  93 EDGDTPLHIAVVQGNLpavhRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDrhgqtaahLA 172
Cdd:PHA02874   33 DETTTPLIDAIRSGDA----KIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILP--------IP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 173 CEHRSptCLRALLDSAapgtLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIkSGRSPLIHAVENNSLSMV 252
Cdd:PHA02874  101 CIEKD--MIKTILDCG----IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD-NGCYPIHIAIKHNFFDII 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034608882 253 QLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKnCHND-TPLMVA 309
Cdd:PHA02874  174 KLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNGfTPLHNA 230
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 135-312 2.78e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 135 PLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSaapgtldleaRNYDGLTALHVAVNTEC 214
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS----------INKCSVFYTLVAIKDAF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 215 -------------------------------------QETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQLLLQ 257
Cdd:PHA02878  110 nnrnveifkiiltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLS 189

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034608882 258 HGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSR 312
Cdd:PHA02878  190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY 244
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 97-264 4.45e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 4.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  97 TPLHIAVVQG-NLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTL--PSVVRLLVTAGASPMALDRHGQTAAHLA- 172
Cdd:PHA03100   70 TPLHYLSNIKyNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNSDGENLLHLYl 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 173 -CEHRSPTCLRALLDSAA------------PGTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKsGRSP 239
Cdd:PHA03100  150 eSNKIDLKILKLLIDKGVdinaknrvnyllSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY-GDTP 228

                         170       180
                  ....*....|....*....|....*
gi 1034608882 240 LIHAVENNSLSMVQLLLQHGANVNA 264
Cdd:PHA03100  229 LHIAILNNNKEIFKLLLNNGPSIKT 253
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 134-274 4.58e-11

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.88  E-value: 4.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 134 TPLHLAVITT-LPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDsAAPGTLDLEARN--YDGLTALHVAV 210
Cdd:cd22192    19 SPLLLAAKENdVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPELVNEPMTSdlYQGETALHIAV 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034608882 211 NTECQETVQLLLERGADIDAVD-------------IKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALH 274
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRatgtffrpgpknlIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 114-309 5.13e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 5.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 114 LVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAAPgtl 193
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY--- 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 194 dLEARNYDGLTALHVAVNTECQETVQLLLERGADIdAVDIKSGRSPLIHAVENNSlSMVQLLLQHgANVNAQMYSGSSAL 273
Cdd:PHA02874  183 -ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI-MNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPL 258

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034608882 274 HSAsgrgLLP-----LVRTLVRSGADSSLKNCHNDTPLMVA 309
Cdd:PHA02874  259 HHA----INPpcdidIIDILLYHKADISIKDNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 113-311 1.01e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.16  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 113 RLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAApgt 192
Cdd:PHA02876  159 LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS--- 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 193 ldleARNYDGLTALHVAVNTECqETVQLLLERGADIDAVDIKSgRSPLIHAVENNSLS-MVQLLLQHGANVNAQMYSGSS 271
Cdd:PHA02876  236 ----NINKNDLSLLKAIRNEDL-ETSLLLYDAGFSVNSIDDCK-NTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGET 309

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034608882 272 ALHSASGRGL-LPLVRTLVRSGADSSLKNCHNDTPLMVARS 311
Cdd:PHA02876  310 PLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAST 350
Ank_2 pfam12796
Ankyrin repeats (3 copies);
240-309 1.01e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 1.01e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 240 LIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVrSGADSSLKNcHNDTPLMVA 309
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYA 68
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 102-294 2.93e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 2.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 102 AVVQGNLPAVHRLVNLFQQGGREldIYNNLrqTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCL 181
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFE--IYDGI--SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 182 RALLDSaapGTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDaVDIKSGRSPLIHAVENNSLSMVQLLLQHGAN 261
Cdd:PHA02875   85 EELLDL---GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPD-IPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034608882 262 VNAQMYSGSSALHSASGRGLLPLVRTLVRSGAD 294
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
Ank_4 pfam13637
Ankyrin repeats (many copies);
202-256 5.83e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 5.83e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034608882 202 GLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHAVENNSLSMVQLLL 256
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 151-303 2.50e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 2.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 151 LVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGAdidA 230
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHAC----NVHIRDANGNTALWNAISAKHHKIFRILYHFAS---I 616

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034608882 231 VDIKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHND 303
Cdd:PLN03192  617 SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDD 689
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 99-306 3.63e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 3.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  99 LHIAVVQGNLPAVHrlvNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSP 178
Cdd:PHA02874    5 LRMCIYSGDIEAIE---KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 179 TCLRALLDsaapgtldlearnyDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSgRSPLIHAVENNSLSMVQLLLQH 258
Cdd:PHA02874   82 DIIKLLID--------------NGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEY 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034608882 259 GANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPL 306
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
92-162 5.25e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.81  E-value: 5.25e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034608882  92 DEDGDTPLHIAVVQGNLPAVHRLVNLFQQGGReldiynNLRQTPLHLAVITTLPSVVRLLVTAGASPMALD 162
Cdd:pfam12796  27 DKNGRTALHLAAKNGHLEIVKLLLEHADVNLK------DNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 182-277 1.18e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 182 RALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHAVENNSLSMVQLLLQH--- 258
Cdd:PTZ00322   99 RILLTGGA----DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KDGKTPLELAEENGFREVVQLLSRHsqc 173

                          90       100
                  ....*....|....*....|...
gi 1034608882 259 ----GANVNAQMYSGSSALHSAS 277
Cdd:PTZ00322  174 hfelGANAKPDSFTGKPPSLEDS 196
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
193-309 1.37e-08

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 55.35  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 193 LDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSA 272
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034608882 273 LHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVA 309
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 95-211 2.33e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.40  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  95 GDTPLHIAVVQGNLPAVHRLVN-------------LFQQGGRELDIYNnlrQTPLHLAVITTLPSVVRLLVTAGASPMAL 161
Cdd:cd22192    89 GETALHIAVVNQNLNLVRELIArgadvvspratgtFFRPGPKNLIYYG---EHPLSFAACVGNEEIVRLLIEHGADIRAQ 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034608882 162 DRHGQTAAH---------LACEhrsptCLRALLDSAAPG---TLDLeARNYDGLTALHVAVN 211
Cdd:cd22192   166 DSLGNTVLHilvlqpnktFACQ-----MYDLILSYDKEDdlqPLDL-VPNNQGLTPFKLAAK 221
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 92-240 3.88e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 3.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  92 DEDGDTPLHIAVVQGNlpavHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHL 171
Cdd:PHA02874  154 DDNGCYPIHIAIKHNF----FDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034608882 172 ACEH-RSPTCLraLLDSAAPGTLDLearnyDGLTALHVAVNTEC-QETVQLLLERGADIDAVDIKsGRSPL 240
Cdd:PHA02874  230 AIIHnRSAIEL--LINNASINDQDI-----DGSTPLHHAINPPCdIDIIDILLYHKADISIKDNK-GENPI 292
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 139-313 5.00e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 5.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 139 AVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDSAApgtldLEARNYDGL-TALHVAVNTECQET 217
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-----IPDVKYPDIeSELHDAVEEGDVKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 218 VQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSL 297
Cdd:PHA02875   84 VEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                         170
                  ....*....|....*.
gi 1034608882 298 KNCHNDTPLMVARSRR 313
Cdd:PHA02875  164 EDCCGCTPLIIAMAKG 179
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 92-232 5.15e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 5.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  92 DEDGDTPLHIAVVqgNLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLP--SVVRLLVTAGASPMALDR------ 163
Cdd:PHA03100  103 DNNGITPLLYAIS--KKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnylls 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034608882 164 ----------HGQTAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVD 232
Cdd:PHA03100  181 ygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGA----NPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 200-274 5.29e-08

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 54.70  E-value: 5.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 200 YDGLTALHVAVNTECQETVQLLLERGADIDA------------VD-IKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQM 266
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgVDsFYHGESPLNAAACLGSPSIVALLSEDPADILTAD 205


                  ....*...
gi 1034608882 267 YSGSSALH 274
Cdd:TIGR00870 206 SLGNTLLH 213
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 180-275 1.20e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 53.22  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 180 CLRALLDSAapgtldLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAV-------------DIKSGRSPLIHAVEN 246
Cdd:cd22194   125 ILDRFINAE------YTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkykheGFYFGETPLALAACT 198

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034608882 247 NSLSMVQLLLQHGA-NVNAQMYSGSSALHS 275
Cdd:cd22194   199 NQPEIVQLLMEKEStDITSQDSRGNTVLHA 228
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 198-309 1.46e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 52.75  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 198 RNYDGLTALHVAVNTECQETVQLLLERGADIDAVdIKSGRSPL-----IHAVENNSLSMVQLLLQHGANVNAQMYSGSSA 272
Cdd:PHA03100   31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSS-TKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITP 109

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034608882 273 LHSASGR--GLLPLVRTLVRSGADSSLKNCHNDTPLMVA 309
Cdd:PHA03100  110 LLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLY 148
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 180-306 2.19e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 180 CLRALLDSAapgTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKS----GRSPLIHAVENNSLSMVQLL 255
Cdd:cd22192    32 AIKKLLKCP---SCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGETALHIAVVNQNLNLVREL 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034608882 256 LQHGANVN--------------AQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPL 306
Cdd:cd22192   109 IARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
236-289 2.88e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034608882 236 GRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLV 289
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 165-274 8.88e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 50.65  E-value: 8.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 165 GQTAAHLAC--EHRSPTCLRALLDSAAPGTLDLE--------ARNYDGLTALHVAVNTECQETVQLLLERGADIDAVD-- 232
Cdd:cd21882    26 GKTCLHKAAlnLNDGVNEAIMLLLEAAPDSGNPKelvnapctDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034608882 233 ----------IKSGRSPLIHAVENNSLSMVQLLLQHG---ANVNAQMYSGSSALH 274
Cdd:cd21882   106 rffrkspgnlFYFGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 95-267 1.25e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.01  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  95 GDTPLHIAVVQGNLPA-------VHRLVNLFQQGgrelDIYnnLRQTPLHLAVITTLPSVVRLLVTAGASPmaldrhgQT 167
Cdd:cd22192    51 GETALHVAALYDNLEAavvlmeaAPELVNEPMTS----DLY--QGETALHIAVVNQNLNLVRELIARGADV-------VS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 168 A-AHLACEHRSPTCLRalldsaapgtldlearnYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHaven 246
Cdd:cd22192   118 PrATGTFFRPGPKNLI-----------------YYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD-SLGNTVLHI---- 175

                         170       180
                  ....*....|....*....|.
gi 1034608882 247 nslsmvqLLLQHGANVNAQMY 267
Cdd:cd22192   176 -------LVLQPNKTFACQMY 189
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 236-264 5.50e-06

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 5.50e-06
                           10        20
                   ....*....|....*....|....*....
gi 1034608882  236 GRSPLIHAVENNSLSMVQLLLQHGANVNA 264
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 201-232 7.79e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.28  E-value: 7.79e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1034608882 201 DGLTALHVAV-NTECQETVQLLLERGADIDAVD 232
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 95-224 8.97e-06

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 8.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  95 GDTPLHIAVVQGNLPAVHRLV------------NLFQQGGRELDIYNNlrQTPLHLAVITTLPSVVRLLVTAGASPMALD 162
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLergasvparacgDFFVKSQGVDSFYHG--ESPLNAAACLGSPSIVALLSEDPADILTAD 205

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034608882 163 RHGQTAAHLA-------CEHRSPTC-----LRALLDSAAPgTLDLEA-RNYDGLTALHVAVNTECQETVQLLLER 224
Cdd:TIGR00870 206 SLGNTLLHLLvmenefkAEYEELSCqmynfALSLLDKLRD-SKELEViLNHQGLTPLKLAAKEGRIVLFRLKLAI 279
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 83-139 1.44e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.48  E-value: 1.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034608882  83 ADIAMATRADedGDTPLHIAVVQGNlpavHRLVN-LFQQGGRELDIYNNLRQTPLHLA 139
Cdd:PHA02736   82 ADINGKERVF--GNTPLHIAVYTQN----YELATwLCNQPGVNMEILNYAFKTPYYVA 133
PHA03095 PHA03095
ankyrin-like protein; Provisional
 91-267 1.48e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  91 ADEDGDTPLHIAVVQGNLPAVhrLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAH 170
Cdd:PHA03095  218 TDMLGNTPLHSMATGSSCKRS--LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLS 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 171 LACEHRSPTCLRALLDSAAP-----GTLD-LEARNYDGLT------------------------ALHVAVNTEC-QETVQ 219
Cdd:PHA03095  296 LMVRNNNGRAVRAALAKNPSaetvaATLNtASVAGGDIPSdatrlcvakvvlrgafsllpepirAYHADFIRECeAEIAV 375

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034608882 220 LLLER-GADIDAVDIKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMY 267
Cdd:PHA03095  376 MRTTRiGTGVSLLDILFARNPDILLVSNASLRKKARLTVYGKALRARIE 424
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 252-309 2.78e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 2.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034608882 252 VQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVA 309
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 200-275 3.51e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 45.57  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 200 YDGLTALHVAVNTECQETVQLLLERGADIDAV-------DIKS------GRSPLIHAVENNSLSMVQLLLQH---GANVN 263
Cdd:cd22196    92 YKGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkKKKGgpgfyfGELPLSLAACTNQLDIVKFLLENphsPADIS 171

                          90
                  ....*....|..
gi 1034608882 264 AQMYSGSSALHS 275
Cdd:cd22196   172 ARDSMGNTVLHA 183
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 81-240 3.78e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  81 LSADIAmatraDEDGDTPLHIAVVQGNLPAVhrLVNLfqQGGRELDIYNNLRQTPLHLAVITTLPSVVRLL--VTAGASP 158
Cdd:PLN03192  549 LDPDIG-----DSKGRTPLHIAASKGYEDCV--LVLL--KHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDP 619

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 159 maldrhgQTAAHLACE---HRSPTCLRALLDSAapgtLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKS 235
Cdd:PLN03192  620 -------HAAGDLLCTaakRNDLTAMKELLKQG----LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688


                  ....*
gi 1034608882 236 GRSPL 240
Cdd:PLN03192  689 DFSPT 693
Ank_5 pfam13857
Ankyrin repeats (many copies);
117-172 4.26e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 4.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034608882 117 LFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLA 172
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 236-265 6.55e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 6.55e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034608882 236 GRSPLIHAV-ENNSLSMVQLLLQHGANVNAQ 265
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 236-264 6.58e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 6.58e-05
                          10        20
                  ....*....|....*....|....*....
gi 1034608882 236 GRSPLIHAVENNSLSMVQLLLQHGANVNA 264
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 200-275 8.17e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.40  E-value: 8.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 200 YDGLTALHVAVNTECQETVQLLLERGADIDAVD-------------IKSGRSPLIHAVENNSLSMVQLLLQHG---ANVN 263
Cdd:cd22193    74 YEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegFYFGELPLSLAACTNQPDIVQYLLENEhqpADIE 153

                          90
                  ....*....|..
gi 1034608882 264 AQMYSGSSALHS 275
Cdd:cd22193   154 AQDSRGNTVLHA 165
PHA02741 PHA02741
hypothetical protein; Provisional
 228-313 9.44e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 42.34  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 228 IDAVDIKSGRSPLIHAVENN---SLSMVQLLLQHGANVNAQ-MYSGSSALHSASGRGLLPLVRTLVRS-GADSSLKNCHN 302
Cdd:PHA02741   53 LNATDDAGQMCIHIAAEKHEaqlAAEIIDHLIELGADINAQeMLEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADN 132

                          90
                  ....*....|.
gi 1034608882 303 DTPLMVARSRR 313
Cdd:PHA02741  133 KSPFELAIDNE 143
Ank_5 pfam13857
Ankyrin repeats (many copies);
191-243 1.00e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034608882 191 GTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPLIHA 243
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKD-EEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
221-276 1.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 1.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034608882 221 LLERG-ADIDAVDiKSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSA 276
Cdd:pfam13857   1 LLEHGpIDLNRLD-GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
150-209 2.78e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 150 LLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALLDsaapGTLDLEARNYDGLTALHVA 209
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA----YGVDLNLKDEEGLTALDLA 56
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 200-275 4.57e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 42.15  E-value: 4.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 200 YDGLTALHVAVNTECQETVQLLLERGADIDAVD-------------IKSGRSPLIHAVENNSLSMVQLLLQHG---ANVN 263
Cdd:cd22195   135 YRGQTALHIAIERRCKHYVELLVEKGADVHAQArgrffqpkdeggyFYFGELPLSLAACTNQPDIVHYLTENAhkkADLR 214

                          90
                  ....*....|..
gi 1034608882 264 AQMYSGSSALHS 275
Cdd:cd22195   215 RQDSRGNTVLHA 226
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 199-293 5.57e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 5.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 199 NYDGLTALHVAVN---TECQETVQLLLERGADIDAVDIKSGRSPLIHAVENNSLSMVQLLL-QHGANVNAQMYSGSSALH 274
Cdd:PHA02736   52 NRHGKQCVHIVSNpdkADPQEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYY 131

                          90
                  ....*....|....*....
gi 1034608882 275 SASGRGLLPLVRTLVRSGA 293
Cdd:PHA02736  132 VACERHDAKMMNILRAKGA 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 201-230 7.07e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 7.07e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034608882  201 DGLTALHVAVNTECQETVQLLLERGADIDA 230
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
255-309 8.22e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 8.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034608882 255 LLQHG-ANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVA 309
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 115-174 8.45e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 8.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 115 VNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACE 174
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEE 157
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 95-224 1.08e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.02  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882  95 GDTPLHIAVVQGNLPAVHRLV------------NLFQQGGRELDIYNNLrqtPLHLAVITTLPSVVRLLVTAGASPMAL- 161
Cdd:cd21882    73 GQTALHIAIENRNLNLVRLLVengadvsaratgRFFRKSPGNLFYFGEL---PLSLAACTNQEEIVRLLLENGAQPAALe 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034608882 162 --DRHGQTAAHLACEHRSPTCLR-ALLDSAAPGTLDLEAR-----------NYDGLTALHVAVNTECQETVQLLLER 224
Cdd:cd21882   150 aqDSLGNTVLHALVLQADNTPENsAFVCQMYNLLLSYGAHldptqqleeipNHQGLTPLKLAAVEGKIVMFQHILQR 226
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 92-164 1.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 1.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034608882  92 DEDGDTPLHIAVVQGNLPAVHRLVNLfqqgGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRH 164
Cdd:PHA03100  189 DVYGFTPLHYAVYNNNPEFVKYLLDL----GANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 165-261 2.06e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.16  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 165 GQTAAHLACEHRSPTCLRALLDSAApgtlDLEARN--------------YDGLTALHVAVNTECQETVQLLLE---RGAD 227
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGA----DVHAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLEnehQPAD 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034608882 228 IDAVDikSGRSPLIHA--------VENNSL--SMVQLLLQHGAN 261
Cdd:cd22193   152 IEAQD--SRGNTVLHAlvtvadntKENTKFvtRMYDMILIRGAK 193
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 218-300 3.41e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 218 VQLLLERGADIDAVDIkSGRSPLIHAVENNSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVR-SGADSS 296
Cdd:PTZ00322   98 ARILLTGGADPNCRDY-DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhSQCHFE 176


                  ....
gi 1034608882 297 LKNC 300
Cdd:PTZ00322  177 LGAN 180
PHA02946 PHA02946
ankyin-like protein; Provisional
 201-263 3.89e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 3.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034608882 201 DGLTALHVAVNTECQETVQLLLERGADIDAVDiKSGRSPL--IHAVENNSLSMVQLLLQHGANVN 263
Cdd:PHA02946   71 DGNYPLHIASKINNNRIVAMLLTHGADPNACD-KQHKTPLyyLSGTDDEVIERINLLVQYGAKIN 134
Ank_4 pfam13637
Ankyrin repeats (many copies);
167-222 3.99e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 3.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034608882 167 TAAHLACEHRSPTCLRALLDSAApgtlDLEARNYDGLTALHVAV---NTECqetVQLLL 222
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGA----DINAVDGNGETALHFAAsngNVEV---LKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 190-303 4.71e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.91  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034608882 190 PGTLDLEARNYDGLTAL-HVAVNTECQETVQLLLERGADIDAVDiksgrsPLIHAVENNSLSMVQLLLQHGAN------- 261
Cdd:TIGR00870  40 PKKLNINCPDRLGRSALfVAAIENENLELTELLLNLSCRGAVGD------TLLHAISLEYVDAVEAILLHLLAafrksgp 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034608882 262 ---VNAQM----YSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHND 303
Cdd:TIGR00870 114 lelANDQYtsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDF 162
Ank_4 pfam13637
Ankyrin repeats (many copies);
134-185 5.10e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 5.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034608882 134 TPLHLAVITTLPSVVRLLVTAGASPMALDRHGQTAAHLACEHRSPTCLRALL 185
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH