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Conserved domains on  [gi|271398185|ref|NP_001162002|]
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ankyrin repeat and SOCS box protein 9 isoform 3 [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

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-251 1.58e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  36 DWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSW 115
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 116 DCVNLLLQHGAsvqpesdlaspiheaarrayggNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLH 194
Cdd:COG0666  167 EIVKLLLEAGA----------------------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNaKDNDGKTALD 224

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 271398185 195 AVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPESPLAQLFLEREGASLPKPK 251
Cdd:COG0666  225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-251 1.58e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  36 DWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSW 115
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 116 DCVNLLLQHGAsvqpesdlaspiheaarrayggNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLH 194
Cdd:COG0666  167 EIVKLLLEAGA----------------------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNaKDNDGKTALD 224

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 271398185 195 AVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPESPLAQLFLEREGASLPKPK 251
Cdd:COG0666  225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
Ank_2 pfam12796
Ankyrin repeats (3 copies);
40-128 2.11e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185   40 MHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHgAQVNGVTADWhTPLFNACVSGSWDCVN 119
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78


                  ....*....
gi 271398185  120 LLLQHGASV 128
Cdd:pfam12796  79 LLLEKGADI 87
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-226 2.01e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.00  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  45 IHGHQLSL-RNLI-SQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLL 122
Cdd:PHA02874   9 IYSGDIEAiEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 123 QHG--ASVQP----ESDLASPIHEAarrayGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLHA 195
Cdd:PHA02874  89 DNGvdTSILPipciEKDMIKTILDC-----GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNGCYPIHI 163

                        170       180       190
                 ....*....|....*....|....*....|.
gi 271398185 196 VARTASEELACLLMDFGADTQAKNAEGKRPV 226
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 81-217 1.80e-05

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: 45.46  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185   81 HLSCVKILLKHGAQvnGVTADwhtPLFNACVSGSWDCVNLLLQHGASVQPESDlaSPIHEAARraYGGNIDHKIshlgTP 160
Cdd:TIGR00870  65 NLELTELLLNLSCR--GAVGD---TLLHAISLEYVDAVEAILLHLLAAFRKSG--PLELANDQ--YTSEFTPGI----TA 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 271398185  161 LYLACENQQRACVKKLLESGADVN---------QGKGQD------SPLHAVARTASEELACLLMDFGADTQA 217
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDsfyhgeSPLNAAACLGSPSIVALLSEDPADILT 203
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 68-96 3.34e-05

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: 39.88  E-value: 3.34e-05
                           10        20
                   ....*....|....*....|....*....
gi 271398185    68 DHVSPLHEACLGGHLSCVKILLKHGAQVN 96
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-211 3.83e-04

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: 41.15  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  73 LHEACLGGHLSCVKILLKHGAQ-VN-GVTADWH---TPLFNACVSGSWDCVNLLLQHGASVQpesdlaSPiheaarRAYG 147
Cdd:cd22192   55 LHVAALYDNLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAVVNQNLNLVRELIARGADVV------SP------RATG 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 271398185 148 G----NIDHKISHLGTPL-YLACENQQRAcVKKLLESGADVnqgKGQDS----PLHAVARTASEELACLLMDF 211
Cdd:cd22192  123 TffrpGPKNLIYYGEHPLsFAACVGNEEI-VRLLIEHGADI---RAQDSlgntVLHILVLQPNKTFACQMYDL 191
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-251 1.58e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  36 DWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSW 115
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 116 DCVNLLLQHGAsvqpesdlaspiheaarrayggNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLH 194
Cdd:COG0666  167 EIVKLLLEAGA----------------------DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNaKDNDGKTALD 224

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 271398185 195 AVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPESPLAQLFLEREGASLPKPK 251
Cdd:COG0666  225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-224 2.66e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.50  E-value: 2.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  35 SDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGS 114
Cdd:COG0666  119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 115 WDCVNLLLQHGAsvqpesdlaspiheaarrayggNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQDSPL 193
Cdd:COG0666  199 LEIVKLLLEAGA----------------------DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNaKDKDGLTAL 256

                        170       180       190
                 ....*....|....*....|....*....|.
gi 271398185 194 HAVARTASEELACLLMDFGADTQAKNAEGKR 224
Cdd:COG0666  257 LLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-228 3.93e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 100.41  E-value: 3.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  32 DAVSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACV 111
Cdd:COG0666   17 LLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAAR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 112 SGSWDCVNLLLQHGASV-QPESDLASPIHEAARR----------AYGGNIDHKISHLGTPLYLACENQQRACVKKLLESG 180
Cdd:COG0666   97 NGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNgnleivklllEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 271398185 181 ADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVEL 228
Cdd:COG0666  177 ADVNaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
40-128 2.11e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185   40 MHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHgAQVNGVTADWhTPLFNACVSGSWDCVN 119
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78


                  ....*....
gi 271398185  120 LLLQHGASV 128
Cdd:pfam12796  79 LLLEKGADI 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-185 6.34e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 6.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185   73 LHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHgasvqpesdlaspiheaarraygGNIDH 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-----------------------ADVNL 57

                          90       100       110
                  ....*....|....*....|....*....|...
gi 271398185  153 KiSHLGTPLYLACENQQRACVKKLLESGADVNQ 185
Cdd:pfam12796  58 K-DNGRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-226 2.01e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.00  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  45 IHGHQLSL-RNLI-SQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLL 122
Cdd:PHA02874   9 IYSGDIEAiEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 123 QHG--ASVQP----ESDLASPIHEAarrayGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLHA 195
Cdd:PHA02874  89 DNGvdTSILPipciEKDMIKTILDC-----GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNGCYPIHI 163

                        170       180       190
                 ....*....|....*....|....*....|.
gi 271398185 196 VARTASEELACLLMDFGADTQAKNAEGKRPV 226
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-184 1.03e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.40  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  38 SPMHEAAIHGHQL-SLRNLISQGWAVNIITADHVSPLHEA-CLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSW 115
Cdd:PHA02876 309 TPLYLMAKNGYDTeNIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNV 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 116 DCVNLLLQHGASVQPESD-LASPIHEA--ARRAY---------GGNIDHKISHLGTPLYLACENQQRA-CVKKLLESGAD 182
Cdd:PHA02876 389 VIINTLLDYGADIEALSQkIGTALHFAlcGTNPYmsvktlidrGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGAD 468


                 ..
gi 271398185 183 VN 184
Cdd:PHA02876 469 VN 470
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 17-229 4.61e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 4.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  17 RDFPGIRLLSNPLMGDaVSDWS---PMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGH-----LSCVKIL 88
Cdd:PHA03100  14 KVKNIKYIIMEDDLND-YSYKKpvlPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  89 LKHGAQVNGVTADWHTPLFNACV--SGSWDCVNLLLQHGASVQP-ESDLASPIHEAARrayGGNIDHKISHL----GTPL 161
Cdd:PHA03100  93 LEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIkNSDGENLLHLYLE---SNKIDLKILKLlidkGVDI 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 162 YLACEnqqracVKKLLESGADVN--QGKGqDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELV 229
Cdd:PHA03100 170 NAKNR------VNYLLSYGVPINikDVYG-FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 30-199 2.41e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  30 MGDAVSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNA 109
Cdd:PHA02878 162 MKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 110 CVS-GSWDCVNLLLQHGASVqpesdlaspiheaarrayggNIDHKISHLgTPLYLACENQQRacVKKLLESGADVNQ-GK 187
Cdd:PHA02878 242 VGYcKDYDILKLLLEHGVDV--------------------NAKSYILGL-TALHSSIKSERK--LKLLLEYGADINSlNS 298

                        170
                 ....*....|..
gi 271398185 188 GQDSPLHAVART 199
Cdd:PHA02878 299 YKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 38-215 5.51e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 5.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  38 SPMHEAAIHGHQLSLRNLISQG-WAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWD 116
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLDLGkFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 117 CVNLLLQHGASVQPESdlaspiheaarrAYGgnidhkishlGTPLYLACENQQRACVKKLLESGADVNQ-GKGQDSPLHA 195
Cdd:PHA02875 150 GIELLIDHKACLDIED------------CCG----------CTPLIIAMAKGDIAICKMLLDSGANIDYfGKNGCVAALC 207

                        170       180
                 ....*....|....*....|.
gi 271398185 196 VA-RTASEELACLLMDFGADT 215
Cdd:PHA02875 208 YAiENNKIDIVRLFIKRGADC 228
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 43-183 7.90e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.64  E-value: 7.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  43 AAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLL 122
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 271398185 123 QHGASVQPES--DLaspIHEAARRA----------YGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADV 183
Cdd:PLN03192 612 HFASISDPHAagDL---LCTAAKRNdltamkellkQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 52-229 8.55e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 8.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  52 LRNLISQGWAVNIITADHV-SPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGAsvqp 130
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA---- 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 131 esdlaspiheaarrayggNIDHKISHLGTPLYLA---CENQQraCVKKLLESGADVNQGKG--QDSPLHAVARtaSEELA 205
Cdd:PHA02878 226 ------------------STDARDKCGNTPLHISvgyCKDYD--ILKLLLEHGVDVNAKSYilGLTALHSSIK--SERKL 283

                        170       180
                 ....*....|....*....|....
gi 271398185 206 CLLMDFGADTQAKNAEGKRPVELV 229
Cdd:PHA02878 284 KLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-96 1.39e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.88  E-value: 1.39e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185   37 WSPMHEAAIHGHQLSLRNLISQgWAVNIITaDHVSPLHEACLGGHLSCVKILLKHGAQVN 96
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 42-132 2.93e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  42 EAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLL 121
Cdd:PTZ00322  88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                         90
                 ....*....|....*...
gi 271398185 122 LQH-------GASVQPES 132
Cdd:PTZ00322 168 SRHsqchfelGANAKPDS 185
Ank_4 pfam13637
Ankyrin repeats (many copies);
37-89 5.50e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 5.50e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 271398185   37 WSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILL 89
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
69-122 1.18e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.18e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 271398185   69 HVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLL 122
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-217 2.87e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 2.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  38 SPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVK-----------------------------IL 88
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkndlsllkairnedletslLL 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  89 LKHGAQVNGVTADWHTPLFNACVSGSWD-CVNLLLQHGASVQPES-DLASPIHEAARRAY-----------GGNIDHKIS 155
Cdd:PHA02876 260 YDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNiKGETPLYLMAKNGYdtenirtlimlGADVNAADR 339

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 271398185 156 HLGTPLYLACE-NQQRACVKKLLESGADVNQGKGQD-SPLHAVARTASEELACLLMDFGADTQA 217
Cdd:PHA02876 340 LYITPLHQASTlDRNKDIVITLLELGANVNARDYCDkTPIHYAAVRNNVVIINTLLDYGADIEA 403
PHA03095 PHA03095
ankyrin-like protein; Provisional
 52-222 8.08e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 8.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  52 LRNLISQGWAVNIITADHVSPLHeACLggHLSC------VKILLKHGAQVNGVTADWHTPLF----NACVsgsWDCVNLL 121
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLH-LYL--HYSSekvkdiVRLLLEAGADVNAPERCGFTPLHlylyNATT---LDVIKLL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 122 LQHGASVQPESDlaspiheaarraYGGNIDHKishlgtplYLACENQQRACVKKLLESGADVNQGKGQD-SPLHA--VAR 198
Cdd:PHA03095 104 IKAGADVNAKDK------------VGRTPLHV--------YLSGFNINPKVIRLLLRKGADVNALDLYGmTPLAVllKSR 163

                        170       180
                 ....*....|....*....|....
gi 271398185 199 TASEELACLLMDFGADTQAKNAEG 222
Cdd:PHA03095 164 NANVELLRLLIDAGADVYAVDDRF 187
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-130 9.92e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 9.92e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 271398185  55 LISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGASVQP 130
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-219 3.99e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.37  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  55 LISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGASVQpESDL 134
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN-KNDL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 135 A------SPIHEAARRAY--GGNIDHKISHLGTPLYLACENQQRA-CVKKLLESGADVNQG--KGQdSPLHAVARTA--S 201
Cdd:PHA02876 243 SllkairNEDLETSLLLYdaGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKniKGE-TPLYLMAKNGydT 321

                        170
                 ....*....|....*...
gi 271398185 202 EELACLLMdFGADTQAKN 219
Cdd:PHA02876 322 ENIRTLIM-LGADVNAAD 338
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-227 5.45e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 5.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  40 MHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVN 119
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 120 LLLQHGAsvqpesdlaspiheaarrayggNIDHKISHLGTPLYLACENQQRACvkKLLESGADVN-QGKGQDSPLH-AVA 197
Cdd:PHA02874 208 LLIDHGN----------------------HIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINdQDIDGSTPLHhAIN 263

                        170       180       190
                 ....*....|....*....|....*....|
gi 271398185 198 RTASEELACLLMDFGADTQAKNAEGKRPVE 227
Cdd:PHA02874 264 PPCDIDIIDILLYHKADISIKDNKGENPID 293
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 82-229 9.19e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.21  E-value: 9.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  82 LSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVNLLLQHGASVQPESDLASPIHEAARRAygGNID---------H 152
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS--KNIDtikaiidnrS 235

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 271398185 153 KISHLGTPLYLACENQQRACVKKLLESGADVNQ-GKGQDSPLHAVARTAS-EELACLLMDFGADTQAKNAEGKRPVELV 229
Cdd:PHA02876 236 NINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSiDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLM 314
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 40-226 1.04e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  40 MHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSWDCVN 119
Cdd:PHA02875   6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 120 LLLQHGasvqpesdlaspiheaarrAYGGNIDHKISHlgTPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLHAVAR 198
Cdd:PHA02875  86 ELLDLG-------------------KFADDVFYKDGM--TPLHLATILKKLDIMKLLIARGADPDiPNTDKFSPLHLAVM 144

                        170       180
                 ....*....|....*....|....*...
gi 271398185 199 TASEELACLLMDFGADTQAKNAEGKRPV 226
Cdd:PHA02875 145 MGDIKGIELLIDHKACLDIEDCCGCTPL 172
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 81-217 1.80e-05

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: 45.46  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185   81 HLSCVKILLKHGAQvnGVTADwhtPLFNACVSGSWDCVNLLLQHGASVQPESDlaSPIHEAARraYGGNIDHKIshlgTP 160
Cdd:TIGR00870  65 NLELTELLLNLSCR--GAVGD---TLLHAISLEYVDAVEAILLHLLAAFRKSG--PLELANDQ--YTSEFTPGI----TA 131

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 271398185  161 LYLACENQQRACVKKLLESGADVN---------QGKGQD------SPLHAVARTASEELACLLMDFGADTQA 217
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDsfyhgeSPLNAAACLGSPSIVALLSEDPADILT 203
PHA03095 PHA03095
ankyrin-like protein; Provisional
 72-226 2.20e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  72 PLHeACLGG---HLSCVKILLKHGAQVNGVTADWHTPLF------NACVsgswDCVNLLLQHGASV-QPESDLASPIHEA 141
Cdd:PHA03095 120 PLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllksrNANV----ELLRLLIDAGADVyAVDDRFRSLLHHH 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 142 AR--RAY----------GGNIDHKISHLGTPL-YLACENQQRAC-VKKLLESGADVN--QGKGQdSPLHAVARTASEELA 205
Cdd:PHA03095 195 LQsfKPRarivreliraGCDPAATDMLGNTPLhSMATGSSCKRSlVLPLLIAGISINarNRYGQ-TPLHYAAVFNNPRAC 273

                        170       180
                 ....*....|....*....|.
gi 271398185 206 CLLMDFGADTQAKNAEGKRPV 226
Cdd:PHA03095 274 RRLIALGADINAVSSDGNTPL 294
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 50-129 2.82e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  50 LSLRNLISQGWAVNIITADHVSPLHEACLGG-HLSCVKILLKHGAQVNGVTADWHTPLFNACvsGSWDCVNLLLQHGASV 128
Cdd:PHA02876 423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500


                 .
gi 271398185 129 Q 129
Cdd:PHA02876 501 R 501
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 68-96 3.34e-05

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: 39.88  E-value: 3.34e-05
                           10        20
                   ....*....|....*....|....*....
gi 271398185    68 DHVSPLHEACLGGHLSCVKILLKHGAQVN 96
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 36-128 9.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 9.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  36 DWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGH-LSCVKILLKHGAQVNGVTADWHTPLFNACVSG- 113
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNc 454

                         90
                 ....*....|....*
gi 271398185 114 SWDCVNLLLQHGASV 128
Cdd:PHA02876 455 KLDVIEMLLDNGADV 469
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-211 3.83e-04

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: 41.15  E-value: 3.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  73 LHEACLGGHLSCVKILLKHGAQ-VN-GVTADWH---TPLFNACVSGSWDCVNLLLQHGASVQpesdlaSPiheaarRAYG 147
Cdd:cd22192   55 LHVAALYDNLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAVVNQNLNLVRELIARGADVV------SP------RATG 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 271398185 148 G----NIDHKISHLGTPL-YLACENQQRAcVKKLLESGADVnqgKGQDS----PLHAVARTASEELACLLMDF 211
Cdd:cd22192  123 TffrpGPKNLIYYGEHPLsFAACVGNEEI-VRLLIEHGADI---RAQDSlgntVLHILVLQPNKTFACQMYDL 191
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 123-228 4.02e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 123 QHGASVQ-PESDLASPIHEAARRAyggNIDHKISHLgtplyLACENQQRAC------VKKLLESGADVN-QGKGQDSPLH 194
Cdd:PTZ00322  49 THLEALEaTENKDATPDHNLTTEE---VIDPVVAHM-----LTVELCQLAAsgdavgARILLTGGADPNcRDYDGRTPLH 120

                         90       100       110
                 ....*....|....*....|....*....|....
gi 271398185 195 AVARTASEELACLLMDFGADTQAKNAEGKRPVEL 228
Cdd:PTZ00322 121 IACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 159-184 4.04e-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: 36.80  E-value: 4.04e-04
                           10        20
                   ....*....|....*....|....*.
gi 271398185   159 TPLYLACENQQRACVKKLLESGADVN 184
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 39-141 5.49e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 5.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  39 PMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNACVSGSwDCV 118
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAI 238

                         90       100
                 ....*....|....*....|...
gi 271398185 119 NLLLQHGASVQPESDLASPIHEA 141
Cdd:PHA02874 239 ELLINNASINDQDIDGSTPLHHA 261
Ank_5 pfam13857
Ankyrin repeats (many copies);
60-106 6.60e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 6.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 271398185   60 WAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPL 106
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 71-96 6.79e-04

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: 36.11  E-value: 6.79e-04
                          10        20
                  ....*....|....*....|....*..
gi 271398185   71 SPLHEACL-GGHLSCVKILLKHGAQVN 96
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVN 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 78-221 1.14e-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: 39.86  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  78 LGGHLSCVKILLKHGAQVNGVTADwhTPLFNACV---SGSWDCVNLLLQhgasVQPESDLASPI--HEAARRAYGGNidh 152
Cdd:cd21882    4 LLGLLECLRWYLTDSAYQRGATGK--TCLHKAALnlnDGVNEAIMLLLE----AAPDSGNPKELvnAPCTDEFYQGQ--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 153 kishlgTPLYLACENQQRACVKKLLESGADV-----------NQGKG---QDSPLHAVARTASEELACLLMDFGADTQAK 218
Cdd:cd21882   75 ------TALHIAIENRNLNLVRLLVENGADVsaratgrffrkSPGNLfyfGELPLSLAACTNQEEIVRLLLENGAQPAAL 148


                 ...
gi 271398185 219 NAE 221
Cdd:cd21882  149 EAQ 151
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 68-96 2.27e-03

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: 34.93  E-value: 2.27e-03
                          10        20
                  ....*....|....*....|....*....
gi 271398185   68 DHVSPLHEACLGGHLSCVKILLKHGAQVN 96
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02946 PHA02946
ankyin-like protein; Provisional
 52-229 2.63e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.50  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  52 LRNLISQGWAVNIITADHVSPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPLFNacVSGSWDCV----NLLLQhgas 127
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY--LSGTDDEVieriNLLVQ---- 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 128 vqpesdlaspiheaarraYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGAD---VNQGKGQDSPLHAVARTASEEL 204
Cdd:PHA02946 129 ------------------YGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEariVDKFGKNHIHRHLMSDNPKAST 190

                        170       180
                 ....*....|....*....|....*
gi 271398185 205 ACLLMDFGADTQAKNAEGKRPVELV 229
Cdd:PHA02946 191 ISWMMKLGISPSKPDHDGNTPLHIV 215
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-128 3.38e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.41  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  38 SPMHEAAIHGHQLSLRNLISQGWAVNIITADHVSPLHEACLggHLSCVKILLKHGAQVNGVTADWHTPLFNA----Cvsg 113
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppC--- 266

                         90
                 ....*....|....*
gi 271398185 114 SWDCVNLLLQHGASV 128
Cdd:PHA02874 267 DIDIIDILLYHKADI 281
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 34-106 4.01e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 37.66  E-value: 4.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 271398185  34 VSDWSPMHEAAIHGHQLSLRNLISQGWAVNIITADHV-SPLHEACLGGHLSCVKILLKHGAQVNGVTADWHTPL 106
Cdd:PHA02884  68 NSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPI 141
PHA03095 PHA03095
ankyrin-like protein; Provisional
 161-228 4.39e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.08  E-value: 4.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 271398185 161 LYLACENQQRAC---VKKLLESGADVNQGKGQDS-PLHAVARTASEELA---CLLMDFGADTQAKNAEGKRPVEL 228
Cdd:PHA03095  15 LYDYLLNASNVTveeVRRLLAAGADVNFRGEYGKtPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHL 89
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 103-196 4.67e-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: 37.94  E-value: 4.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 103 HTPLFNACVSGSWDCVNLLLQHGASVQPESDlaspihEAARRAYGGNIDHKISHlgtPLYLACENQQRACVKKLLESGAD 182
Cdd:cd21882   74 QTALHIAIENRNLNLVRLLVENGADVSARAT------GRFFRKSPGNLFYFGEL---PLSLAACTNQEEIVRLLLENGAQ 144

                         90
                 ....*....|....*...
gi 271398185 183 VNQGKGQDS----PLHAV 196
Cdd:cd21882  145 PAALEAQDSlgntVLHAL 162
PHA02798 PHA02798
ankyrin-like protein; Provisional
 85-185 5.08e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.89  E-value: 5.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185  85 VKILLKHGAQVNGVTADWHTPLfnaCV--------SGSWDCVNLLLQHGASV-QPESDLASPIHEAARRAYGGN------ 149
Cdd:PHA02798  54 VKLFINLGANVNGLDNEYSTPL---CTilsnikdyKHMLDIVKILIENGADInKKNSDGETPLYCLLSNGYINNleillf 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 271398185 150 -IDH--------KISHLGTPLYLACENQ-QRACVKKLLESGADVNQ 185
Cdd:PHA02798 131 mIENgadttlldKDGFTMLQVYLQSNHHiDIEIIKLLLEKGVDINT 176
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 101-128 5.33e-03

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: 33.72  E-value: 5.33e-03
                           10        20
                   ....*....|....*....|....*...
gi 271398185   101 DWHTPLFNACVSGSWDCVNLLLQHGASV 128
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 66-129 5.70e-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: 37.75  E-value: 5.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 271398185   66 TADHvSPLHEACLGGHLSCVKILLKHGAQVN------------GVTADWHT--PL-FNACVsGSWDCVNLLLQHGASVQ 129
Cdd:TIGR00870 126 TPGI-TALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFYHGesPLnAAACL-GSPSIVALLSEDPADIL 202
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 159-184 7.77e-03

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: 33.38  E-value: 7.77e-03
                          10        20
                  ....*....|....*....|....*.
gi 271398185  159 TPLYLACENQQRACVKKLLESGADVN 184
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
159-208 7.91e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 33.79  E-value: 7.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 271398185  159 TPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLL 208
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINaVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 159-226 8.57e-03

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: 37.30  E-value: 8.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 271398185 159 TPLYLACENQQRACVKKLLESGADVNQG--------KGQDS-------PLHAVARTASEELACLLMDFGADTQAKNAEGK 223
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGADVVSPratgtffrPGPKNliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170


                 ...
gi 271398185 224 RPV 226
Cdd:cd22192  171 TVL 173
 
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.
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