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Conserved domains on  [gi|1616589496|ref|NP_001356629|]
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NF-kappa-B inhibitor beta isoform 4 [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];
56-206 1.29e-22

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  56 EDGDTALHLAVIHQHEPFLDFLLgfSAGTEymdlqndlgqeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLR 135
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLL--EAGAD----------------------VNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616589496 136 DAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 206
Cdd:COG0666   174 EAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-206 1.29e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  56 EDGDTALHLAVIHQHEPFLDFLLgfSAGTEymdlqndlgqeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLR 135
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLL--EAGAD----------------------VNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616589496 136 DAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 206
Cdd:COG0666   174 EAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
PHA03095 PHA03095
ankyrin-like protein; Provisional
 111-206 1.79e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 111 ENYEGH---TPLHVAV---IHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVE-AQAADVLELLLRAGANPAARMYGGR 183
Cdd:PHA03095   40 VNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGR 118

                          90       100
                  ....*....|....*....|....*.
gi 1616589496 184 TPLgSAMLRP---NPILARLLRAHGA 206
Cdd:PHA03095  119 TPL-HVYLSGfniNPKVIRLLLRKGA 143
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 58-198 5.07e-12

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: 65.42  E-value: 5.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  58 GDTALHLAVIHQHepfldfllgFSAGTEYMDLQNDLgqeeeeseedWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDA 137
Cdd:cd22192    51 GETALHVAALYDN---------LEAAVVLMEAAPEL----------VNEPMTSDLYQGETALHIAVVNQNLNLVRELIAR 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616589496 138 GADLDKPEPT-------------CGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILA 198
Cdd:cd22192   112 GADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFA 185
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-178 6.37e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 6.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  62 LHLAVIHQHEPFLDFLLGFSAGTEYMDLqndlgqeeeeseedwklqleaenyEGHTPLHVAVIHKDVEMVRLLRDaGADL 141
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK------------------------NGRTALHLAAKNGHLEIVKLLLE-HADV 55

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1616589496 142 DkpEPTCGRSPLHLAVEAQAADVLELLLRAGANPAAR 178
Cdd:pfam12796  56 N--LKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 58-178 6.32e-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: 53.16  E-value: 6.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  58 GDTALHLAVIHQHEpfldfllGFSAGTEYMdLQNDLGQEEEESEEDWKLqleAENYEGHTPLHVAVIHKDVEMVRLLRDA 137
Cdd:TIGR00870  82 GDTLLHAISLEYVD-------AVEAILLHL-LAAFRKSGPLELANDQYT---SEFTPGITALHLAAHRQNYEIVKLLLER 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1616589496 138 GADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAAR 178
Cdd:TIGR00870 151 GASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILTA 204
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 114-143 2.73e-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: 42.96  E-value: 2.73e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1616589496  114 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 143
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-206 1.29e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  56 EDGDTALHLAVIHQHEPFLDFLLgfSAGTEymdlqndlgqeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLR 135
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLL--EAGAD----------------------VNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616589496 136 DAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 206
Cdd:COG0666   174 EAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-206 4.26e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.71  E-value: 4.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  53 YVTEDGDTALHLAVIHQHEPFLDFLLgfSAGTEymdlqndlgqeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVR 132
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLL--EAGAD----------------------VNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616589496 133 LLRDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 206
Cdd:COG0666   138 LLLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
57-215 6.96e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 6.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  57 DGDTALHLAVIHQHEPFLDFLLGFSAgteymdlqndlgqeeeeseedwklQLEAENYEGHTPLHVAVIHKDVEMVRLLRD 136
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGA------------------------DVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616589496 137 AGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGAPEPEGEDEK 215
Cdd:COG0666   208 AGADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
 111-206 1.79e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 111 ENYEGH---TPLHVAV---IHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVE-AQAADVLELLLRAGANPAARMYGGR 183
Cdd:PHA03095   40 VNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGR 118

                          90       100
                  ....*....|....*....|....*.
gi 1616589496 184 TPLgSAMLRP---NPILARLLRAHGA 206
Cdd:PHA03095  119 TPL-HVYLSGfniNPKVIRLLLRKGA 143
PHA03095 PHA03095
ankyrin-like protein; Provisional
 115-206 4.41e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 4.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 115 GHTPLHVAVIHKDVE-MVRLLRDAGADLDKpEPTCGRSPLH--LAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAML 191
Cdd:PHA03095   83 GFTPLHLYLYNATTLdVIKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLK 161

                          90
                  ....*....|....*..
gi 1616589496 192 RPN--PILARLLRAHGA 206
Cdd:PHA03095  162 SRNanVELLRLLIDAGA 178
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 58-198 5.07e-12

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: 65.42  E-value: 5.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  58 GDTALHLAVIHQHepfldfllgFSAGTEYMDLQNDLgqeeeeseedWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDA 137
Cdd:cd22192    51 GETALHVAALYDN---------LEAAVVLMEAAPEL----------VNEPMTSDLYQGETALHIAVVNQNLNLVRELIAR 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616589496 138 GADLDKPEPT-------------CGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILA 198
Cdd:cd22192   112 GADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFA 185
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-206 1.91e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.05  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  62 LHLAVIHQHEPFLDFLLGFSAGTEYMDLQNDLGQEEEESEEDWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADL 141
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616589496 142 DKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 206
Cdd:COG0666    81 NAKDDG-GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-178 6.37e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 6.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  62 LHLAVIHQHEPFLDFLLGFSAGTEYMDLqndlgqeeeeseedwklqleaenyEGHTPLHVAVIHKDVEMVRLLRDaGADL 141
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK------------------------NGRTALHLAAKNGHLEIVKLLLE-HADV 55

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1616589496 142 DkpEPTCGRSPLHLAVEAQAADVLELLLRAGANPAAR 178
Cdd:pfam12796  56 N--LKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 56-206 1.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  56 EDGDTALHLAVIHQHEPFLDFLLGFSAGTEymdlqndlgqeeeeseedwklqleAENYEGHTPLHVAVIHKDVEMVRLLR 135
Cdd:PHA02875  100 KDGMTPLHLATILKKLDIMKLLIARGADPD------------------------IPNTDKFSPLHLAVMMGDIKGIELLI 155

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1616589496 136 DAGADLDKpEPTCGRSPLHLAVEAQAADVLELLLRAGANPAarmYGGRTPLGSAMLRP----NPILARLLRAHGA 206
Cdd:PHA02875  156 DHKACLDI-EDCCGCTPLIIAMAKGDIAICKMLLDSGANID---YFGKNGCVAALCYAiennKIDIVRLFIKRGA 226
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 112-206 4.28e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.29  E-value: 4.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 112 NYEGHTPLHVAV--IHKDVEMVRLLRDAGAD----------LDKPEPT-----CGRSPLHLAVEAQAADVLELLLRAGAN 174
Cdd:PHA03100  138 NSDGENLLHLYLesNKIDLKILKLLIDKGVDinaknrvnylLSYGVPInikdvYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1616589496 175 PAARMYGGRTPLGSAMLRPNPILARLLRAHGA 206
Cdd:PHA03100  218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 62-192 1.64e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  62 LHLAVIHQHEPFLDFLLGFSAGTEYMDLQndlgqeeeeseedwklqleaenyeGHTPLHVAVIH-KDVEMVRLLRDAGAD 140
Cdd:PHA02878  205 LHHAVKHYNKPIVHILLENGASTDARDKC------------------------GNTPLHISVGYcKDYDILKLLLEHGVD 260

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1616589496 141 LDKPEPTCGRSPLHLAVEAQaaDVLELLLRAGANPAARMYGGRTPLGSAMLR 192
Cdd:PHA02878  261 VNAKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-142 3.64e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.81  E-value: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  52 GYVTEDGDTALHLAVIHQHEPFLDFLLgfsagtEYMDLQNDLgqeeeeseedwklqleaenyEGHTPLHVAVIHKDVEMV 131
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLL------EHADVNLKD--------------------NGRTALHYAARSGHLEIV 77

                          90
                  ....*....|.
gi 1616589496 132 RLLRDAGADLD 142
Cdd:pfam12796  78 KLLLEKGADIN 88
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 115-206 1.32e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 115 GHTPLHVAVIHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPN 194
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANVNIPD-KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCK 246

                          90
                  ....*....|...
gi 1616589496 195 PI-LARLLRAHGA 206
Cdd:PHA02878  247 DYdILKLLLEHGV 259
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 56-194 2.09e-08

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: 54.50  E-value: 2.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  56 EDGDTALHLAVIHQHEPFLDfllgfsAGTEYMDLQNDLGQEEEESeedwKLQLEAENYEGHTPLHVAVIHKDVEMVRLLR 135
Cdd:cd21882    24 ATGKTCLHKAALNLNDGVNE------AIMLLLEAAPDSGNPKELV----NAPCTDEFYQGQTALHIAIENRNLNLVRLLV 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1616589496 136 DAGADLD---------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAARMYG---GRTPLGSAMLRPN 194
Cdd:cd21882    94 ENGADVSaratgrffrKSPGNLfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALVLQAD 167
PHA03095 PHA03095
ankyrin-like protein; Provisional
 108-189 3.40e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 3.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 108 LEAENYEGHTPLHVAVIHK--DVEMVRLLRDAGADL---DkpepTCGRSPLH-LAVEAQA-ADVLELLLRAGANPAARMY 180
Cdd:PHA03095  145 VNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVyavD----DRFRSLLHhHLQSFKPrARIVRELIRAGCDPAATDM 220


                  ....*....
gi 1616589496 181 GGRTPLGSA 189
Cdd:PHA03095  221 LGNTPLHSM 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
115-169 5.51e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 5.51e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1616589496 115 GHTPLHVAVIHKDVEMVRLLRDAGADLDKPePTCGRSPLHLAVEAQAADVLELLL 169
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 58-178 6.32e-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: 53.16  E-value: 6.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  58 GDTALHLAVIHQHEpfldfllGFSAGTEYMdLQNDLGQEEEESEEDWKLqleAENYEGHTPLHVAVIHKDVEMVRLLRDA 137
Cdd:TIGR00870  82 GDTLLHAISLEYVD-------AVEAILLHL-LAAFRKSGPLELANDQYT---SEFTPGITALHLAAHRQNYEIVKLLLER 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1616589496 138 GADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAAR 178
Cdd:TIGR00870 151 GASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILTA 204
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 112-186 2.12e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 112 NYEGHTPLHVAVIHKDVEMVRLLRDAGAD---LDKPeptcGRSPLHLAVEAQAADVLELLLR-------AGANPAARMYG 181
Cdd:PTZ00322  112 DYDGRTPLHIACANGHVQVVRVLLEFGADptlLDKD----GKTPLELAEENGFREVVQLLSRhsqchfeLGANAKPDSFT 187


                  ....*
gi 1616589496 182 GRTPL 186
Cdd:PTZ00322  188 GKPPS 192
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 111-206 6.97e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 6.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 111 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTCgRSPLHLAVEAQAADVLELLLRAGANPAARMY-GGRTPLGSA 189
Cdd:PHA02875   31 EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLA 109

                          90
                  ....*....|....*..
gi 1616589496 190 MLRPNPILARLLRAHGA 206
Cdd:PHA02875  110 TILKKLDIMKLLIARGA 126
PHA03095 PHA03095
ankyrin-like protein; Provisional
 110-208 2.19e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.10  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 110 AENYEGHTPLHVAVIH---KDVEMVRLLrDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPL 186
Cdd:PHA03095  217 ATDMLGNTPLHSMATGsscKRSLVLPLL-IAGISINARNRY-GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294

                          90       100
                  ....*....|....*....|...
gi 1616589496 187 GSAMLRPNP-ILARLLRAHGAPE 208
Cdd:PHA03095  295 SLMVRNNNGrAVRAALAKNPSAE 317
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 114-143 2.73e-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: 42.96  E-value: 2.73e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1616589496  114 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 143
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 127-202 4.03e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 4.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616589496 127 DVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAML-RPNPILARLLR 202
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKhYNKPIVHILLE 222
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 108-217 5.91e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 5.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 108 LEAENYEGHTPLHVAVIHK-DVEMVRLLRDAGADLDKPEpTCGRSPLHLAVEA-QAADVLELLLRAGANPAARMYGGRTP 185
Cdd:PHA02876  300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD-RLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTP 378

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1616589496 186 LGSAMLRPNPILARLLRAHGApEPEGEDEKSG 217
Cdd:PHA02876  379 IHYAAVRNNVVIINTLLDYGA-DIEALSQKIG 409
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-186 7.12e-06

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 46.49  E-value: 7.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  54 VTEDGDTALHLAVIHQHEPFLDFLLGFSAgteymdlqndlgqeeeeseedwklQLEAENYEGHTPLHVAVIHKDVEMVRL 133
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGA------------------------DVNAKDNDGKTALDLAAENGNLEIVKL 237

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1616589496 134 LRDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPL 186
Cdd:COG0666   238 LLEAGADLNAKDKD-GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 103-189 1.02e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 103 DWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKpEPTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGG 182
Cdd:PHA02874  112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190


                  ....*..
gi 1616589496 183 RTPLGSA 189
Cdd:PHA02874  191 ESPLHNA 197
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 111-177 4.83e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 44.46  E-value: 4.83e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616589496 111 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADL---------DKPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAA 177
Cdd:cd22197    90 EYYRGHSALHIAIEKRSLQCVKLLVENGADVharacgrffQKKQGTCfyfGELPLSLAACTKQWDVVNYLLENPHQPAS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 111-191 7.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 111 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAM 190
Cdd:PHA02874  153 EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN-GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231


                  .
gi 1616589496 191 L 191
Cdd:PHA02874  232 I 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 149-175 1.03e-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: 38.72  E-value: 1.03e-04
                           10        20
                   ....*....|....*....|....*..
gi 1616589496  149 GRSPLHLAVEAQAADVLELLLRAGANP 175
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 115-174 1.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 1.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1616589496 115 GHTPLHVAVIHKDVEMVRLLRDAGADLDkpepTC---GRSPLHLAVEAQAADVLELLLRAGAN 174
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPN----LVnkyGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 114-142 1.21e-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: 38.42  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1616589496 114 EGHTPLHVAVIH-KDVEMVRLLRDAGADLD 142
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 112-206 2.02e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.63  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 112 NYEGHTPLHVAV---IHKDVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQAADVLELLLR-AGANPAARMYGGRTPLG 187
Cdd:PHA02736   52 NRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNqPGVNMEILNYAFKTPYY 131

                          90
                  ....*....|....*....
gi 1616589496 188 SAMLRPNPILARLLRAHGA 206
Cdd:PHA02736  132 VACERHDAKMMNILRAKGA 150
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 109-177 2.22e-04

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: 42.44  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 109 EAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANP 175
Cdd:cd22194   135 TEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEGfyfGETPLALAACTNQPEIVQLLMEKESTD 214


                  ..
gi 1616589496 176 AA 177
Cdd:cd22194   215 IT 216
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 114-143 3.74e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 3.74e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1616589496 114 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 143
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
108-156 6.49e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 6.49e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1616589496 108 LEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPtCGRSPLHLA 156
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 149-178 6.78e-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: 36.50  E-value: 6.78e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1616589496 149 GRSPLHLAV-EAQAADVLELLLRAGANPAAR 178
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 111-176 1.66e-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: 39.39  E-value: 1.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1616589496 111 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPA 176
Cdd:cd22193    72 EYYEGQTALHIAIERRQGDIVALLVENGADVHahakgrffqpKYQGEGfyfGELPLSLAACTNQPDIVQYLLENEHQPA 150
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 148-177 2.15e-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: 2.15e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1616589496 148 CGRSPLHLAVEAQAADVLELLLRAGANPAA 177
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
58-134 2.28e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 2.28e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1616589496  58 GDTALHLAVIHQHEPFLDFLLGFsagteymdlqndlgqeeeeseedwKLQLEAENYEGHTPLHVAVIHKDVEMVRLL 134
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEK------------------------GADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
133-186 2.36e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 2.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1616589496 133 LLRDAGADLDKPEpTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPL 186
Cdd:pfam13857   1 LLEHGPIDLNRLD-GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 115-201 2.62e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 38.79  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 115 GHTPLHVAVIHKDVEMVRLLRDAG---ADLDkpeptcGRSPLHLAVEAQAA-DVLELLLRAGANPAARMYGGRTPLGSAM 190
Cdd:PHA02874  223 GFTPLHNAIIHNRSAIELLINNASindQDID------GSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAF 296

                          90
                  ....*....|...
gi 1616589496 191 --LRPNPILARLL 201
Cdd:PHA02874  297 kyINKDPVIKDII 309
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 57-155 3.02e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.70  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496  57 DGDTALHLAVIHQHEPFLDFLLGFSAGTEYM---DL------QNDLGQEEEESEEDwkLQLEAENYEGHTPLHVAVIHKD 127
Cdd:PLN03192  590 NGNTALWNAISAKHHKIFRILYHFASISDPHaagDLlctaakRNDLTAMKELLKQG--LNVDSEDHQGATALQVAMAEDH 667

                          90       100
                  ....*....|....*....|....*...
gi 1616589496 128 VEMVRLLRDAGADLDKPEPTCGRSPLHL 155
Cdd:PLN03192  668 VDMVRLLIMNGADVDKANTDDDFSPTEL 695
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 75-145 6.20e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 36.72  E-value: 6.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1616589496  75 DFLLGFSAGTEYMDLQNDLGQeeeeseeDWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPE 145
Cdd:PHA02743   95 NTLLHIAASTKNYELAEWLCR-------QLGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGAVCDDPL 158
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 112-217 7.55e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 36.33  E-value: 7.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616589496 112 NYEGHTPLHVAVIH---KDVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQAADVLELLLRA-GANPAARMYGGRTPLG 187
Cdd:PHA02743   54 DHHGRQCTHMVAWYdraNAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYH 133

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1616589496 188 SAMLRPNPILARLLRAHGA--PEPEGEDEKSG 217
Cdd:PHA02743  134 IAYKMRDRRMMEILRANGAvcDDPLSIGLSDE 165
 
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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