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Conserved domains on  [gi|226052096|ref|NP_035037|]
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NF-kappa-B inhibitor alpha [Mus musculus]

Protein Classification

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

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-256 1.25e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.07  E-value: 1.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  34 LDSMKDEEYEQMVKELREIRLQPQEAPLAAEPWKQQLTEDGDSFLHLAIIHEEKPLTMEVIGQVKGDLAFLNFQNNLQQT 113
Cdd:COG0666   10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 114 PLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLtqtctpqhlhsvLQ------ATNYNGHTCL 187
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL------------LEagadvnAQDNDGNTPL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226052096 188 HLASIHGYLAIVEHLVTLGADVNAQEPcNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-256 1.25e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.07  E-value: 1.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  34 LDSMKDEEYEQMVKELREIRLQPQEAPLAAEPWKQQLTEDGDSFLHLAIIHEEKPLTMEVIGQVKGDLAFLNFQNNLQQT 113
Cdd:COG0666   10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 114 PLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLtqtctpqhlhsvLQ------ATNYNGHTCL 187
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL------------LEagadvnAQDNDGNTPL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226052096 188 HLASIHGYLAIVEHLVTLGADVNAQEPcNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-212 1.36e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  115 LHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTQTCTPQHlhsvlqatNYNGHTCLHLASIHG 194
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--------KDNGRTALHYAARSG 72

                          90
                  ....*....|....*...
gi 226052096  195 YLAIVEHLVTLGADVNAQ 212
Cdd:pfam12796  73 HLEIVKLLLEKGADINVK 90
PHA02741 PHA02741
hypothetical protein; Provisional
 140-256 1.45e-14

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 70.46  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 140 RDFRGNTPLHLACEQGCLASVAVLTQTCTPQHLHSVLQATNYNGHTCLHLASI--HGYLA--IVEHLVTLGADVNAQEPC 215
Cdd:PHA02741  17 KNSEGENFFHEAARCGCFDIIARFTPFIRGDCHAAALNATDDAGQMCIHIAAEkhEAQLAaeIIDHLIELGADINAQEML 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 226052096 216 NGRTALHLAVDLQNPDLVSLLL-KCGADVNRVTYQGYSPYQL 256
Cdd:PHA02741  97 EGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFEL 138
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 105-244 1.21e-07

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: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  105 NFQNNLQQTPLHLAVITNQP-GIAEALLKAGCDPELrdfrGNTPLHLACE---QGCLASVAVLTQ----TCTPQHLHSVL 176
Cdd:TIGR00870  46 NCPDRLGRSALFVAAIENENlELTELLLNLSCRGAV----GDTLLHAISLeyvDAVEAILLHLLAafrkSGPLELANDQY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  177 QATNYNGHTCLHLASIHGYLAIVEHLVTLGADVNAQEPCN-------------GRTALHLAVDLQNPDLVSLLLKCGADV 243
Cdd:TIGR00870 122 TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADI 201


                  .
gi 226052096  244 N 244
Cdd:TIGR00870 202 L 202
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 58-203 3.06e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  58 EAP-LAAEPWKQQLTEdGDSFLHLAIIHEEKPLTMEVIG--------QVKGdLAFLNFQNNL---QQTPLHLAVITNQPG 125
Cdd:cd22192   73 AAPeLVNEPMTSDLYQ-GETALHIAVVNQNLNLVRELIArgadvvspRATG-TFFRPGPKNLiyyGEHPLSFAACVGNEE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 126 IAEALLKAGCDPELRDFRGNTPLH---------LACE--QGCLASVAvltqtctPQHLHSVLQATNYNGHTCLHLASIHG 194
Cdd:cd22192  151 IVRLLIEHGADIRAQDSLGNTVLHilvlqpnktFACQmyDLILSYDK-------EDDLQPLDLVPNNQGLTPFKLAAKEG 223


                 ....*....
gi 226052096 195 YLAIVEHLV 203
Cdd:cd22192  224 NIVMFQHLV 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 182-211 1.22e-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: 41.42  E-value: 1.22e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 226052096   182 NGHTCLHLASIHGYLAIVEHLVTLGADVNA 211
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-256 1.25e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.07  E-value: 1.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  34 LDSMKDEEYEQMVKELREIRLQPQEAPLAAEPWKQQLTEDGDSFLHLAIIHEEKPLTMEVIGQVKGDLAFLNFQNNLQQT 113
Cdd:COG0666   10 LLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 114 PLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLtqtctpqhlhsvLQ------ATNYNGHTCL 187
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL------------LEagadvnAQDNDGNTPL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226052096 188 HLASIHGYLAIVEHLVTLGADVNAQEPcNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-253 8.83e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 8.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  18 DGLKKERLVDDRHDSGLDSMKDEEYEQMVKELREIRLQPQEAPLAAEPWKQQLTEDGDSFLHLAIIHEEKPLTMEVIGQv 97
Cdd:COG0666   31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  98 KGDLaflNFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLtqtctpqhlhsvLQ 177
Cdd:COG0666  110 GADV---NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL------------LE 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 178 A------TNYNGHTCLHLASIHGYLAIVEHLVTLGADVNAQEPcNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGY 251
Cdd:COG0666  175 AgadvnaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253


                 ..
gi 226052096 252 SP 253
Cdd:COG0666  254 TA 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-212 1.36e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 1.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  115 LHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTQTCTPQHlhsvlqatNYNGHTCLHLASIHG 194
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--------KDNGRTALHYAARSG 72

                          90
                  ....*....|....*...
gi 226052096  195 YLAIVEHLVTLGADVNAQ 212
Cdd:pfam12796  73 HLEIVKLLLEKGADINVK 90
PHA02741 PHA02741
hypothetical protein; Provisional
 140-256 1.45e-14

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 70.46  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 140 RDFRGNTPLHLACEQGCLASVAVLTQTCTPQHLHSVLQATNYNGHTCLHLASI--HGYLA--IVEHLVTLGADVNAQEPC 215
Cdd:PHA02741  17 KNSEGENFFHEAARCGCFDIIARFTPFIRGDCHAAALNATDDAGQMCIHIAAEkhEAQLAaeIIDHLIELGADINAQEML 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 226052096 216 NGRTALHLAVDLQNPDLVSLLL-KCGADVNRVTYQGYSPYQL 256
Cdd:PHA02741  97 EGDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFEL 138
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 113-253 1.74e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.55  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 113 TPLHL-----AVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQgCLASVAVLTqtcTPQHLHSVLQATNYNGHTCL 187
Cdd:PHA03100  70 TPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK-KSNSYSIVE---YLLDNGANVNIKNSDGENLL 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 188 HLA--SIHGYLAIVEHLVTLGADVNAQE----------PCN-----GRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQG 250
Cdd:PHA03100 146 HLYleSNKIDLKILKLLIDKGVDINAKNrvnyllsygvPINikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225


                 ...
gi 226052096 251 YSP 253
Cdd:PHA03100 226 DTP 228
PHA03095 PHA03095
ankyrin-like protein; Provisional
 112-238 1.22e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 112 QTPLH--LAVITNQPGIAEALLKAGCDPELRDFRGNTPLH-LACEQGCLASVAVltqtctPQHLHSV-LQATNYNGHTCL 187
Cdd:PHA03095 188 RSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHsMATGSSCKRSLVL------PLLIAGIsINARNRYGQTPL 261

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226052096 188 HLASIHGYLAIVEHLVTLGADVNAQEPCnGRTALHLAVDLQNPDLVSLLLK 238
Cdd:PHA03095 262 HYAAVFNNPRACRRLIALGADINAVSSD-GNTPLSLMVRNNNGRAVRAALA 311
PHA03095 PHA03095
ankyrin-like protein; Provisional
 104-253 4.25e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.20  E-value: 4.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 104 LNFQNNLQQTPLHLAVITNQ--PGIAEALLKAGCDPELRDFRGNTPLHLACE-----QGCLASVAVLTqtCTPQhlhsvl 176
Cdd:PHA03095 145 VNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQsfkprARIVRELIRAG--CDPA------ 216

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226052096 177 qATNYNGHTCLHLASIHGYLA--IVEHLVTLGADVNAQEPcNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA03095 217 -ATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNR-YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 109-253 1.05e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.29  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 109 NLQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTQTctpqhlHSVLQATNYNGHTCLH 188
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEN------GASTDARDKCGNTPLH 239

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226052096 189 LASihGYL---AIVEHLVTLGADVNAQEPCNGRTALHLAvdLQNPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA02878 240 ISV--GYCkdyDILKLLLEHGVDVNAKSYILGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTP 303
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 113-247 5.29e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.09  E-value: 5.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 113 TPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTqtctpQHlHSVLQATNYNGHTCLHLASI 192
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI-----DH-KACLDIEDCCGCTPLIIAMA 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226052096 193 HGYLAIVEHLVTLGADVN--AQEPCngRTALHLAVDLQNPDLVSLLLKCGADVNRVT 247
Cdd:PHA02875 178 KGDIAICKMLLDSGANIDyfGKNGC--VAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 104-253 2.95e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.75  E-value: 2.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 104 LNFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTQTctpqhlHSVLQATNYNG 183
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK------GAYANVKDNNG 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226052096 184 HTCLHLASIHGYLAIVEHLVTLGADVNAQepCN-GRTALHLAVdLQNPDLVSLLLKcGADVNRVTYQGYSP 253
Cdd:PHA02874 191 ESPLHNAAEYGDYACIKLLIDHGNHIMNK--CKnGFTPLHNAI-IHNRSAIELLIN-NASINDQDIDGSTP 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 75-253 5.30e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.04  E-value: 5.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  75 DSFLHLAIIHEE---------KPLTMEVIGQVKGDLAFLNFQNNLQQTPLHLAVITNQP---GIAEALLKAGCDPELRDF 142
Cdd:PHA03095   2 EEDESVDIIMEAalydyllnaSNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 143 RGNTPLHLaceqgCLasvavltqtctpqhlhsvlqatnYNGHTclhlasihgyLAIVEHLVTLGADVNAQEPCnGRTALH 222
Cdd:PHA03095  82 CGFTPLHL-----YL-----------------------YNATT----------LDVIKLLIKAGADVNAKDKV-GRTPLH 122

                        170       180       190
                 ....*....|....*....|....*....|...
gi 226052096 223 --LAVDLQNPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA03095 123 vyLSGFNINPKVIRLLLRKGADVNALDLYGMTP 155
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 76-253 6.57e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.59  E-value: 6.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  76 SFLHLAIiheeKPLTMEVIGQVKGDLAFLNFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQG 155
Cdd:PHA02874 126 TFLHYAI----KKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 156 CLASVAVLTqtctpQHLHSVLQATNyNGHTCLHLASIHGYLAIveHLVTLGADVNAQEpCNGRTALHLAvdLQNP---DL 232
Cdd:PHA02874 202 DYACIKLLI-----DHGNHIMNKCK-NGFTPLHNAIIHNRSAI--ELLINNASINDQD-IDGSTPLHHA--INPPcdiDI 270

                        170       180
                 ....*....|....*....|.
gi 226052096 233 VSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA02874 271 IDILLYHKADISIKDNKGENP 291
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 118-256 9.05e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.50  E-value: 9.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 118 AVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTQTCTPQH------------------------LH 173
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHirdangntalwnaisakhhkifriLY 611

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 174 SVLQATN-YNGHTCLHLASIHGYLAIVEHLVTLGADVNAQEPcNGRTALHLAVDLQNPDLVSLLLKCGADVNRV-TYQGY 251
Cdd:PLN03192 612 HFASISDpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDH-QGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDF 690


                 ....*
gi 226052096 252 SPYQL 256
Cdd:PLN03192 691 SPTEL 695
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 140-265 1.36e-09

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 56.04  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 140 RDFRGNTPLHLACEQGCLASVAVLTQTCTPQHLHSVLQaTNYNGHTCLHLASIHGYLAIVEHLVTL---GADVNAQEPCN 216
Cdd:PHA02736  13 PDIEGENILHYLCRNGGVTDLLAFKNAISDENRYLVLE-YNRHGKQCVHIVSNPDKADPQEKLKLLmewGADINGKERVF 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226052096 217 GRTALHLAVDLQNPDLVSLLL-KCGADVNRVTYQGYSPYQLTWGRPSTRI 265
Cdd:PHA02736  92 GNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKM 141
Ank_5 pfam13857
Ankyrin repeats (many copies);
104-151 2.14e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 2.14e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 226052096  104 LNFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLA 151
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 114-244 2.75e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 2.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 114 PLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLAC----EQGCLASVAVLTQTCTPQHLHSVLQATNYNGHTCLHL 189
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFKI 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226052096 190 ASIHGY---------------------LAIVEHLVTLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVN 244
Cdd:PHA02878 120 ILTNRYkniqtidlvyidkkskddiieAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVN 195
PHA03095 PHA03095
ankyrin-like protein; Provisional
 26-151 4.76e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 4.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  26 VDDRHDSGLDSMKD--EEYEQMVKELREIRLQPQEAPLAaepwkqqltedGDSFLHLAIIHEEKPLTmeVIGQVKGDLAF 103
Cdd:PHA03095 183 VDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDML-----------GNTPLHSMATGSSCKRS--LVLPLLIAGIS 249

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 226052096 104 LNFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLA 151
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 118-256 1.01e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 118 AVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTQtctpqhlHSVLQATNYNG-HTCLHLASIHGYL 196
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMK-------HGAIPDVKYPDiESELHDAVEEGDV 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 197 AIVEHLVTLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:PHA02875  82 KAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 105-244 1.21e-07

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: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  105 NFQNNLQQTPLHLAVITNQP-GIAEALLKAGCDPELrdfrGNTPLHLACE---QGCLASVAVLTQ----TCTPQHLHSVL 176
Cdd:TIGR00870  46 NCPDRLGRSALFVAAIENENlELTELLLNLSCRGAV----GDTLLHAISLeyvDAVEAILLHLLAafrkSGPLELANDQY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  177 QATNYNGHTCLHLASIHGYLAIVEHLVTLGADVNAQEPCN-------------GRTALHLAVDLQNPDLVSLLLKCGADV 243
Cdd:TIGR00870 122 TSEFTPGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADI 201


                  .
gi 226052096  244 N 244
Cdd:TIGR00870 202 L 202
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-163 1.27e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096   78 LHLAIIHEEKPLTMEVIGQVKGdlafLNFQNNLQQTPLHLAVITNQPGIAEALLKaGCDPELRDfRGNTPLHLACEQGCL 157
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD----ANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHL 74


                  ....*.
gi 226052096  158 ASVAVL 163
Cdd:pfam12796  75 EIVKLL 80
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 58-203 3.06e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  58 EAP-LAAEPWKQQLTEdGDSFLHLAIIHEEKPLTMEVIG--------QVKGdLAFLNFQNNL---QQTPLHLAVITNQPG 125
Cdd:cd22192   73 AAPeLVNEPMTSDLYQ-GETALHIAVVNQNLNLVRELIArgadvvspRATG-TFFRPGPKNLiyyGEHPLSFAACVGNEE 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 126 IAEALLKAGCDPELRDFRGNTPLH---------LACE--QGCLASVAvltqtctPQHLHSVLQATNYNGHTCLHLASIHG 194
Cdd:cd22192  151 IVRLLIEHGADIRAQDSLGNTVLHilvlqpnktFACQmyDLILSYDK-------EDDLQPLDLVPNNQGLTPFKLAAKEG 223


                 ....*....
gi 226052096 195 YLAIVEHLV 203
Cdd:cd22192  224 NIVMFQHLV 232
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 104-247 7.99e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 7.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 104 LNFQNNLQQTPLHLAVITnqPGIAE---ALLKAGCDPELRDFRGNTPLHLACEQGC-LASVAVLTQtctpqhLHSVLQAT 179
Cdd:PHA02876 266 VNSIDDCKNTPLHHASQA--PSLSRlvpKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIM------LGADVNAA 337

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226052096 180 NYNGHTCLHLAS-IHGYLAIVEHLVTLGADVNAQEPCNgRTALHLAVDLQNPDLVSLLLKCGADVNRVT 247
Cdd:PHA02876 338 DRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCD-KTPIHYAAVRNNVVIINTLLDYGADIEALS 405
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 100-243 1.09e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.01  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 100 DLAFLNFQNNLQQTPLHLAVITNQPGIAEALLK-AGCDPELRDFRGNTPLHLACEQGCLaSVAVLTQTCTPQHLHSVLQA 178
Cdd:cd22192    6 DELHLLQQKRISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNL-EAAVVLMEAAPELVNEPMTS 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226052096 179 TNYNGHTCLHLASIHGYLAIVEHLVTLGADVNAQEPCN-------------GRTALHLAVDLQNPDLVSLLLKCGADV 243
Cdd:cd22192   85 DLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADI 162
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-141 1.47e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 1.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226052096   69 QLTEDGDSFLHLAIIHEEKPLTMEVIGQVKGDLaflnfqNNLQQTPLHLAVITNQPGIAEALLKAGCDPELRD 141
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL------KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_5 pfam13857
Ankyrin repeats (many copies);
170-224 2.31e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 2.31e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226052096  170 QHLHSVLQATNYNGHTCLHLASIHGYLAIVEHLVTLGADVNAQEPCnGRTALHLA 224
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE-GLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-253 2.58e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 102 AFLNFQNNLQQTPLHLAVITNQPGIAEALL--KAGCDPELRDFRGNTPLHLACEQGCLASVavltqtcTPQHLH--SVLQ 177
Cdd:PHA02876 229 AIIDNRSNINKNDLSLLKAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQAPSLSRL-------VPKLLErgADVN 301

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226052096 178 ATNYNGHTCLHLASIHGY-LAIVEHLVTLGADVNAQEPCNgRTALHLAVDL-QNPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA02876 302 AKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLY-ITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTP 378
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-253 3.85e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 3.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 102 AFLNFQNNLQQTPLHLA-VITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTQtctpqhLHSVLQATN 180
Cdd:PHA02876 332 ADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD------YGADIEALS 405

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226052096 181 YNGHTCLHLA--SIHGYLAiVEHLVTLGADVNAQEPcNGRTALHLAVDLQ-NPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA02876 406 QKIGTALHFAlcGTNPYMS-VKTLIDRGANVNSKNK-DLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYP 479
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-244 7.13e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 7.13e-06
                          10        20
                  ....*....|....*....|....*....
gi 226052096  216 NGRTALHLAVDLQNPDLVSLLLKCGADVN 244
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-247 7.22e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.28  E-value: 7.22e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 226052096  216 NGRTALHLAVD-LQNPDLVSLLLKCGADVNRVT 247
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 130-215 9.91e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 9.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 130 LLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTqtctpqHLHSVLQATNYNGHTCLHLASIHGYLAIVEHLVTLGADV 209
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL------DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                 ....*.
gi 226052096 210 NAQEPC 215
Cdd:PHA03100 252 KTIIET 257
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 105-253 1.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 105 NFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTQTCTpqHLHSVLQAtnyNGH 184
Cdd:PHA02875  29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYK---DGM 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 185 TCLHLASIHGYLAIVEHLVTLGADVNAqePCNGRTA-LHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSP 253
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDI--PNTDKFSpLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 112-171 1.14e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 1.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 112 QTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQGCLASVAVLTQTCTPQH 171
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHF 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 182-211 1.22e-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: 41.42  E-value: 1.22e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 226052096   182 NGHTCLHLASIHGYLAIVEHLVTLGADVNA 211
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 104-152 1.23e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.58  E-value: 1.23e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 226052096 104 LNFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLAC 152
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 180-269 1.77e-05

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 44.42  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 180 NYNGHTCLHLASIH---GYLAIVEHLVTLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLK-CGADVNRVTYQGYSPYQ 255
Cdd:PHA02743  54 DHHGRQCTHMVAWYdraNAVMKIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRqLGVNLGAINYQHETAYH 133

                         90
                 ....*....|....
gi 226052096 256 LTWGRPSTRIQQQL 269
Cdd:PHA02743 134 IAYKMRDRRMMEIL 147
Ank_4 pfam13637
Ankyrin repeats (many copies);
183-237 2.81e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 2.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 226052096  183 GHTCLHLASIHGYLAIVEHLVTLGADVNAQePCNGRTALHLAVDLQNPDLVSLLL 237
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 183-247 3.04e-05

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: 45.39  E-value: 3.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226052096 183 GHTCLHLASIHGYLAIVehLVTLGAD---VNaqEPCN-----GRTALHLAVDLQNPDLVSLLLKCGADVN--RVT 247
Cdd:cd22192   51 GETALHVAALYDNLEAA--VVLMEAApelVN--EPMTsdlyqGETALHIAVVNQNLNLVRELIARGADVVspRAT 121
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 216-244 3.26e-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: 40.26  E-value: 3.26e-05
                           10        20
                   ....*....|....*....|....*....
gi 226052096   216 NGRTALHLAVDLQNPDLVSLLLKCGADVN 244
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-212 3.76e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 3.76e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 226052096  182 NGHTCLHLASIH-GYLAIVEHLVTLGADVNAQ 212
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNAR 32
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 76-239 5.03e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 5.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  76 SFLHLAIIHEEkpltmevIGQVKGDLAFLNFQNNLQQTPLHLAVITN--QPGIAEALLKAGCdpelrdfrgntplHLACE 153
Cdd:PTZ00322  33 SFERMAAIQEE-------IARIDTHLEALEATENKDATPDHNLTTEEviDPVVAHMLTVELC-------------QLAAS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 154 QGCLASVAVLTQTCTPQhlhsvlqATNYNGHTCLHLASIHGYLAIVEHLVTLGADVNAQEPcNGRTALHLAVDLQNPDLV 233
Cdd:PTZ00322  93 GDAVGARILLTGGADPN-------CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK-DGKTPLELAEENGFREVV 164


                 ....*.
gi 226052096 234 SLLLKC 239
Cdd:PTZ00322 165 QLLSRH 170
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 165-243 6.10e-05

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: 44.49  E-value: 6.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 165 QTCTPQHLHSVLQATNYNGHTCLHLASIH---GYLAIVEHLVTLGAD-------VNAQ---EPCNGRTALHLAVDLQNPD 231
Cdd:cd21882    8 LECLRWYLTDSAYQRGATGKTCLHKAALNlndGVNEAIMLLLEAAPDsgnpkelVNAPctdEFYQGQTALHIAIENRNLN 87

                         90
                 ....*....|..
gi 226052096 232 LVSLLLKCGADV 243
Cdd:cd21882   88 LVRLLVENGADV 99
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 110-257 7.63e-05

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: 44.23  E-value: 7.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 110 LQQTPLHLAVITNQPGIAEALLKagCDPELRD-------FRGNTPLHLACEQGCLASVAVL------------TQTCTPQ 170
Cdd:cd22192   50 LGETALHVAALYDNLEAAVVLME--AAPELVNepmtsdlYQGETALHIAVVNQNLNLVRELiargadvvspraTGTFFRP 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 171 HLHSVLqatnYNGHTCLHLASIHGYLAIVEHLVTLGADVNAQEpCNGRTALHLAVDLQNPDLV----SLLLKCGADVNRV 246
Cdd:cd22192  128 GPKNLI----YYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD-SLGNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLQ 202

                        170
                 ....*....|....*..
gi 226052096 247 T------YQGYSPYQLT 257
Cdd:cd22192  203 PldlvpnNQGLTPFKLA 219
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 196-252 7.88e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 7.88e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226052096 196 LAIVEHLVTLGADVNAQEpCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYS 252
Cdd:PHA02876 158 LLIAEMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLS 213
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 102-240 1.89e-04

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: 42.86  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 102 AFLNFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPELrdFRGNTPLHLACEQGCLASVAVLTQTCTPQHLHS---VLQA 178
Cdd:cd22193   36 ALLNLNPGTNDTIRILLDIAEKTDNLKRFINAEYTDEY--YEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrFFQP 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 179 TN-----YNGHTCLHLASIHGYLAIVEHLVT---LGADVNAQEPcNGRTALHLAVDL-----QNPDLVS-----LLLKCG 240
Cdd:cd22193  114 KYqgegfYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDS-RGNTVLHALVTVadntkENTKFVTrmydmILIRGA 192
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 74-203 2.08e-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: 42.82  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  74 GDSFLHLAIIHEEKPLTMEVI-------GQVKGDlaFLNFQNNLQ-----QTPLHLAVITNQPGIAEALLKAGCDP-ELR 140
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIakgadvnAHAKGV--FFNPKYKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDiTSQ 218

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226052096 141 DFRGNTPLHlaceqgCLASVAVLTQT---------------CTPQHLHSVlqaTNYNGHTCLHLASIHGYLAIVEHLV 203
Cdd:cd22194  219 DSRGNTVLH------ALVTVAEDSKTqndfvkrmydmillkSENKNLETI---RNNEGLTPLQLAAKMGKAEILKYIL 287
Ank_4 pfam13637
Ankyrin repeats (many copies);
144-203 2.60e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 2.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  144 GNTPLHLACEQGCLASVAVLTQTCTPqhlhsvLQATNYNGHTCLHLASIHGYLAIVEHLV 203
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD------INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 60-203 2.99e-04

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: 42.17  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  60 PLAAEPWKQQLTEdGDSFLHLAIIHEEKPLT-------MEVIGQVKGDlAFLNFQNNL---QQTPLHLAVITNQPGIAEA 129
Cdd:cd21882   60 ELVNAPCTDEFYQ-GQTALHIAIENRNLNLVrllvengADVSARATGR-FFRKSPGNLfyfGELPLSLAACTNQEEIVRL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 130 LLKAGCDP---ELRDFRGNTPLHLACEQG----------CLASVAVLTQTCTPQHLHSVLQATNYNGHTCLHLASIHGYL 196
Cdd:cd21882  138 LLENGAQPaalEAQDSLGNTVLHALVLQAdntpensafvCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKLAAVEGKI 217


                 ....*..
gi 226052096 197 AIVEHLV 203
Cdd:cd21882  218 VMFQHIL 224
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 182-244 4.92e-04

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 41.72  E-value: 4.92e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226052096 182 NGHTCLHLA----------SIHGYLAIVEHLVTLGADVNAQEPCN---GRTALHLAVDLQNPDLVSLLLKCGADVN 244
Cdd:cd22196   46 TGKTCLLKAmlnlhngqndTISLLLDIAEKTGNLKEFVNAAYTDSyykGQTALHIAIERRNMHLVELLVQNGADVH 121
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-243 4.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 4.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 102 AFLNFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLA-CEQGCLASVAVLTQTctpqhlHSVLQATN 180
Cdd:PHA02876 366 ANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDR------GANVNSKN 439

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226052096 181 YNGHTCLHLASIHG-YLAIVEHLVTLGADVNAqepCNGRTALHLAVDLQNPDLVSLLLKCGADV 243
Cdd:PHA02876 440 KDLSTPLHYACKKNcKLDVIEMLLDNGADVNA---INIQNQYPLLIALEYHGIVNILLHYGAEL 500
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 180-237 8.50e-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: 40.90  E-value: 8.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226052096 180 NYNGHTCLHLASIHGYLAIVEHLVTLGADVNAQ------EPCN-------GRTALHLAVDLQNPDLVSLLL 237
Cdd:cd22194  138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffNPKYkhegfyfGETPLALAACTNQPEIVQLLM 208
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 78-257 9.64e-04

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: 40.83  E-value: 9.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096   78 LHLAIIHEEKPLTMEVIGQVKGDLAFlnfqnnlQQTPLHLAVITNQPGIAEALLKAGCDPELR----DFR---------- 143
Cdd:TIGR00870 102 LHLLAAFRKSGPLELANDQYTSEFTP-------GITALHLAAHRQNYEIVKLLLERGASVPARacgdFFVksqgvdsfyh 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096  144 GNTPLHLAceqGCLASVAVLTQTCtpQHLHSVLqATNYNGHTCLHLASIH-------------------GYLAIVEHLVT 204
Cdd:TIGR00870 175 GESPLNAA---ACLGSPSIVALLS--EDPADIL-TADSLGNTLLHLLVMEnefkaeyeelscqmynfalSLLDKLRDSKE 248

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226052096  205 LGADVNAQepcnGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLT 257
Cdd:TIGR00870 249 LEVILNHQ----GLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLS 297
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-211 1.02e-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: 36.08  E-value: 1.02e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 226052096  182 NGHTCLHLASIHGYLAIVEHLVTLGADVNA 211
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 112-141 1.26e-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. 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: 35.73  E-value: 1.26e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 226052096  112 QTPLHLAVI-TNQPGIAEALLKAGCDPELRD 141
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 40-203 1.71e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.06  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096   40 EEYEQMVKELREIRLQPQE----APLAAEPWKQQLTEDgDSFLHLAIIHEE----KPLTME-------------VIGQVK 98
Cdd:TIGR00870  91 LEYVDAVEAILLHLLAAFRksgpLELANDQYTSEFTPG-ITALHLAAHRQNyeivKLLLERgasvparacgdffVKSQGV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096   99 GDLAFlnfqnnlQQTPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLA-------CEQGCLAS------VAVLTQ 165
Cdd:TIGR00870 170 DSFYH-------GESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkAEYEELSCqmynfaLSLLDK 242

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 226052096  166 TCTPQHLHSVLqatNYNGHTCLHLASIHGYLAIVEHLV 203
Cdd:TIGR00870 243 LRDSKELEVIL---NHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 144-249 1.87e-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: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 144 GNTPLHLAC---EQGCLASVAVLTQTCTPQHLHSVL---QATN--YNGHTCLHLASIHGYLAIVEHLVTLGADVNA---- 211
Cdd:cd21882   26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnaPCTDefYQGQTALHIAIENRNLNLVRLLVENGADVSAratg 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 226052096 212 ----QEPCN----GRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQ 249
Cdd:cd21882  106 rffrKSPGNlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQ 151
Ank_5 pfam13857
Ankyrin repeats (many copies);
207-256 2.13e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 2.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 226052096  207 ADVNAQEPCnGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:pfam13857   7 IDLNRLDGE-GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
113-155 2.20e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 2.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 226052096  113 TPLHLAVITNQPGIAEALLKAGCDPELRDFRGNTPLHLACEQG 155
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 184-256 3.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 38.26  E-value: 3.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226052096 184 HTCLHLASIHgyLAIVEHLVTLGADVNAQEPCNGRTALHLAVDLQ---NPDLVSLLLKCGADVNRVTYQGYSPYQL 256
Cdd:PHA02859  56 FSCLEKDKVN--VEILKFLIENGADVNFKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHM 129
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 183-244 5.28e-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: 38.24  E-value: 5.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226052096 183 GHTCLHLA--SIHG--------YLAIVEHLVTLGADVNAQ---EPCNGRTALHLAVDLQNPDLVSLLLKCGADVN 244
Cdd:cd22193   29 GKTCLMKAllNLNPgtndtiriLLDIAEKTDNLKRFINAEytdEYYEGQTALHIAIERRQGDIVALLVENGADVH 103
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 113-139 6.62e-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: 6.62e-03
                           10        20
                   ....*....|....*....|....*..
gi 226052096   113 TPLHLAVITNQPGIAEALLKAGCDPEL 139
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 102-225 6.94e-03

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: 38.20  E-value: 6.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226052096 102 AFLNFQNNLQQTPLHLAVITNQPGIAEALLKAGCDPElrDFRGNTPLHLACEQGCLASVAVLTQTCTPQHLHS---VLQA 178
Cdd:cd22194  101 ALLNINENTKEIVRILLAFAEENGILDRFINAEYTEE--AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvFFNP 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 226052096 179 TN-----YNGHTCLHLASIHGYLAIVEHLVTLGADVNAQEPCNGRTALHLAV 225
Cdd:cd22194  179 KYkhegfYFGETPLALAACTNQPEIVQLLMEKESTDITSQDSRGNTVLHALV 230
 
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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