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Conserved domains on  [gi|21361135|ref|NP_002494|]
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NF-kappa-B inhibitor beta isoform 1 [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];
56-298 2.68e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.19  E-value: 2.68e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  56 EDGDTALHLAVIHQHEPFLDFLLgfsAGTEYMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLAC 135
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLL---AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 136 RVGAHACARALLqprprrpreapdtylAQGPDrtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAV 215
Cdd:COG0666 129 YNGNLEIVKLLL---------------EAGAD--------------------------------VNAQDNDGNTPLHLAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 216 IHKDVEMVRLLRDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRA 295
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240


                ...
gi 21361135 296 HGA 298
Cdd:COG0666 241 AGA 243
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-298 2.68e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.19  E-value: 2.68e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  56 EDGDTALHLAVIHQHEPFLDFLLgfsAGTEYMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLAC 135
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLL---AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 136 RVGAHACARALLqprprrpreapdtylAQGPDrtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAV 215
Cdd:COG0666 129 YNGNLEIVKLLL---------------EAGAD--------------------------------VNAQDNDGNTPLHLAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 216 IHKDVEMVRLLRDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRA 295
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240


                ...
gi 21361135 296 HGA 298
Cdd:COG0666 241 AGA 243
PHA03095 PHA03095
ankyrin-like protein; Provisional
 203-298 1.20e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  203 ENYEGH---TPLHVAV---IHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVE-AQAADVLELLLRAGANPAARMYGGR 275
Cdd:PHA03095  40 VNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGR 118

                         90       100
                 ....*....|....*....|....*.
gi 21361135  276 TPLgSAMLRP---NPILARLLRAHGA 298
Cdd:PHA03095 119 TPL-HVYLSGfniNPKVIRLLLRKGA 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-148 4.47e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 4.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135    62 LHLAVIHQHEPFLDFLLGFSAGteyMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAErrGHTALHLACRVGAHA 141
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75


                  ....*..
gi 21361135   142 CARALLQ 148
Cdd:pfam12796  76 IVKLLLE 82
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 205-290 1.55e-10

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: 62.34  E-value: 1.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 205 YEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPT-------------CGRSPLHLAVEAQAADVLELLLRAGANPAARM 271
Cdd:cd22192  87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                        90
                ....*....|....*....
gi 21361135 272 YGGRTPLGSAMLRPNPILA 290
Cdd:cd22192 167 SLGNTVLHILVLQPNKTFA 185
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 203-270 4.85e-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: 51.62  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135   203 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAA 269
Cdd:TIGR00870 124 EFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILT 203


                  .
gi 21361135   270 R 270
Cdd:TIGR00870 204 A 204
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 206-235 6.95e-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: 42.19  E-value: 6.95e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 21361135    206 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 235
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-298 2.68e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.19  E-value: 2.68e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  56 EDGDTALHLAVIHQHEPFLDFLLgfsAGTEYMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLAC 135
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLL---AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 136 RVGAHACARALLqprprrpreapdtylAQGPDrtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAV 215
Cdd:COG0666 129 YNGNLEIVKLLL---------------EAGAD--------------------------------VNAQDNDGNTPLHLAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 216 IHKDVEMVRLLRDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRA 295
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240


                ...
gi 21361135 296 HGA 298
Cdd:COG0666 241 AGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-307 1.29e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 1.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  53 YVTEDGDTALHLAVIHQHEPFLDFLLgfSAGTEyMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALH 132
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLL--EAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 133 LACRVGAHACARALLqprprrpreapdtylAQGPDrtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLH 212
Cdd:COG0666 159 LAAANGNLEIVKLLL---------------EAGAD--------------------------------VNARDNDGETPLH 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 213 VAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARL 292
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                       250
                ....*....|....*
gi 21361135 293 LRAHGAPEPEGEDEK 307
Cdd:COG0666 271 LLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
87-298 5.37e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.55  E-value: 5.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  87 MDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLqprprrpreapdtylAQGP 166
Cdd:COG0666  47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL---------------EAGA 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 167 DrtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLH 246
Cdd:COG0666 112 D--------------------------------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLH 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 21361135 247 LAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 298
Cdd:COG0666 159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-278 4.68e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.61  E-value: 4.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  56 EDGDTALHLAVIHQHEPFLDFLLgfSAGTEyMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLAC 135
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLL--EAGAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 136 RVGAHACARALlqprprrpreapdtyLAQGPDrtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAV 215
Cdd:COG0666 195 ENGHLEIVKLL---------------LEAGAD--------------------------------VNAKDNDGKTALDLAA 227

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361135 216 IHKDVEMVRLLRDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPL 278
Cdd:COG0666 228 ENGNLEIVKLLLEAGADLNAKDKD-GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 203-298 1.20e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  203 ENYEGH---TPLHVAV---IHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVE-AQAADVLELLLRAGANPAARMYGGR 275
Cdd:PHA03095  40 VNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGR 118

                         90       100
                 ....*....|....*....|....*.
gi 21361135  276 TPLgSAMLRP---NPILARLLRAHGA 298
Cdd:PHA03095 119 TPL-HVYLSGfniNPKVIRLLLRKGA 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-148 4.47e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 4.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135    62 LHLAVIHQHEPFLDFLLGFSAGteyMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAErrGHTALHLACRVGAHA 141
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75


                  ....*..
gi 21361135   142 CARALLQ 148
Cdd:pfam12796  76 IVKLLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
98-234 1.13e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135    98 LHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLQprprrpreapdtylaqgpdrtpdtnhtpv 177
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----------------------------- 51

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 21361135   178 alYPDSDLekeeeeseedwklqleaeNYEGHTPLHVAVIHKDVEMVRLLRDAGADLD 234
Cdd:pfam12796  52 --HADVNL------------------KDNGRTALHYAARSGHLEIVKLLLEKGADIN 88
PHA03095 PHA03095
ankyrin-like protein; Provisional
 207-298 2.31e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 2.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  207 GHTPLHVAVIHKDVE-MVRLLRDAGADLDKpEPTCGRSPLH--LAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAML 283
Cdd:PHA03095  83 GFTPLHLYLYNATTLdVIKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLK 161

                         90
                 ....*....|....*..
gi 21361135  284 RPN--PILARLLRAHGA 298
Cdd:PHA03095 162 SRNanVELLRLLIDAGA 178
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 205-290 1.55e-10

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: 62.34  E-value: 1.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 205 YEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPT-------------CGRSPLHLAVEAQAADVLELLLRAGANPAARM 271
Cdd:cd22192  87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                        90
                ....*....|....*....
gi 21361135 272 YGGRTPLGSAMLRPNPILA 290
Cdd:cd22192 167 SLGNTVLHILVLQPNKTFA 185
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-300 1.65e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135   58 GDTALHLAVIHQH-EPFLDFLLGFSAGTEYmdlQNDLGQTALH--LAAILGETSTVEKLYAAGAGLCVAERRGHTALH-- 132
Cdd:PHA03095  83 GFTPLHLYLYNATtLDVIKLLIKAGADVNA---KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvl 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  133 ------------LACRVGAHACA-----RALLQprprrpreapdtYLAQGPDRTPDTNHTPVALYPDSdlekeeeeseed 195
Cdd:PHA03095 160 lksrnanvellrLLIDAGADVYAvddrfRSLLH------------HHLQSFKPRARIVRELIRAGCDP------------ 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  196 wklqlEAENYEGHTPLHVAVIH---KDVEMVRLLrDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMY 272
Cdd:PHA03095 216 -----AATDMLGNTPLHSMATGsscKRSLVLPLL-IAGISINARNRY-GQTPLHYAAVFNNPRACRRLIALGADINAVSS 288

                        250       260
                 ....*....|....*....|....*....
gi 21361135  273 GGRTPLGSAMLRPNP-ILARLLRAHGAPE 300
Cdd:PHA03095 289 DGNTPLSLMVRNNNGrAVRAALAKNPSAE 317
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 204-298 1.07e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.29  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  204 NYEGHTPLHVAV--IHKDVEMVRLLRDAGAD----------LDKPEPT-----CGRSPLHLAVEAQAADVLELLLRAGAN 266
Cdd:PHA03100 138 NSDGENLLHLYLesNKIDLKILKLLIDKGVDinaknrvnylLSYGVPInikdvYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                         90       100       110
                 ....*....|....*....|....*....|..
gi 21361135  267 PAARMYGGRTPLGSAMLRPNPILARLLRAHGA 298
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 206-298 2.24e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  206 EGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRP 285
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPN-TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90
                 ....*....|...
gi 21361135  286 NPILARLLRAHGA 298
Cdd:PHA02875 180 DIAICKMLLDSGA 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
211-298 3.15e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 3.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135   211 LHVAVIHKDVEMVRLLRDAGADLDKPEPtCGRSPLHLAVEAQAADVLELLLragANPAARMYG-GRTPLGSAMLRPNPIL 289
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLL---EHADVNLKDnGRTALHYAARSGHLEI 76


                  ....*....
gi 21361135   290 ARLLRAHGA 298
Cdd:pfam12796  77 VKLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
206-270 7.91e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 7.91e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361135   206 EGHTPLHVAVIHKDVEMVRLLRDaGADLDkpEPTCGRSPLHLAVEAQAADVLELLLRAGANPAAR 270
Cdd:pfam12796  29 NGRTALHLAAKNGHLEIVKLLLE-HADVN--LKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 207-298 3.05e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  207 GHTPLHVAVIHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPN 286
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPD-KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCK 246

                         90
                 ....*....|...
gi 21361135  287 PI-LARLLRAHGA 298
Cdd:PHA02878 247 DYdILKLLLEHGV 259
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 209-298 3.82e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 3.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  209 TPLHVAVIHKDVEMVRLLRDAGADLDKpEPTCGRSPLHLAVEAQAADVLELLLRAGANPAarmYGGRTPLGSAMLRP--- 285
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDI-EDCCGCTPLIIAMAKGDIAICKMLLDSGANID---YFGKNGCVAALCYAien 212

                         90
                 ....*....|....
gi 21361135  286 -NPILARLLRAHGA 298
Cdd:PHA02875 213 nKIDIVRLFIKRGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-118 4.05e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 4.05e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21361135    52 GYVTEDGDTALHLAVIHQHEPFLDFLLgfsagtEYMDLQN-DLGQTALHLAAILGETSTVEKLYAAGA 118
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLL------EHADVNLkDNGRTALHYAARSGHLEIVKLLLEKGA 85
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-261 2.49e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.49e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 21361135   207 GHTPLHVAVIHKDVEMVRLLRDAGADLDKPePTCGRSPLHLAVEAQAADVLELLL 261
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 201-284 3.05e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  201 EAENYEGHTPLHVAVIH-KDVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQaaDVLELLLRAGANPAARMYGGRTPLG 279
Cdd:PHA02878 228 DARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLS 305


                 ....*
gi 21361135  280 SAMLR 284
Cdd:PHA02878 306 SAVKQ 310
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 203-270 4.85e-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: 51.62  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135   203 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAA 269
Cdd:TIGR00870 124 EFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILT 203


                  .
gi 21361135   270 R 270
Cdd:TIGR00870 204 A 204
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 204-278 6.35e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 6.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  204 NYEGHTPLHVAVIHKDVEMVRLLRDAGAD---LDKPeptcGRSPLHLAVEAQAADVLELLLR-------AGANPAARMYG 273
Cdd:PTZ00322 112 DYDGRTPLHIACANGHVQVVRVLLEFGADptlLDKD----GKTPLELAEENGFREVVQLLSRhsqchfeLGANAKPDSFT 187


                 ....*
gi 21361135  274 GRTPL 278
Cdd:PTZ00322 188 GKPPS 192
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 203-298 1.41e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  203 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTCgRSPLHLAVEAQAADVLELLLRAGANPAARMY-GGRTPLGSA 281
Cdd:PHA02875  31 EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLA 109

                         90
                 ....*....|....*..
gi 21361135  282 MLRPNPILARLLRAHGA 298
Cdd:PHA02875 110 TILKKLDIMKLLIARGA 126
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 57-266 5.69e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135   57 DGDTALHLAVIHQHEPFLDFLLGFSAgteYMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLC-VAERRGHTALHLAC 135
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKHGA---IPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLAT 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  136 RVGAHACARALLQPRPRRprEAPDTylaqgpDRTpDTNHTPVALypdSDLEKEEEESeeDWKLQLEAENYEGHTPLHVAV 215
Cdd:PHA02875 111 ILKKLDIMKLLIARGADP--DIPNT------DKF-SPLHLAVMM---GDIKGIELLI--DHKACLDIEDCCGCTPLIIAM 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21361135  216 IHKDVEMVRLLRDAGADLDkpepTCGRSP----LHLAVEAQAADVLELLLRAGAN 266
Cdd:PHA02875 177 AKGDIAICKMLLDSGANID----YFGKNGcvaaLCYAIENNKIDIVRLFIKRGAD 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 206-235 6.95e-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: 42.19  E-value: 6.95e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 21361135    206 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 235
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 219-294 7.99e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 7.99e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361135  219 DVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAML-RPNPILARLLR 294
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKhYNKPIVHILLE 222
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 203-286 8.85e-06

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: 47.57  E-value: 8.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 203 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD---------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAAR 270
Cdd:cd21882  69 EFYQGQTALHIAIENRNLNLVRLLVENGADVSaratgrffrKSPGNLfyfGELPLSLAACTNQEEIVRLLLENGAQPAAL 148

                        90
                ....*....|....*....
gi 21361135 271 MYG---GRTPLGSAMLRPN 286
Cdd:cd21882 149 EAQdslGNTVLHALVLQAD 167
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 207-298 9.71e-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: 47.31  E-value: 9.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 207 GHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTC----GRSPLHLAVEAQAADVLELLLRAGA--------------NPA 268
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGPK 130

                        90       100       110
                ....*....|....*....|....*....|
gi 21361135 269 ARMYGGRTPLGSAMLRPNPILARLLRAHGA 298
Cdd:cd22192 131 NLIYYGEHPLSFAACVGNEEIVRLLIEHGA 160
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 200-309 1.19e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  200 LEAENYEGHTPLHVAVIHK-DVEMVRLLRDAGADLDKPEpTCGRSPLHLAVEA-QAADVLELLLRAGANPAARMYGGRTP 277
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD-RLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTP 378

                         90       100       110
                 ....*....|....*....|....*....|..
gi 21361135  278 LGSAMLRPNPILARLLRAHGApEPEGEDEKSG 309
Cdd:PHA02876 379 IHYAAVRNNVVIINTLLDYGA-DIEALSQKIG 409
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 173-281 1.23e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  173 NHTPVALYPDSDLEKEEEESEEDWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKpEPTCGRSPLHLAVEAQ 252
Cdd:PHA02874  90 NGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHN 168

                         90       100
                 ....*....|....*....|....*....
gi 21361135  253 AADVLELLLRAGANPAARMYGGRTPLGSA 281
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDNNGESPLHNA 197
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 203-269 9.18e-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: 9.18e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361135 203 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADL---------DKPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAA 269
Cdd:cd22197  90 EYYRGHSALHIAIEKRSLQCVKLLVENGADVharacgrffQKKQGTCfyfGELPLSLAACTKQWDVVNYLLENPHQPAS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 203-283 1.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  203 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAM 282
Cdd:PHA02874 153 EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN-GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231


                 .
gi 21361135  283 L 283
Cdd:PHA02874 232 I 232
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 207-266 2.18e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 2.18e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361135  207 GHTPLHVAVIHKDVEMVRLLRDAGADLDkpepTC---GRSPLHLAVEAQAADVLELLLRAGAN 266
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPN----LVnkyGDTPLHIAILNNNKEIFKLLLNNGPS 250
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 241-267 2.42e-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: 37.95  E-value: 2.42e-04
                           10        20
                   ....*....|....*....|....*..
gi 21361135    241 GRSPLHLAVEAQAADVLELLLRAGANP 267
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 204-298 3.06e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.63  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  204 NYEGHTPLHVAV---IHKDVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQAADVLELLLR-AGANPAARMYGGRTPLG 279
Cdd:PHA02736  52 NRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNqPGVNMEILNYAFKTPYY 131

                         90
                 ....*....|....*....
gi 21361135  280 SAMLRPNPILARLLRAHGA 298
Cdd:PHA02736 132 VACERHDAKMMNILRAKGA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 206-234 3.69e-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: 37.65  E-value: 3.69e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 21361135   206 EGHTPLHVAVIH-KDVEMVRLLRDAGADLD 234
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 201-269 4.08e-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: 42.44  E-value: 4.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135 201 EAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANP 267
Cdd:cd22194 135 TEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEGfyfGETPLALAACTNQPEIVQLLMEKESTD 214


                ..
gi 21361135 268 AA 269
Cdd:cd22194 215 IT 216
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 60-293 5.18e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.87  E-value: 5.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135   60 TALHLAVIHQHEPFLDFLLGFSAGteyMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGA 139
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  140 HACARALLQprprrpreapdtylaqgpdrtpDTNHTPValypdsdlekeeeeseedwklqleaENYEGHTPLHVAVIHKD 219
Cdd:PHA02874 203 YACIKLLID----------------------HGNHIMN-------------------------KCKNGFTPLHNAIIHNR 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135  220 VEMVRLLRDAG---ADLDkpeptcGRSPLHLAVEAQAA-DVLELLLRAGANPAARMYGGRTPLGSAM--LRPNPILARLL 293
Cdd:PHA02874 236 SAIELLINNASindQDID------GSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAFkyINKDPVIKDII 309
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 206-235 8.62e-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: 36.47  E-value: 8.62e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 21361135   206 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 235
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 198-298 1.60e-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: 40.45  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135   198 LQLEAENYEGHTPLHVAV--IHKDVEMV-RLLRDAGADLDKP---------EPTCGRSPLHLAVEAQAADVLELLLRAGA 265
Cdd:TIGR00870  73 LNLSCRGAVGDTLLHAISleYVDAVEAIlLHLLAAFRKSGPLelandqytsEFTPGITALHLAAHRQNYEIVKLLLERGA 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 21361135   266 NPAAR--------------MYGGRTPLGSAMLRPNPILARLLRAHGA 298
Cdd:TIGR00870 153 SVPARacgdffvksqgvdsFYHGESPLNAAACLGSPSIVALLSEDPA 199
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 56-147 1.78e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361135   56 EDGDTALHLAVIHQHEPFLDFLLGFSAGTeymDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLAC 135
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM 176

                         90
                 ....*....|..
gi 21361135  136 RVGAHACARALL 147
Cdd:PHA02875 177 AKGDIAICKMLL 188
Ank_5 pfam13857
Ankyrin repeats (many copies);
200-248 1.79e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 21361135   200 LEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPtCGRSPLHLA 248
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 241-270 2.00e-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: 35.34  E-value: 2.00e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 21361135   241 GRSPLHLAVE-AQAADVLELLLRAGANPAAR 270
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 203-268 2.90e-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: 2.90e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361135 203 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPA 268
Cdd:cd22193  72 EYYEGQTALHIAIERRQGDIVALLVENGADVHahakgrffqpKYQGEGfyfGELPLSLAACTNQPDIVQYLLENEHQPA 150
Ank_4 pfam13637
Ankyrin repeats (many copies);
96-147 3.09e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 3.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 21361135    96 TALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALL 147
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
58-113 3.09e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 3.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 21361135    58 GDTALHLAVIHQHEPFLDFLLGFSAGteyMDLQNDLGQTALHLAAILGETSTVEKL 113
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 240-269 5.01e-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: 34.16  E-value: 5.01e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 21361135   240 CGRSPLHLAVEAQAADVLELLLRAGANPAA 269
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-278 6.26e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 6.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 21361135   225 LLRDAGADLDKPEpTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPL 278
Cdd:pfam13857   1 LLEHGPIDLNRLD-GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
 
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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