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Conserved domains on  [gi|2462565531|ref|XP_054177051|]
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NF-kappa-B inhibitor beta isoform X1 [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];
50-266 9.58e-28

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 9.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531  50 AGTEYMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLqprprrpreapdty 129
Cdd:COG0666    75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-------------- 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 130 lAQGPDrtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcG 209
Cdd:COG0666   141 -EAGAD--------------------------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-G 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462565531 210 RSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 266
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-266 9.58e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 9.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531  50 AGTEYMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLqprprrpreapdty 129
Cdd:COG0666    75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-------------- 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 130 lAQGPDrtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcG 209
Cdd:COG0666   141 -EAGAD--------------------------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-G 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462565531 210 RSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 266
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
PHA03095 PHA03095
ankyrin-like protein; Provisional
 171-266 7.87e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 7.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 171 ENYEGH---TPLHVAV---IHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVE-AQAADVLELLLRAGANPAARMYGGR 243
Cdd:PHA03095   40 VNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGR 118

                          90       100
                  ....*....|....*....|....*.
gi 2462565531 244 TPLgSAMLRP---NPILARLLRAHGA 266
Cdd:PHA03095  119 TPL-HVYLSGfniNPKVIRLLLRKGA 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-202 1.16e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531  66 LHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLQprprrpreapdtylaqgpdrtpdtnhtpv 145
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----------------------------- 51

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462565531 146 alYPDSDLekeeeeseedwklqleaeNYEGHTPLHVAVIHKDVEMVRLLRDAGADLD 202
Cdd:pfam12796  52 --HADVNL------------------KDNGRTALHYAARSGHLEIVKLLLEKGADIN 88
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 173-258 1.15e-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: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 173 YEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPT-------------CGRSPLHLAVEAQAADVLELLLRAGANPAARM 239
Cdd:cd22192    87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                          90
                  ....*....|....*....
gi 2462565531 240 YGGRTPLGSAMLRPNPILA 258
Cdd:cd22192   167 SLGNTVLHILVLQPNKTFA 185
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 171-238 3.87e-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: 3.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 171 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAA 237
Cdd:TIGR00870 124 EFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILT 203


                  .
gi 2462565531 238 R 238
Cdd:TIGR00870 204 A 204
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 174-203 3.42e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 3.42e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462565531  174 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 203
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-266 9.58e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 9.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531  50 AGTEYMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLqprprrpreapdty 129
Cdd:COG0666    75 AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-------------- 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 130 lAQGPDrtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcG 209
Cdd:COG0666   141 -EAGAD--------------------------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-G 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462565531 210 RSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 266
Cdd:COG0666   187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-266 4.85e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 4.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531  55 MDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLqprprrpreapdtylAQGP 134
Cdd:COG0666    47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL---------------EAGA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 135 DrtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLH 214
Cdd:COG0666   112 D--------------------------------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLH 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462565531 215 LAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 266
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-275 1.22e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.41  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531  56 DLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLqprprrpreapdtylAQGPD 135
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL---------------EAGAD 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 136 rtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHL 215
Cdd:COG0666   179 --------------------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDL 225

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 216 AVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGAPEPEGEDEK 275
Cdd:COG0666   226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
 171-266 7.87e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.59  E-value: 7.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 171 ENYEGH---TPLHVAV---IHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVE-AQAADVLELLLRAGANPAARMYGGR 243
Cdd:PHA03095   40 VNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGR 118

                          90       100
                  ....*....|....*....|....*.
gi 2462565531 244 TPLgSAMLRP---NPILARLLRAHGA 266
Cdd:PHA03095  119 TPL-HVYLSGfniNPKVIRLLLRKGA 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-202 1.16e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531  66 LHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLQprprrpreapdtylaqgpdrtpdtnhtpv 145
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----------------------------- 51

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462565531 146 alYPDSDLekeeeeseedwklqleaeNYEGHTPLHVAVIHKDVEMVRLLRDAGADLD 202
Cdd:pfam12796  52 --HADVNL------------------KDNGRTALHYAARSGHLEIVKLLLEKGADIN 88
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-246 3.21e-12

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 66.13  E-value: 3.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531  56 DLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALlqprprrpreapdtyLAQGPD 135
Cdd:COG0666   147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL---------------LEAGAD 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 136 rtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHL 215
Cdd:COG0666   212 --------------------------------VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD-GLTALLL 258

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462565531 216 AVEAQAADVLELLLRAGANPAARMYGGRTPL 246
Cdd:COG0666   259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 175-266 1.58e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 1.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 175 GHTPLHVAVIHKDVE-MVRLLRDAGADLDKpEPTCGRSPLH--LAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAML 251
Cdd:PHA03095   83 GFTPLHLYLYNATTLdVIKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLK 161

                          90
                  ....*....|....*..
gi 2462565531 252 RPN--PILARLLRAHGA 266
Cdd:PHA03095  162 SRNanVELLRLLIDAGA 178
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 173-258 1.15e-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: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 173 YEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPT-------------CGRSPLHLAVEAQAADVLELLLRAGANPAARM 239
Cdd:cd22192    87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                          90
                  ....*....|....*....
gi 2462565531 240 YGGRTPLGSAMLRPNPILA 258
Cdd:cd22192   167 SLGNTVLHILVLQPNKTFA 185
Ank_2 pfam12796
Ankyrin repeats (3 copies);
179-266 5.80e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 5.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 179 LHVAVIHKDVEMVRLLRDAGADLDKPEPtCGRSPLHLAVEAQAADVLELLLragANPAARMYG-GRTPLGSAMLRPNPIL 257
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLL---EHADVNLKDnGRTALHYAARSGHLEI 76


                  ....*....
gi 2462565531 258 ARLLRAHGA 266
Cdd:pfam12796  77 VKLLLEKGA 85
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 172-266 8.27e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.29  E-value: 8.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 172 NYEGHTPLHVAV--IHKDVEMVRLLRDAGAD----------LDKPEPT-----CGRSPLHLAVEAQAADVLELLLRAGAN 234
Cdd:PHA03100  138 NSDGENLLHLYLesNKIDLKILKLLIDKGVDinaknrvnylLSYGVPInikdvYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462565531 235 PAARMYGGRTPLGSAMLRPNPILARLLRAHGA 266
Cdd:PHA03100  218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Ank_2 pfam12796
Ankyrin repeats (3 copies);
174-238 1.71e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 1.71e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462565531 174 EGHTPLHVAVIHKDVEMVRLLRDaGADLDkpEPTCGRSPLHLAVEAQAADVLELLLRAGANPAAR 238
Cdd:pfam12796  29 NGRTALHLAAKNGHLEIVKLLLE-HADVN--LKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 174-266 1.75e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 174 EGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRP 253
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPN-TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                          90
                  ....*....|...
gi 2462565531 254 NPILARLLRAHGA 266
Cdd:PHA02875  180 DIAICKMLLDSGA 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
55-116 7.64e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 7.64e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462565531  55 MDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAErrGHTALHLACRVGAHACARALLQ 116
Cdd:pfam12796  23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKLLLE 82
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 175-266 2.41e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 175 GHTPLHVAVIHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPN 254
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANVNIPD-KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCK 246

                          90
                  ....*....|...
gi 2462565531 255 PI-LARLLRAHGA 266
Cdd:PHA02878  247 DYdILKLLLEHGV 259
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 177-266 3.06e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 3.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 177 TPLHVAVIHKDVEMVRLLRDAGADLDKpEPTCGRSPLHLAVEAQAADVLELLLRAGANPAarmYGGRTPLGSAMLRP--- 253
Cdd:PHA02875  137 SPLHLAVMMGDIKGIELLIDHKACLDI-EDCCGCTPLIIAMAKGDIAICKMLLDSGANID---YFGKNGCVAALCYAien 212

                          90
                  ....*....|....
gi 2462565531 254 -NPILARLLRAHGA 266
Cdd:PHA02875  213 nKIDIVRLFIKRGA 226
PHA03095 PHA03095
ankyrin-like protein; Provisional
 168-249 9.16e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 168 LEAENYEGHTPLHVAVIHK--DVEMVRLLRDAGADLDKPEpTCGRSPLH-LAVEAQA-ADVLELLLRAGANPAARMYGGR 243
Cdd:PHA03095  145 VNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVD-DRFRSLLHhHLQSFKPrARIVRELIRAGCDPAATDMLGN 223


                  ....*.
gi 2462565531 244 TPLGSA 249
Cdd:PHA03095  224 TPLHSM 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
175-229 1.14e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 1.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462565531 175 GHTPLHVAVIHKDVEMVRLLRDAGADLDKPePTCGRSPLHLAVEAQAADVLELLL 229
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 169-252 2.46e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 169 EAENYEGHTPLHVAVIH-KDVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQaaDVLELLLRAGANPAARMYGGRTPLG 247
Cdd:PHA02878  228 DARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLS 305


                  ....*
gi 2462565531 248 SAMLR 252
Cdd:PHA02878  306 SAVKQ 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-268 3.38e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531  58 QNDLGQTALH--LAAILGETSTVEKLYAAGAGLCVAERRGHTALH--------------LACRVGAHACA-----RALLQ 116
Cdd:PHA03095  113 KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksrnanvellrLLIDAGADVYAvddrfRSLLH 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 117 prprrpreapdtYLAQGPDRTPDTNHTPVALYPDSdlekeeeeseedwklqlEAENYEGHTPLHVAVIH---KDVEMVRL 193
Cdd:PHA03095  193 ------------HHLQSFKPRARIVRELIRAGCDP-----------------AATDMLGNTPLHSMATGsscKRSLVLPL 243

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462565531 194 LrDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNP-ILARLLRAHGAPE 268
Cdd:PHA03095  244 L-IAGISINARNRY-GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGrAVRAALAKNPSAE 317
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 171-238 3.87e-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: 3.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 171 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAA 237
Cdd:TIGR00870 124 EFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILT 203


                  .
gi 2462565531 238 R 238
Cdd:TIGR00870 204 A 204
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 172-246 8.54e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 8.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 172 NYEGHTPLHVAVIHKDVEMVRLLRDAGAD---LDKPeptcGRSPLHLAVEAQAADVLELLLR-------AGANPAARMYG 241
Cdd:PTZ00322  112 DYDGRTPLHIACANGHVQVVRVLLEFGADptlLDKD----GKTPLELAEENGFREVVQLLSRhsqchfeLGANAKPDSFT 187


                  ....*
gi 2462565531 242 GRTPL 246
Cdd:PTZ00322  188 GKPPS 192
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 171-266 1.16e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 171 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTCgRSPLHLAVEAQAADVLELLLRAGANPAARMY-GGRTPLGSA 249
Cdd:PHA02875   31 EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLA 109

                          90
                  ....*....|....*..
gi 2462565531 250 MLRPNPILARLLRAHGA 266
Cdd:PHA02875  110 TILKKLDIMKLLIARGA 126
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 174-203 3.42e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.96  E-value: 3.42e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462565531  174 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 203
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 187-262 6.59e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 6.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462565531 187 DVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAML-RPNPILARLLR 262
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKhYNKPIVHILLE 222
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 171-254 7.27e-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: 7.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 171 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD---------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAAR 238
Cdd:cd21882    69 EFYQGQTALHIAIENRNLNLVRLLVENGADVSaratgrffrKSPGNLfyfGELPLSLAACTNQEEIVRLLLENGAQPAAL 148

                          90
                  ....*....|....*....
gi 2462565531 239 MYG---GRTPLGSAMLRPN 254
Cdd:cd21882   149 EAQdslGNTVLHALVLQAD 167
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 175-266 7.96e-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: 7.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 175 GHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTC----GRSPLHLAVEAQAADVLELLLRAGA--------------NPA 236
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGPK 130

                          90       100       110
                  ....*....|....*....|....*....|
gi 2462565531 237 ARMYGGRTPLGSAMLRPNPILARLLRAHGA 266
Cdd:cd22192   131 NLIYYGEHPLSFAACVGNEEIVRLLIEHGA 160
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 141-249 9.15e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 9.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 141 NHTPVALYPDSDLEKEEEESEEDWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKpEPTCGRSPLHLAVEAQ 220
Cdd:PHA02874   90 NGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHN 168

                          90       100
                  ....*....|....*....|....*....
gi 2462565531 221 AADVLELLLRAGANPAARMYGGRTPLGSA 249
Cdd:PHA02874  169 FFDIIKLLLEKGAYANVKDNNGESPLHNA 197
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 168-277 9.76e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 9.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 168 LEAENYEGHTPLHVAVIHK-DVEMVRLLRDAGADLDKPEpTCGRSPLHLAVEA-QAADVLELLLRAGANPAARMYGGRTP 245
Cdd:PHA02876  300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD-RLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTP 378

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462565531 246 LGSAMLRPNPILARLLRAHGApEPEGEDEKSG 277
Cdd:PHA02876  379 IHYAAVRNNVVIINTLLDYGA-DIEALSQKIG 409
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 63-234 1.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531  63 QTALHLAAILGETSTVEKLYAAGAGLC-VAERRGHTALHLACRVGAHACARALLQPRPRRprEAPDTylaqgpDRTpDTN 141
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADP--DIPNT------DKF-SPL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 142 HTPVALypdSDLEKEEEESeeDWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDkpepTCGRSP----LHLAV 217
Cdd:PHA02875  140 HLAVMM---GDIKGIELLI--DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID----YFGKNGcvaaLCYAI 210

                         170
                  ....*....|....*..
gi 2462565531 218 EAQAADVLELLLRAGAN 234
Cdd:PHA02875  211 ENNKIDIVRLFIKRGAD 227
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 171-237 7.65e-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: 7.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565531 171 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADL---------DKPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAA 237
Cdd:cd22197    90 EYYRGHSALHIAIEKRSLQCVKLLVENGADVharacgrffQKKQGTCfyfGELPLSLAACTKQWDVVNYLLENPHQPAS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 171-251 1.12e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 171 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAM 250
Cdd:PHA02874  153 EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN-GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231


                  .
gi 2462565531 251 L 251
Cdd:PHA02874  232 I 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 209-235 1.26e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 1.26e-04
                           10        20
                   ....*....|....*....|....*..
gi 2462565531  209 GRSPLHLAVEAQAADVLELLLRAGANP 235
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-202 1.56e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 1.56e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462565531 174 EGHTPLHVAVIH-KDVEMVRLLRDAGADLD 202
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 175-234 1.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 1.84e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462565531 175 GHTPLHVAVIHKDVEMVRLLRDAGADLDkpepTC---GRSPLHLAVEAQAADVLELLLRAGAN 234
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPN----LVnkyGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 172-266 2.70e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.63  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 172 NYEGHTPLHVAV---IHKDVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQAADVLELLLR-AGANPAARMYGGRTPLG 247
Cdd:PHA02736   52 NRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNqPGVNMEILNYAFKTPYY 131

                          90
                  ....*....|....*....
gi 2462565531 248 SAMLRPNPILARLLRAHGA 266
Cdd:PHA02736  132 VACERHDAKMMNILRAKGA 150
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 169-237 3.43e-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: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 169 EAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANP 235
Cdd:cd22194   135 TEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEGfyfGETPLALAACTNQPEIVQLLMEKESTD 214


                  ..
gi 2462565531 236 AA 237
Cdd:cd22194   215 IT 216
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-203 3.73e-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: 37.24  E-value: 3.73e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462565531 174 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 203
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 55-115 7.90e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 7.90e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462565531  55 MDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALL 115
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 209-238 8.73e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 8.73e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462565531 209 GRSPLHLAV-EAQAADVLELLLRAGANPAAR 238
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_5 pfam13857
Ankyrin repeats (many copies);
168-216 9.63e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 9.63e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462565531 168 LEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPtCGRSPLHLA 216
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 166-266 1.35e-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: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 166 LQLEAENYEGHTPLHVAV--IHKDVEMV-RLLRDAGADLDKP---------EPTCGRSPLHLAVEAQAADVLELLLRAGA 233
Cdd:TIGR00870  73 LNLSCRGAVGDTLLHAISleYVDAVEAIlLHLLAAFRKSGPLelandqytsEFTPGITALHLAAHRQNYEIVKLLLERGA 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462565531 234 NPAAR--------------MYGGRTPLGSAMLRPNPILARLLRAHGA 266
Cdd:TIGR00870 153 SVPARacgdffvksqgvdsFYHGESPLNAAACLGSPSIVALLSEDPA 199
Ank_4 pfam13637
Ankyrin repeats (many copies);
64-115 1.80e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 1.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462565531  64 TALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALL 115
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 55-261 2.23e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531  55 MDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLQprprrpreapdtylaqgp 134
Cdd:PHA02874  150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID------------------ 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462565531 135 drtpDTNHTPValypdsdlekeeeeseedwklqleaENYEGHTPLHVAVIHKDVEMVRLLRDAG---ADLDkpeptcGRS 211
Cdd:PHA02874  212 ----HGNHIMN-------------------------KCKNGFTPLHNAIIHNRSAIELLINNASindQDID------GST 256

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462565531 212 PLHLAVEAQAA-DVLELLLRAGANPAARMYGGRTPLGSAM--LRPNPILARLL 261
Cdd:PHA02874  257 PLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAFkyINKDPVIKDII 309
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 208-237 2.25e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 2.25e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462565531 208 CGRSPLHLAVEAQAADVLELLLRAGANPAA 237
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 171-236 2.47e-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: 2.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462565531 171 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPA 236
Cdd:cd22193    72 EYYEGQTALHIAIERRQGDIVALLVENGADVHahakgrffqpKYQGEGfyfGELPLSLAACTNQPDIVQYLLENEHQPA 150
Ank_5 pfam13857
Ankyrin repeats (many copies);
193-246 3.33e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 3.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462565531 193 LLRDAGADLDKPEpTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPL 246
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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