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Conserved domains on  [gi|340805857|ref|NP_001230045|]
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NF-kappa-B inhibitor beta isoform 2 [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];
2-212 2.63e-25

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.57  E-value: 2.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857   2 DLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLqprprrpreapdtylAQGPD 81
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL---------------EAGAD 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  82 rtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHL 161
Cdd:COG0666  146 --------------------------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHL 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 340805857 162 AVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 212
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-212 2.63e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.57  E-value: 2.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857   2 DLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLqprprrpreapdtylAQGPD 81
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL---------------EAGAD 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  82 rtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHL 161
Cdd:COG0666  146 --------------------------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHL 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 340805857 162 AVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 212
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
PHA03095 PHA03095
ankyrin-like protein; Provisional
 117-212 2.03e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.67  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 117 ENYEGH---TPLHVAV---IHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVE-AQAADVLELLLRAGANPAARMYGGR 189
Cdd:PHA03095  40 VNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGR 118

                         90       100
                 ....*....|....*....|....*.
gi 340805857 190 TPLgSAMLRP---NPILARLLRAHGA 212
Cdd:PHA03095 119 TPL-HVYLSGfniNPKVIRLLLRKGA 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-148 9.11e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 9.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857   12 LHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLQprprrpreapdtylaqgpdrtpdtnhtpv 91
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----------------------------- 51

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 340805857   92 alYPDSDLekeeeeseedwklqleaeNYEGHTPLHVAVIHKDVEMVRLLRDAGADLD 148
Cdd:pfam12796  52 --HADVNL------------------KDNGRTALHYAARSGHLEIVKLLLEKGADIN 88
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 119-204 5.89e-11

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: 5.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 119 YEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPT-------------CGRSPLHLAVEAQAADVLELLLRAGANPAARM 185
Cdd:cd22192   87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                         90
                 ....*....|....*....
gi 340805857 186 YGGRTPLGSAMLRPNPILA 204
Cdd:cd22192  167 SLGNTVLHILVLQPNKTFA 185
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 117-184 2.32e-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: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  117 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAA 183
Cdd:TIGR00870 124 EFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILT 203


                  .
gi 340805857  184 R 184
Cdd:TIGR00870 204 A 204
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 120-149 7.17e-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: 41.80  E-value: 7.17e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 340805857   120 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 149
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-212 2.63e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.57  E-value: 2.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857   2 DLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLqprprrpreapdtylAQGPD 81
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL---------------EAGAD 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  82 rtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHL 161
Cdd:COG0666  146 --------------------------------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHL 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 340805857 162 AVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 212
Cdd:COG0666  193 AAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-212 6.01e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 6.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857   1 MDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLqprprrpreapdtylAQGP 80
Cdd:COG0666   47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL---------------EAGA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  81 DrtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLH 160
Cdd:COG0666  112 D--------------------------------VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 340805857 161 LAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGA 212
Cdd:COG0666  159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-221 1.26e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857   2 DLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLqprprrpreapdtylAQGPD 81
Cdd:COG0666  114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL---------------EAGAD 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  82 rtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHL 161
Cdd:COG0666  179 --------------------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND-GKTALDL 225

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 162 AVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGAPEPEGEDEK 221
Cdd:COG0666  226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
 117-212 2.03e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.67  E-value: 2.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 117 ENYEGH---TPLHVAV---IHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVE-AQAADVLELLLRAGANPAARMYGGR 189
Cdd:PHA03095  40 VNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGR 118

                         90       100
                 ....*....|....*....|....*.
gi 340805857 190 TPLgSAMLRP---NPILARLLRAHGA 212
Cdd:PHA03095 119 TPL-HVYLSGfniNPKVIRLLLRKGA 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-148 9.11e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 9.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857   12 LHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLQprprrpreapdtylaqgpdrtpdtnhtpv 91
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE----------------------------- 51

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 340805857   92 alYPDSDLekeeeeseedwklqleaeNYEGHTPLHVAVIHKDVEMVRLLRDAGADLD 148
Cdd:pfam12796  52 --HADVNL------------------KDNGRTALHYAARSGHLEIVKLLLEKGADIN 88
PHA03095 PHA03095
ankyrin-like protein; Provisional
 121-212 3.20e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 3.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 121 GHTPLHVAVIHKDVE-MVRLLRDAGADLDKpEPTCGRSPLH--LAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAML 197
Cdd:PHA03095  83 GFTPLHLYLYNATTLdVIKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLK 161

                         90
                 ....*....|....*..
gi 340805857 198 RPN--PILARLLRAHGA 212
Cdd:PHA03095 162 SRNanVELLRLLIDAGA 178
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 119-204 5.89e-11

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: 5.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 119 YEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPT-------------CGRSPLHLAVEAQAADVLELLLRAGANPAARM 185
Cdd:cd22192   87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                         90
                 ....*....|....*....
gi 340805857 186 YGGRTPLGSAMLRPNPILA 204
Cdd:cd22192  167 SLGNTVLHILVLQPNKTFA 185
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-192 9.62e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.74  E-value: 9.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857   2 DLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALlqprprrpreapdtyLAQGPD 81
Cdd:COG0666  147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL---------------LEAGAD 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  82 rtpdtnhtpvalypdsdlekeeeeseedwklqLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHL 161
Cdd:COG0666  212 --------------------------------VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD-GLTALLL 258

                        170       180       190
                 ....*....|....*....|....*....|.
gi 340805857 162 AVEAQAADVLELLLRAGANPAARMYGGRTPL 192
Cdd:COG0666  259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 118-212 4.63e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 59.29  E-value: 4.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 118 NYEGHTPLHVAV--IHKDVEMVRLLRDAGAD----------LDKPEPT-----CGRSPLHLAVEAQAADVLELLLRAGAN 180
Cdd:PHA03100 138 NSDGENLLHLYLesNKIDLKILKLLIDKGVDinaknrvnylLSYGVPInikdvYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                         90       100       110
                 ....*....|....*....|....*....|..
gi 340805857 181 PAARMYGGRTPLGSAMLRPNPILARLLRAHGA 212
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 120-212 1.00e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 120 EGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRP 199
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPN-TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179

                         90
                 ....*....|...
gi 340805857 200 NPILARLLRAHGA 212
Cdd:PHA02875 180 DIAICKMLLDSGA 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-212 2.74e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.20  E-value: 2.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  125 LHVAVIHKDVEMVRLLRDAGADLDKPEPtCGRSPLHLAVEAQAADVLELLLragANPAARMYG-GRTPLGSAMLRPNPIL 203
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLL---EHADVNLKDnGRTALHYAARSGHLEI 76


                  ....*....
gi 340805857  204 ARLLRAHGA 212
Cdd:pfam12796  77 VKLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
120-184 6.80e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 6.80e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 340805857  120 EGHTPLHVAVIHKDVEMVRLLRDaGADLDkpEPTCGRSPLHLAVEAQAADVLELLLRAGANPAAR 184
Cdd:pfam12796  29 NGRTALHLAAKNGHLEIVKLLLE-HADVN--LKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 121-212 1.42e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 121 GHTPLHVAVIHKDVEMVRLLRDAGADLDKPEpTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPN 200
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPD-KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCK 246

                         90
                 ....*....|...
gi 340805857 201 PI-LARLLRAHGA 212
Cdd:PHA02878 247 DYdILKLLLEHGV 259
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 123-212 1.84e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 1.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 123 TPLHVAVIHKDVEMVRLLRDAGADLDKpEPTCGRSPLHLAVEAQAADVLELLLRAGANPAarmYGGRTPLGSAMLRP--- 199
Cdd:PHA02875 137 SPLHLAVMMGDIKGIELLIDHKACLDI-EDCCGCTPLIIAMAKGDIAICKMLLDSGANID---YFGKNGCVAALCYAien 212

                         90
                 ....*....|....
gi 340805857 200 -NPILARLLRAHGA 212
Cdd:PHA02875 213 nKIDIVRLFIKRGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-62 2.63e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 2.63e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 340805857    1 MDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAErrGHTALHLACRVGAHACARALLQ 62
Cdd:pfam12796  23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVKLLLE 82
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 115-198 1.51e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 115 EAENYEGHTPLHVAVIH-KDVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQaaDVLELLLRAGANPAARMYGGRTPLG 193
Cdd:PHA02878 228 DARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLS 305


                 ....*
gi 340805857 194 SAMLR 198
Cdd:PHA02878 306 SAVKQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
121-175 1.79e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 1.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 340805857  121 GHTPLHVAVIHKDVEMVRLLRDAGADLDKPePTCGRSPLHLAVEAQAADVLELLL 175
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 114-195 1.83e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 114 LEAENYEGHTPLHVAVIHK--DVEMVRLLRDAGADLDKPEpTCGRSPLH-LAVEAQA-ADVLELLLRAGANPAARMYGGR 189
Cdd:PHA03095 145 VNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVD-DRFRSLLHhHLQSFKPrARIVRELIRAGCDPAATDMLGN 223


                 ....*.
gi 340805857 190 TPLGSA 195
Cdd:PHA03095 224 TPLHSM 229
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 117-184 2.32e-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: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  117 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAA 183
Cdd:TIGR00870 124 EFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILT 203


                  .
gi 340805857  184 R 184
Cdd:TIGR00870 204 A 204
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 117-212 7.41e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 7.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 117 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTCgRSPLHLAVEAQAADVLELLLRAGANPAARMY-GGRTPLGSA 195
Cdd:PHA02875  31 EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDI-ESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLA 109

                         90
                 ....*....|....*..
gi 340805857 196 MLRPNPILARLLRAHGA 212
Cdd:PHA02875 110 TILKKLDIMKLLIARGA 126
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 118-192 8.09e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 8.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 118 NYEGHTPLHVAVIHKDVEMVRLLRDAGAD---LDKPeptcGRSPLHLAVEAQAADVLELLLR-------AGANPAARMYG 187
Cdd:PTZ00322 112 DYDGRTPLHIACANGHVQVVRVLLEFGADptlLDKD----GKTPLELAEENGFREVVQLLSRhsqchfeLGANAKPDSFT 187


                 ....*
gi 340805857 188 GRTPL 192
Cdd:PTZ00322 188 GKPPS 192
PHA03095 PHA03095
ankyrin-like protein; Provisional
 4-214 1.30e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857   4 QNDLGQTALH--LAAILGETSTVEKLYAAGAGLCVAERRGHTALH--------------LACRVGAHACA-----RALLQ 62
Cdd:PHA03095 113 KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksrnanvellrLLIDAGADVYAvddrfRSLLH 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  63 prprrpreapdtYLAQGPDRTPDTNHTPVALYPDSdlekeeeeseedwklqlEAENYEGHTPLHVAVIH---KDVEMVRL 139
Cdd:PHA03095 193 ------------HHLQSFKPRARIVRELIRAGCDP-----------------AATDMLGNTPLHSMATGsscKRSLVLPL 243

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 340805857 140 LrDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNP-ILARLLRAHGAPE 214
Cdd:PHA03095 244 L-IAGISINARNRY-GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGrAVRAALAKNPSAE 317
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 133-208 4.28e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 4.28e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 340805857 133 DVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAML-RPNPILARLLR 208
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKhYNKPIVHILLE 222
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 117-200 4.66e-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: 4.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 117 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD---------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAAR 184
Cdd:cd21882   69 EFYQGQTALHIAIENRNLNLVRLLVENGADVSaratgrffrKSPGNLfyfGELPLSLAACTNQEEIVRLLLENGAQPAAL 148

                         90
                 ....*....|....*....
gi 340805857 185 MYG---GRTPLGSAMLRPN 200
Cdd:cd21882  149 EAQdslGNTVLHALVLQAD 167
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 121-212 5.10e-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: 5.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 121 GHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTC----GRSPLHLAVEAQAADVLELLLRAGA--------------NPA 182
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyqGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGPK 130

                         90       100       110
                 ....*....|....*....|....*....|
gi 340805857 183 ARMYGGRTPLGSAMLRPNPILARLLRAHGA 212
Cdd:cd22192  131 NLIYYGEHPLSFAACVGNEEIVRLLIEHGA 160
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 87-195 5.50e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 5.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  87 NHTPVALYPDSDLEKEEEESEEDWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKpEPTCGRSPLHLAVEAQ 166
Cdd:PHA02874  90 NGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCYPIHIAIKHN 168

                         90       100
                 ....*....|....*....|....*....
gi 340805857 167 AADVLELLLRAGANPAARMYGGRTPLGSA 195
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDNNGESPLHNA 197
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 114-223 6.28e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 6.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 114 LEAENYEGHTPLHVAVIHK-DVEMVRLLRDAGADLDKPEpTCGRSPLHLAVEA-QAADVLELLLRAGANPAARMYGGRTP 191
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD-RLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTP 378

                         90       100       110
                 ....*....|....*....|....*....|..
gi 340805857 192 LGSAMLRPNPILARLLRAHGApEPEGEDEKSG 223
Cdd:PHA02876 379 IHYAAVRNNVVIINTLLDYGA-DIEALSQKIG 409
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 120-149 7.17e-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: 41.80  E-value: 7.17e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 340805857   120 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 149
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-180 9.73e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 9.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857   9 QTALHLAAILGETSTVEKLYAAGAGLC-VAERRGHTALHLACRVGAHACARALLQPRPRRprEAPDTylaqgpDRTpDTN 87
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADP--DIPNT------DKF-SPL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  88 HTPVALypdSDLEKEEEESeeDWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDkpepTCGRSP----LHLAV 163
Cdd:PHA02875 140 HLAVMM---GDIKGIELLI--DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID----YFGKNGcvaaLCYAI 210

                        170
                 ....*....|....*..
gi 340805857 164 EAQAADVLELLLRAGAN 180
Cdd:PHA02875 211 ENNKIDIVRLFIKRGAD 227
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 117-183 5.10e-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: 5.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 340805857 117 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADL---------DKPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPAA 183
Cdd:cd22197   90 EYYRGHSALHIAIEKRSLQCVKLLVENGADVharacgrffQKKQGTCfyfGELPLSLAACTKQWDVVNYLLENPHQPAS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 117-197 7.66e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 7.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 117 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTcGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAM 196
Cdd:PHA02874 153 EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN-GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231


                 .
gi 340805857 197 L 197
Cdd:PHA02874 232 I 232
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 121-180 1.26e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 1.26e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 340805857 121 GHTPLHVAVIHKDVEMVRLLRDAGADLDkpepTC---GRSPLHLAVEAQAADVLELLLRAGAN 180
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPN----LVnkyGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 118-212 2.09e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.63  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 118 NYEGHTPLHVAV---IHKDVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQAADVLELLLR-AGANPAARMYGGRTPLG 193
Cdd:PHA02736  52 NRHGKQCVHIVSnpdKADPQEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNqPGVNMEILNYAFKTPYY 131

                         90
                 ....*....|....*....
gi 340805857 194 SAMLRPNPILARLLRAHGA 212
Cdd:PHA02736 132 VACERHDAKMMNILRAKGA 150
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 115-183 2.34e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857 115 EAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANP 181
Cdd:cd22194  135 TEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEGfyfGETPLALAACTNQPEIVQLLMEKESTD 214


                 ..
gi 340805857 182 AA 183
Cdd:cd22194  215 IT 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 155-181 2.43e-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: 37.57  E-value: 2.43e-04
                           10        20
                   ....*....|....*....|....*..
gi 340805857   155 GRSPLHLAVEAQAADVLELLLRAGANP 181
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 120-148 3.59e-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: 37.27  E-value: 3.59e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 340805857  120 EGHTPLHVAVIH-KDVEMVRLLRDAGADLD 148
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 120-149 8.24e-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: 36.08  E-value: 8.24e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 340805857  120 EGHTPLHVAVIHKDVEMVRLLRDAGADLDK 149
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 112-212 9.40e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 9.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  112 LQLEAENYEGHTPLHVAV--IHKDVEMV-RLLRDAGADLDKP---------EPTCGRSPLHLAVEAQAADVLELLLRAGA 179
Cdd:TIGR00870  73 LNLSCRGAVGDTLLHAISleYVDAVEAIlLHLLAAFRKSGPLelandqytsEFTPGITALHLAAHRQNYEIVKLLLERGA 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 340805857  180 NPAAR--------------MYGGRTPLGSAMLRPNPILARLLRAHGA 212
Cdd:TIGR00870 153 SVPARacgdffvksqgvdsFYHGESPLNAAACLGSPSIVALLSEDPA 199
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-61 1.03e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 1.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340805857   1 MDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALL 61
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-207 1.59e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857   1 MDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLQprprrpreapdtylaqgp 80
Cdd:PHA02874 150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID------------------ 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340805857  81 drtpDTNHTPValypdsdlekeeeeseedwklqleaENYEGHTPLHVAVIHKDVEMVRLLRDAG---ADLDkpeptcGRS 157
Cdd:PHA02874 212 ----HGNHIMN-------------------------KCKNGFTPLHNAIIHNRSAIELLINNASindQDID------GST 256

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 340805857 158 PLHLAVEAQAA-DVLELLLRAGANPAARMYGGRTPLGSAM--LRPNPILARLL 207
Cdd:PHA02874 257 PLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAFkyINKDPVIKDII 309
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 117-182 1.74e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 39.39  E-value: 1.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 340805857 117 ENYEGHTPLHVAVIHKDVEMVRLLRDAGADLD----------KPEPTC---GRSPLHLAVEAQAADVLELLLRAGANPA 182
Cdd:cd22193   72 EYYEGQTALHIAIERRQGDIVALLVENGADVHahakgrffqpKYQGEGfyfGELPLSLAACTNQPDIVQYLLENEHQPA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 155-184 1.89e-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: 34.96  E-value: 1.89e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 340805857  155 GRSPLHLAVE-AQAADVLELLLRAGANPAAR 184
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
Ank_5 pfam13857
Ankyrin repeats (many copies);
114-162 2.24e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 2.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 340805857  114 LEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPtCGRSPLHLA 162
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.34e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 2.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 340805857   10 TALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALL 61
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 154-183 4.65e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.77  E-value: 4.65e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 340805857  154 CGRSPLHLAVEAQAADVLELLLRAGANPAA 183
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
139-192 7.24e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.24  E-value: 7.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 340805857  139 LLRDAGADLDKPEpTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPL 192
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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