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Conserved domains on  [gi|564361019|ref|XP_006242074|]
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ankyrin repeat domain-containing protein 54 isoform X1 [Rattus norvegicus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-235 8.62e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 8.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 113 LRDSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVIT 192
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 564361019 193 TLLRGGARVDALDRAGRTPLHLAksklniLQEGHsqcLEAVRL 235
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLA------AENGH---LEIVKL 204
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-235 8.62e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 8.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 113 LRDSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVIT 192
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 564361019 193 TLLRGGARVDALDRAGRTPLHLAksklniLQEGHsqcLEAVRL 235
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLA------AENGH---LEIVKL 204
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-205 4.29e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 4.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019  117 ANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHgADPNQQDGlGNTPLHLAACTNHVPVITTLLR 196
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82


                  ....*....
gi 564361019  197 GGARVDALD 205
Cdd:pfam12796  83 KGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 107-215 2.28e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 107 VHALKRlrdSANANdIETVQQLLEDGADPCAADDKGRTALH-FA-SCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAA- 183
Cdd:PHA03095 156 LAVLLK---SRNAN-VELLRLLIDAGADVYAVDDRFRSLLHhHLqSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAt 231

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564361019 184 -CTNHVPVITTLLRGGARVDALDRAGRTPLHLA 215
Cdd:PHA03095 232 gSSCKRSLVLPLLIAGISINARNRYGQTPLHYA 264
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-221 2.23e-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: 64.65  E-value: 2.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 120 NDIETVQQLLEDGADPCAAD------DKGRTAL-----H---FASCNGNDQIVQLLLDHGADPNQQDGLGNTPLH-LAAC 184
Cdd:cd22192  100 QNLNLVRELIARGADVVSPRatgtffRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQ 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564361019 185 TNHVPV------ITTLLRGG--ARVDAL-DRAGRTPLHLAKSKLNI 221
Cdd:cd22192  180 PNKTFAcqmydlILSYDKEDdlQPLDLVpNNQGLTPFKLAAKEGNI 225
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 141-169 4.06e-07

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: 45.66  E-value: 4.06e-07
                           10        20
                   ....*....|....*....|....*....
gi 564361019   141 KGRTALHFASCNGNDQIVQLLLDHGADPN 169
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 120-221 2.25e-06

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: 49.31  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019  120 NDIETVQQLLEDGAD---PCAADD-----------KGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACT 185
Cdd:TIGR00870 139 QNYEIVKLLLERGASvpaRACGDFfvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVME 218

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564361019  186 NHVPVITT---------LLRGGARVDA-------LDRAGRTPLHLAKSKLNI 221
Cdd:TIGR00870 219 NEFKAEYEelscqmynfALSLLDKLRDskeleviLNHQGLTPLKLAAKEGRI 270
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-235 8.62e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 8.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 113 LRDSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVIT 192
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 564361019 193 TLLRGGARVDALDRAGRTPLHLAksklniLQEGHsqcLEAVRL 235
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLA------AENGH---LEIVKL 204
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-220 5.74e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 5.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 117 ANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLR 196
Cdd:COG0666  128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         90       100
                 ....*....|....*....|....
gi 564361019 197 GGARVDALDRAGRTPLHLAKSKLN 220
Cdd:COG0666  208 AGADVNAKDNDGKTALDLAAENGN 231
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
113-215 5.30e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 5.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 113 LRDSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVIT 192
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                         90       100
                 ....*....|....*....|...
gi 564361019 193 TLLRGGARVDALDRAGRTPLHLA 215
Cdd:COG0666  138 LLLEAGADVNAQDNDGNTPLHLA 160
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-222 6.52e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.26  E-value: 6.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 117 ANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLR 196
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         90       100
                 ....*....|....*....|....*.
gi 564361019 197 GGARVDALDRAGRTPLHLAKSKLNIL 222
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAAL 266
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-205 4.29e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 4.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019  117 ANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHgADPNQQDGlGNTPLHLAACTNHVPVITTLLR 196
Cdd:pfam12796   5 AKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLLE 82


                  ....*....
gi 564361019  197 GGARVDALD 205
Cdd:pfam12796  83 KGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 107-215 2.28e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 107 VHALKRlrdSANANdIETVQQLLEDGADPCAADDKGRTALH-FA-SCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAA- 183
Cdd:PHA03095 156 LAVLLK---SRNAN-VELLRLLIDAGADVYAVDDRFRSLLHhHLqSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMAt 231

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564361019 184 -CTNHVPVITTLLRGGARVDALDRAGRTPLHLA 215
Cdd:PHA03095 232 gSSCKRSLVLPLLIAGISINARNRYGQTPLHYA 264
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 110-219 5.03e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.46  E-value: 5.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 110 LKRLRDSANANDIET--VQQLLEDGADPCAAD-DKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTN 186
Cdd:PHA02878 133 LVYIDKKSKDDIIEAeiTKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHY 212

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564361019 187 HVPVITTLLRGGARVDALDRAGRTPLHLAKSKL 219
Cdd:PHA02878 213 NKPIVHILLENGASTDARDKCGNTPLHISVGYC 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
146-231 1.17e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019  146 LHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRgGARVDALDRaGRTPLHLAksklniLQEG 225
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYA------ARSG 72


                  ....*.
gi 564361019  226 HSQCLE 231
Cdd:pfam12796  73 HLEIVK 78
PHA03095 PHA03095
ankyrin-like protein; Provisional
 98-243 2.55e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.30  E-value: 2.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019  98 RRLGPTGKEVH--------ALKRLRDSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADP 168
Cdd:PHA03095  31 RRLLAAGADVNfrgeygktPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADV 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564361019 169 NQQDGLGNTPLHlAACTN---HVPVITTLLRGGARVDALDRAGRTPLHlaksklnILQEGHSQCLEAVRLEVKQIIHM 243
Cdd:PHA03095 111 NAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLA-------VLLKSRNANVELLRLLIDAGADV 180
PHA03095 PHA03095
ankyrin-like protein; Provisional
 110-221 1.53e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.91  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 110 LKRLRDSANAnDIETVQQLLEDGADPCAADDKGRTALH-FASCNGND--QIVQLLLDHGADPNQQDGLGNTPLHLAACTN 186
Cdd:PHA03095  16 YDYLLNASNV-TVEEVRRLLAAGADVNFRGEYGKTPLHlYLHYSSEKvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNA 94

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 564361019 187 HV-PVITTLLRGGARVDALDRAGRTPLHLAKSKLNI 221
Cdd:PHA03095  95 TTlDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNI 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
109-215 1.60e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 69.98  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 109 ALKRLRDSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHV 188
Cdd:COG0666   21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100

                         90       100
                 ....*....|....*....|....*..
gi 564361019 189 PVITTLLRGGARVDALDRAGRTPLHLA 215
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLA 127
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 123-215 6.30e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 6.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 123 ETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVD 202
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90
                 ....*....|...
gi 564361019 203 ALDRAGRTPLHLA 215
Cdd:PHA02874 185 VKDNNGESPLHNA 197
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-212 7.74e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 68.06  E-value: 7.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 117 ANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLR 196
Cdd:COG0666  194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273

                         90
                 ....*....|....*.
gi 564361019 197 GGARVDALDRAGRTPL 212
Cdd:COG0666  274 ALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 125-215 1.05e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 125 VQQLLEDGADPCAADDKGRTALH----FASCNgnDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGAR 200
Cdd:PHA03095 205 VRELIRAGCDPAATDMLGNTPLHsmatGSSCK--RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGAD 282

                         90
                 ....*....|....*
gi 564361019 201 VDALDRAGRTPLHLA 215
Cdd:PHA03095 283 INAVSSDGNTPLSLM 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-215 2.73e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 2.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 116 SANANDIETVQQLLEDGADPCAADDKGRTALHFASC-NGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTL 194
Cdd:PHA02876 315 AKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                         90       100
                 ....*....|....*....|.
gi 564361019 195 LRGGARVDALDRAGRTPLHLA 215
Cdd:PHA02876 395 LDYGADIEALSQKIGTALHFA 415
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 118-223 6.02e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.23  E-value: 6.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 118 NANDIETVQQLLEDGADPCAADDKGRTALHFASCNG-----NDQIVQLLLDHGADPNQQDGLGNTPLHLAACT--NHVPV 190
Cdd:PHA03100  44 EARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSI 123

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564361019 191 ITTLLRGGARVDALDRAGRTPLHLA----KSKLNILQ 223
Cdd:PHA03100 124 VEYLLDNGANVNIKNSDGENLLHLYlesnKIDLKILK 160
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 125-222 6.28e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.63  E-value: 6.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 125 VQQLLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADPNQQDGLGNTPLHLAACTN-HVPVITTLLRGGARVD 202
Cdd:PHA02876 290 VPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVN 369

                         90       100
                 ....*....|....*....|
gi 564361019 203 ALDRAGRTPLHLAKSKLNIL 222
Cdd:PHA02876 370 ARDYCDKTPIHYAAVRNNVV 389
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 117-206 6.97e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 6.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 117 ANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLR 196
Cdd:PHA03100 167 VDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246

                         90
                 ....*....|
gi 564361019 197 GGARVDALDR 206
Cdd:PHA03100 247 NGPSIKTIIE 256
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 120-215 1.75e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 120 NDIETVQQLLEDGADPCAADDKGRTALH-FASCNGND-QIVQLLLDHGADPNQQDGL----------------GNTPLHL 181
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHlYLESNKIDlKILKLLIDKGVDINAKNRVnyllsygvpinikdvyGFTPLHY 198

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564361019 182 AACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 215
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 120-221 2.23e-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: 64.65  E-value: 2.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 120 NDIETVQQLLEDGADPCAAD------DKGRTAL-----H---FASCNGNDQIVQLLLDHGADPNQQDGLGNTPLH-LAAC 184
Cdd:cd22192  100 QNLNLVRELIARGADVVSPRatgtffRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiLVLQ 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564361019 185 TNHVPV------ITTLLRGG--ARVDAL-DRAGRTPLHLAKSKLNI 221
Cdd:cd22192  180 PNKTFAcqmydlILSYDKEDdlQPLDLVpNNQGLTPFKLAAKEGNI 225
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 110-215 2.35e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.53  E-value: 2.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 110 LKRLRDSANANDIETVQQLLEDGADPCAADDKGRTALHFAScNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVP 189
Cdd:PTZ00322  51 LEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQ 129

                         90       100
                 ....*....|....*....|....*.
gi 564361019 190 VITTLLRGGARVDALDRAGRTPLHLA 215
Cdd:PTZ00322 130 VVRVLLEFGADPTLLDKDGKTPLELA 155
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 117-196 2.40e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.53  E-value: 2.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 117 ANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLR 196
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-195 1.07e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 1.07e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564361019  142 GRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLL 195
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 120-215 2.15e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 61.52  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 120 NDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGA 199
Cdd:PHA02874 135 GDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214

                         90
                 ....*....|....*.
gi 564361019 200 RVDALDRAGRTPLHLA 215
Cdd:PHA02874 215 HIMNKCKNGFTPLHNA 230
PHA02946 PHA02946
ankyin-like protein; Provisional
 121-212 2.33e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 61.22  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 121 DIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNH--VPVITTLLRGG 198
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYG 130

                         90
                 ....*....|....*
gi 564361019 199 ARV-DALDRAGRTPL 212
Cdd:PHA02946 131 AKInNSVDEEGCGPL 145
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-222 1.33e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 116 SANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQI-VQLLLDHGADPNQQDGLGNTPLHLAACTNHVP-VITT 193
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEM 461

                         90       100       110
                 ....*....|....*....|....*....|..
gi 564361019 194 LLRGGARVDALDRAGRTPLHLA---KSKLNIL 222
Cdd:PHA02876 462 LLDNGADVNAINIQNQYPLLIAleyHGIVNIL 493
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 125-235 1.45e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.11  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 125 VQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPL----------------HLAA----- 183
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyHFASisdph 620

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564361019 184 ------CT----NHVPVITTLLRGGARVDALDRAGRTPLHLAksklniLQEGHsqcLEAVRL 235
Cdd:PLN03192 621 aagdllCTaakrNDLTAMKELLKQGLNVDSEDHQGATALQVA------MAEDH---VDMVRL 673
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 113-221 2.80e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 2.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 113 LRDSANANDIETVQQLLEDGAdpcAADD----KGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHV 188
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGK---FADDvfykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110
                 ....*....|....*....|....*....|...
gi 564361019 189 PVITTLLRGGARVDALDRAGRTPLHLAKSKLNI 221
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDI 181
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 106-201 3.58e-09

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: 57.72  E-value: 3.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 106 EVHAL--KRLRDS-----ANANDIETVQQLLE-DGADPCAADDKGRTALHFASCNGNDQIVQLLLDhgADP---NQ---- 170
Cdd:cd22192    7 ELHLLqqKRISESplllaAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPelvNEpmts 84

                         90       100       110
                 ....*....|....*....|....*....|.
gi 564361019 171 QDGLGNTPLHLAACTNHVPVITTLLRGGARV 201
Cdd:cd22192   85 DLYQGETALHIAVVNQNLNLVRELIARGADV 115
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 141-213 8.47e-09

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 56.74  E-value: 8.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 141 KGRTALHFASCNGNDQIVQLLLDHGADPN------------QQDG--LGNTPLHLAACTNHVPVITTLLRG---GARVDA 203
Cdd:cd22196   93 KGQTALHIAIERRNMHLVELLVQNGADVHarasgeffkkkkGGPGfyFGELPLSLAACTNQLDIVKFLLENphsPADISA 172

                         90
                 ....*....|
gi 564361019 204 LDRAGRTPLH 213
Cdd:cd22196  173 RDSMGNTVLH 182
Ank_5 pfam13857
Ankyrin repeats (many copies);
128-182 1.63e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 1.63e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564361019  128 LLEDG-ADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLA 182
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 121-212 4.49e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 54.53  E-value: 4.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 121 DIETVQQLLEDGADPCAADDKGRTALH--FASCNGNDQIVQLLLDHGADPNQQDGLGNTPLH-----------LAACTNH 187
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvniLDPETDN 375

                         90       100
                 ....*....|....*....|....*...
gi 564361019 188 ---VPVITTLLRGGARVDALDRAGRTPL 212
Cdd:PHA02716 376 dirLDVIQCLISLGADITAVNCLGYTPL 403
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 108-220 5.72e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 5.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 108 HALKRLRDSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQD-GLGNTPLHLAACTN 186
Cdd:PHA02878 100 YTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENK 179

                         90       100       110
                 ....*....|....*....|....*....|....
gi 564361019 187 HVPVITTLLRGGARVDALDRAGRTPLHLAKSKLN 220
Cdd:PHA02878 180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYN 213
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 125-221 6.49e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 54.12  E-value: 6.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 125 VQQLLEDGAD-------------PCAADDKGRTALHFASCNGNDQIVQLLLDHGADP---NQQDGLGNTPLH-LAACTNH 187
Cdd:cd21882   89 VRLLVENGADvsaratgrffrksPGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHaLVLQADN 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 564361019 188 VPVITT--------LLRGGARVDAL-------DRAGRTPLHLAKSKLNI 221
Cdd:cd21882  169 TPENSAfvcqmynlLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGKI 217
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 121-208 8.65e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 8.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 121 DIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGAR 200
Cdd:PHA02875 114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193


                 ....*...
gi 564361019 201 VDALDRAG 208
Cdd:PHA02875 194 IDYFGKNG 201
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 121-217 8.89e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 8.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 121 DIETVQQLLEDGADPCAADDKGRTALHFASCNGN-DQIVQLLLDHGADPNQQDGLGNTPLHLAACTNH-VPVITTLLRGG 198
Cdd:PHA02876 252 DLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLG 331

                         90
                 ....*....|....*....
gi 564361019 199 ARVDALDRAGRTPLHLAKS 217
Cdd:PHA02876 332 ADVNAADRLYITPLHQAST 350
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-172 1.59e-07

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: 46.90  E-value: 1.59e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564361019  141 KGRTALHFASC-NGNDQIVQLLLDHGADPNQQD 172
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 120-215 1.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 120 NDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVitTLLRGGA 199
Cdd:PHA02874 168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNA 245

                         90
                 ....*....|....*.
gi 564361019 200 RVDALDRAGRTPLHLA 215
Cdd:PHA02874 246 SINDQDIDGSTPLHHA 261
Ank_4 pfam13637
Ankyrin repeats (many copies);
117-162 2.36e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.36e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 564361019  117 ANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLL 162
Cdd:pfam13637   9 AASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 101-213 2.79e-07

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: 52.16  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 101 GPTGKE--VHALKRLRDSANAndieTVQQLLEDGADP----------CAAD-DKGRTALHFASCNGNDQIVQLLLDHGAD 167
Cdd:cd22197   44 GSTGKTclMKAVLNLQDGVNA----CIMPLLEIDKDSgnpkplvnaqCTDEyYRGHSALHIAIEKRSLQCVKLLVENGAD 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564361019 168 PN---------QQDG----LGNTPLHLAACTNHVPVITTLLRGG---ARVDALDRAGRTPLH 213
Cdd:cd22197  120 VHaracgrffqKKQGtcfyFGELPLSLAACTKQWDVVNYLLENPhqpASLQAQDSLGNTVLH 181
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 141-213 3.05e-07

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: 51.80  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 141 KGRTALHFASCNGNDQIVQLLLDHGAD-------------PNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDAL--- 204
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADvsaratgrffrksPGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALeaq 151


                 ....*....
gi 564361019 205 DRAGRTPLH 213
Cdd:cd21882  152 DSLGNTVLH 160
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 159-229 3.15e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 49.49  E-value: 3.15e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564361019 159 QLLLDHGADPNQQDGL-GNTPLHLAACTNHVPVITTLLRG-GARVDALDRAGRTPLHLAKSK-----LNILQEGHSQC 229
Cdd:PHA02736  75 KLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERhdakmMNILRAKGAQC 152
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 125-215 3.89e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 3.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 125 VQQLLEDGADPCAADDKGRTALHFASCNGND-QIVQLLLDHGADPNQQDG-LGNTPLHLAActnHVP-VITTLLRGGARV 201
Cdd:PHA02878 217 VHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLTALHSSI---KSErKLKLLLEYGADI 293

                         90
                 ....*....|....
gi 564361019 202 DALDRAGRTPLHLA 215
Cdd:PHA02878 294 NSLNSYKLTPLSSA 307
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 141-169 4.06e-07

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: 45.66  E-value: 4.06e-07
                           10        20
                   ....*....|....*....|....*....
gi 564361019   141 KGRTALHFASCNGNDQIVQLLLDHGADPN 169
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 118-213 4.50e-07

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: 51.30  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 118 NANDIETVQQLL----EDG-------ADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPN------------QQDG- 173
Cdd:cd22194  106 NENTKEIVRILLafaeENGildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpkyKHEGf 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 564361019 174 -LGNTPLHLAACTNHVPVITTLL-RGGARVDALDRAGRTPLH 213
Cdd:cd22194  186 yFGETPLALAACTNQPEIVQLLMeKESTDITSQDSRGNTVLH 227
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 141-213 5.94e-07

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: 50.95  E-value: 5.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 141 KGRTALHFASCNGNDQIVQLLLDHGAD-----------PNQQDG---LGNTPLHLAACTNHVPVITTLLRGG---ARVDA 203
Cdd:cd22193   75 EGQTALHIAIERRQGDIVALLVENGADvhahakgrffqPKYQGEgfyFGELPLSLAACTNQPDIVQYLLENEhqpADIEA 154

                         90
                 ....*....|
gi 564361019 204 LDRAGRTPLH 213
Cdd:cd22193  155 QDSRGNTVLH 164
Ank_5 pfam13857
Ankyrin repeats (many copies);
161-215 6.60e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 6.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 564361019  161 LLDHG-ADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLA 215
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 125-207 8.00e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 8.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 125 VQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDAL 204
Cdd:PHA03095 240 VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319


                 ...
gi 564361019 205 DRA 207
Cdd:PHA03095 320 AAT 322
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 105-205 9.07e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.45  E-value: 9.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 105 KEVHALKRLRDSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPN--QQDGLgnTPLHLA 182
Cdd:PHA02876 141 ESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiiALDDL--SVLECA 218

                         90       100
                 ....*....|....*....|...
gi 564361019 183 ACTNHVPVITTLLRGGARVDALD 205
Cdd:PHA02876 219 VDSKNIDTIKAIIDNRSNINKND 241
PHA02946 PHA02946
ankyin-like protein; Provisional
 154-213 2.13e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.90  E-value: 2.13e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 154 NDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLH 213
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY 110
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 120-221 2.25e-06

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: 49.31  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019  120 NDIETVQQLLEDGAD---PCAADD-----------KGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACT 185
Cdd:TIGR00870 139 QNYEIVKLLLERGASvpaRACGDFfvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVME 218

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564361019  186 NHVPVITT---------LLRGGARVDA-------LDRAGRTPLHLAKSKLNI 221
Cdd:TIGR00870 219 NEFKAEYEelscqmynfALSLLDKLRDskeleviLNHQGLTPLKLAAKEGRI 270
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 141-216 2.86e-06

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: 48.92  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019  141 KGRTALHFASCNGNDQIVQLLLDHGADPN------------QQDGL--GNTPLHLAACTNHVPVITTLLRGGARVDALDR 206
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVParacgdffvksqGVDSFyhGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90
                  ....*....|
gi 564361019  207 AGRTPLHLAK 216
Cdd:TIGR00870 207 LGNTLLHLLV 216
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-169 7.85e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 7.85e-06
                          10        20
                  ....*....|....*....|....*....
gi 564361019  141 KGRTALHFASCNGNDQIVQLLLDHGADPN 169
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
175-231 2.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 2.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 564361019  175 GNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAksklniLQEGHSQCLE 231
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA------ASNGNVEVLK 51
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 175-206 7.17e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 7.17e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 564361019  175 GNTPLHLAAC-TNHVPVITTLLRGGARVDALDR 206
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 115-213 9.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 9.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 115 DSANANdIETVQQLLEDGAD-PCAADDKGRTALH-FASCNGN--DQIVQLLLDHGADPNQQDGLGNTPLH--LAACTNHV 188
Cdd:PHA02859  60 EKDKVN-VEILKFLIENGADvNFKTRDNNLSALHhYLSFNKNvePEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRI 138

                         90       100
                 ....*....|....*....|....*
gi 564361019 189 PVITTLLRGGARVDALDRAGRTPLH 213
Cdd:PHA02859 139 NVIKLLIDSGVSFLNKDFDNNNILY 163
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 113-220 1.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.41  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 113 LRDSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNgNDQIVQLLLDHgADPNQQDGLGNTPLHLA---ACTnhVP 189
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINN-ASINDQDIDGSTPLHHAinpPCD--ID 269

                         90       100       110
                 ....*....|....*....|....*....|.
gi 564361019 190 VITTLLRGGARVDALDRAGRTPLHLAKSKLN 220
Cdd:PHA02874 270 IIDILLYHKADISIKDNKGENPIDTAFKYIN 300
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 153-305 1.54e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.70  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 153 GNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSK-----LNILQE--- 224
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAkhhkiFRILYHfas 615

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 225 -------GHSQCLEAVRLEVKqiihMLREYLeRLGRHEQRERLDDLcTRLQMTSTKEQVDEVTDLL---ASFTSLSL--Q 292
Cdd:PLN03192 616 isdphaaGDLLCTAAKRNDLT----AMKELL-KQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLImngADVDKANTddD 689

                        170
                 ....*....|...
gi 564361019 293 MQSMEKRAPLGQE 305
Cdd:PLN03192 690 FSPTELRELLQKR 702
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 141-213 3.39e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 42.53  E-value: 3.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 141 KGRTALHFASCNGNDQIVQLLLDHGAD-----------PNQQDG---LGNTPLHLAACTNHVPVITTLLRGGARVDAL-- 204
Cdd:cd22195  136 RGQTALHIAIERRCKHYVELLVEKGADvhaqargrffqPKDEGGyfyFGELPLSLAACTNQPDIVHYLTENAHKKADLrr 215

                         90
                 ....*....|
gi 564361019 205 -DRAGRTPLH 213
Cdd:cd22195  216 qDSRGNTVLH 225
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 116-167 4.28e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 4.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564361019 116 SANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGAD 167
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 119-215 4.94e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 4.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 119 ANDIetVQQLLEDGADpcaaddkgrTALHFASCNGNDqIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGG 198
Cdd:PHA02874  80 AHDI--IKLLIDNGVD---------TSILPIPCIEKD-MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG 147

                         90
                 ....*....|....*..
gi 564361019 199 ARVDALDRAGRTPLHLA 215
Cdd:PHA02874 148 ADVNIEDDNGCYPIHIA 164
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 115-215 4.94e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 4.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 115 DSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTL 194
Cdd:PHA02875   8 DAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87

                         90       100
                 ....*....|....*....|..
gi 564361019 195 LRGGARV-DALDRAGRTPLHLA 215
Cdd:PHA02875  88 LDLGKFAdDVFYKDGMTPLHLA 109
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 175-203 5.77e-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: 36.80  E-value: 5.77e-04
                           10        20
                   ....*....|....*....|....*....
gi 564361019   175 GNTPLHLAACTNHVPVITTLLRGGARVDA 203
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 97-213 1.25e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019  97 HRRLGPTGKEVHALKRLRDSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQI--VQLLLDHGADPNQQ-DG 173
Cdd:PHA02946  60 HRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKINNSvDE 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564361019 174 LGNTPlhLAACTNHVP-VITTLLRGGARVDALDRAGRTPLH 213
Cdd:PHA02946 140 EGCGP--LLACTDPSErVFKKIMSIGFEARIVDKFGKNHIH 178
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 122-164 2.28e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 2.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 564361019 122 IETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLLDH 164
Cdd:PTZ00322 128 VQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 121-182 3.62e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.09  E-value: 3.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564361019 121 DIETVQQLLEDGADPCAADD-KGRTALHFAScnGNDQIVQLLLDHGADPNQQDGLGNTPLHLA 182
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02791 PHA02791
ankyrin-like protein; Provisional
 113-162 4.32e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.48  E-value: 4.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564361019 113 LRDSANANDIETVQQLLEDGADPCAADDKGRTALHFASCNGNDQIVQLLL 162
Cdd:PHA02791  65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFV 114
PHA02791 PHA02791
ankyrin-like protein; Provisional
 134-239 6.35e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 37.71  E-value: 6.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564361019 134 DPCAADDKGRTALHFASCNGNDQIVQLLLDHGADPNQQDglGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLH 213
Cdd:PHA02791  22 DAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALY 99

                         90       100
                 ....*....|....*....|....*.
gi 564361019 214 LAKSKLNilqeghsqcLEAVRLEVKQ 239
Cdd:PHA02791 100 YAVDSGN---------MQTVKLFVKK 116
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 157-221 7.33e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.12  E-value: 7.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564361019 157 IVQLLLDHGADPNQQDGLGNTPLHLAACTNHVPVITTLLRGGARVDALDRAGRTPLHLAKSKLNI 221
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224
PHA02741 PHA02741
hypothetical protein; Provisional
 137-183 9.14e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 36.56  E-value: 9.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564361019 137 AADDKGRTALHFASCNGNDQ----IVQLLLDHGADPNQQDGL-GNTPLHLAA 183
Cdd:PHA02741  55 ATDDAGQMCIHIAAEKHEAQlaaeIIDHLIELGADINAQEMLeGDTALHLAA 106
 
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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