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Conserved domains on  [gi|50897294|ref|NP_001002920|]
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POTE ankyrin domain family member A isoform 1 [Homo sapiens]

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];
63-232 1.48e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 1.48e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  63 REDLGKLHRAAWWGEVPRADLIVMLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQC 142
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294 143 QEDECALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKA 222
Cdd:COG0666 131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                       170
                ....*....|
gi 50897294 223 NLNALDRFGR 232
Cdd:COG0666 211 DVNAKDNDGK 220
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
63-232 1.48e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 1.48e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  63 REDLGKLHRAAWWGEVPRADLIVMLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQC 142
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294 143 QEDECALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKA 222
Cdd:COG0666 131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                       170
                ....*....|
gi 50897294 223 NLNALDRFGR 232
Cdd:COG0666 211 DVNAKDNDGK 220
Ank_2 pfam12796
Ankyrin repeats (3 copies);
103-195 9.27e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 9.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   103 LHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQHGtDPNLPDmYGNTALHYAVYNEDKLMAK 182
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 50897294   183 TLLLYGADIESKN 195
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 84-230 2.63e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 2.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   84 IVMLRGPGINKRDKKKRTALHLACAN--GNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECAL------------ 149
Cdd:PHA03100  91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKIlkllidkgvdin 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  150 ------MLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKAN 223
Cdd:PHA03100 171 aknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                 ....*..
gi 50897294  224 LNALDRF 230
Cdd:PHA03100 251 IKTIIET 257
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 101-231 4.02e-08

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: 55.40  E-value: 4.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294 101 TALHLACANGNSEVVS-LLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQhgTDP---NLP---DMY-GNTALHYA 172
Cdd:cd22192  19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPelvNEPmtsDLYqGETALHIA 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50897294 173 VYNEDKLMAKTLLLYGADIES---------KNKGGLT-----PLLLAVHGQKQRMVKFLIKKKANLNALDRFG 231
Cdd:cd22192  97 VVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 101-221 1.05e-05

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: 47.77  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   101 TALHLACANGNSEVVSLLLDRQCQLHV------FDSKKRTAL-------IKAVQC--QEDECALmLLQHGTDPNLPDMYG 165
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDSfyhgespLNAAAClgSPSIVAL-LSEDPADILTADSLG 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50897294   166 NTALHYAVYNED------KL---MAKTLLLYGADIESK-------NKGGLTPLLLAVHGQKQRMVKFLIKKK 221
Cdd:TIGR00870 209 NTLLHLLVMENEfkaeyeELscqMYNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKLAIK 280
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 164-192 4.76e-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: 37.18  E-value: 4.76e-04
                           10        20
                   ....*....|....*....|....*....
gi 50897294    164 YGNTALHYAVYNEDKLMAKTLLLYGADIE 192
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
63-232 1.48e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 1.48e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  63 REDLGKLHRAAWWGEVPRADLIVMLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQC 142
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294 143 QEDECALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKA 222
Cdd:COG0666 131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                       170
                ....*....|
gi 50897294 223 NLNALDRFGR 232
Cdd:COG0666 211 DVNAKDNDGK 220
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
69-231 8.62e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 8.62e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  69 LHRAAWWGEVPRADLIVmLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECA 148
Cdd:COG0666  91 LHAAARNGDLEIVKLLL-EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294 149 LMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKANLNALD 228
Cdd:COG0666 170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249


                ...
gi 50897294 229 RFG 231
Cdd:COG0666 250 KDG 252
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
65-232 2.84e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.13  E-value: 2.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  65 DLGKLHRAAWWGEVPRADLIVMLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQE 144
Cdd:COG0666  20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294 145 DECALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKANL 224
Cdd:COG0666 100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179


                ....*...
gi 50897294 225 NALDRFGR 232
Cdd:COG0666 180 NARDNDGE 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
69-233 2.26e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 2.26e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  69 LHRAAWWGEVPRADLIVmLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECA 148
Cdd:COG0666 124 LHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294 149 LMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKANLNALD 228
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282


                ....*
gi 50897294 229 RFGRI 233
Cdd:COG0666 283 LDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
103-195 9.27e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 9.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   103 LHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQHGtDPNLPDmYGNTALHYAVYNEDKLMAK 182
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 50897294   183 TLLLYGADIESKN 195
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-232 1.00e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.16  E-value: 1.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  92 INKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQHGTDPNLPDMYGNTALHY 171
Cdd:COG0666  14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50897294 172 AVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKANLNALDRFGR 232
Cdd:COG0666  94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN 154
Ank_2 pfam12796
Ankyrin repeats (3 copies);
69-162 1.97e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 1.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294    69 LHRAAWWGEVPRADLIVMlRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHvfDSKKRTALIKAVQCQEDECA 148
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE-NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 50897294   149 LMLLQHGTDPNLPD 162
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 84-230 2.63e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 2.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   84 IVMLRGPGINKRDKKKRTALHLACAN--GNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECAL------------ 149
Cdd:PHA03100  91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKIlkllidkgvdin 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  150 ------MLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKAN 223
Cdd:PHA03100 171 aknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                 ....*..
gi 50897294  224 LNALDRF 230
Cdd:PHA03100 251 IKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 88-234 4.77e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 4.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   88 RGPGINKRDKKKRTALH--LACANGNSEVVSLLLDRQCQLHVFDSKKRTAL-IKAVQCQEDECAL-MLLQHGTDPNLPDM 163
Cdd:PHA03095 141 KGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhHHLQSFKPRARIVrELIRAGCDPAATDM 220

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50897294  164 YGNTALHY-AVYNEDK--LMAKtLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKANLNALDRFGRIC 234
Cdd:PHA03095 221 LGNTPLHSmATGSSCKrsLVLP-LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTP 293
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 89-228 5.17e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 5.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   89 GPGINKRDKKK-RTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQHGTDPNLPDMYGNT 167
Cdd:PHA02878 157 GADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50897294  168 ALHYAV-YNEDKLMAKTLLLYGADIESKNK-GGLTPLLLAVHgqKQRMVKFLIKKKANLNALD 228
Cdd:PHA02878 237 PLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLN 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
 79-232 2.15e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   79 PRADLIVMLR----GPGINKRDKKKRTALHLACANGNS---EVVSLLLDRqcqlhvfdskkrtalikavqcqedecalml 151
Cdd:PHA03095  23 SNVTVEEVRRllaaGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEA------------------------------ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  152 lqhGTDPNLPDMYGNTALHYAVYNEDKL-MAKTLLLYGADIESKNKGGLTPLLLAVHGQ--KQRMVKFLIKKKANLNALD 228
Cdd:PHA03095  73 ---GADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALD 149


                 ....
gi 50897294  229 RFGR 232
Cdd:PHA03095 150 LYGM 153
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 80-234 2.65e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 2.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   80 RADLIVML--RGPGINKRDKKKRTALHLAC-----ANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALM-- 150
Cdd:PHA03100  47 NIDVVKILldNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVey 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  151 LLQHGTDPNLPDMYGNTALHYAV-YNEDKL-MAKTLLL----------------YGADIESKNKGGLTPLLLAVHGQKQR 212
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLeSNKIDLkILKLLIDkgvdinaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPE 206

                        170       180
                 ....*....|....*....|..
gi 50897294  213 MVKFLIKKKANLNALDRFGRIC 234
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTP 228
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 96-226 2.80e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 2.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   96 DKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQ--HGTDPNLpdmyGNTALHYAV 173
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaSISDPHA----AGDLLCTAA 630

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 50897294  174 YNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKANLNA 226
Cdd:PLN03192 631 KRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 84-230 3.99e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 3.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   84 IVMLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFD-----------------------------SKKRT 134
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlddlsvlecavdsknidtikaiidnrsniNKNDL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  135 ALIKAVQCQEDECALMLLQHGTDPNLPDMYGNTALHYAVYNE--DKLMAKtLLLYGADIESKNKGGLTPL-LLAVHGQKQ 211
Cdd:PHA02876 243 SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPslSRLVPK-LLERGADVNAKNIKGETPLyLMAKNGYDT 321

                        170
                 ....*....|....*....
gi 50897294  212 RMVKFLIKKKANLNALDRF 230
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRL 340
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 69-230 4.75e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 4.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   69 LHRAAWWGEVPRADLIVMLRGPGINKRDKKKRTALHLACANG-NSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQED-E 146
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkD 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  147 CALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRM-VKFLIKKKANLN 225
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436


                 ....*
gi 50897294  226 ALDRF 230
Cdd:PHA02876 437 SKNKD 441
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 69-225 4.82e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.24  E-value: 4.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   69 LHRAAWWGEVPRADLIVMLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECA 148
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50897294  149 LMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGG-LTPLLLAVHGQKQRMVKFLIKKKANLN 225
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 88-231 9.50e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 9.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   88 RGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVF-----------------------DSKKRTALIKAVQCQ- 143
Cdd:PHA02878  59 RGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFytlvaikdafnnrnveifkiiltNRYKNIQTIDLVYIDk 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  144 -------EDECALMLLQHGTDPNLPDMY-GNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVK 215
Cdd:PHA02878 139 kskddiiEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVH 218

                        170
                 ....*....|....*.
gi 50897294  216 FLIKKKANLNALDRFG 231
Cdd:PHA02878 219 ILLENGASTDARDKCG 234
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 89-206 2.57e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.29  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   89 GPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQHGTDPNLPDMYGNTA 168
Cdd:PHA02874 114 GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 50897294  169 LHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAV 206
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI 231
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 85-206 3.02e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 3.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   85 VMLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAV-QCQEDECALMLLQHGTDPNLPD- 162
Cdd:PHA02878 187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSy 266

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 50897294  163 MYGNTALHYAVYNEDKLmaKTLLLYGADIESKNKGGLTPLLLAV 206
Cdd:PHA02878 267 ILGLTALHSSIKSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 84-231 5.73e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 5.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   84 IVMLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQ---------------------- 141
Cdd:PHA02874  20 IIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKigahdiikllidngvdtsilpi 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  142 -CQEDECALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKK 220
Cdd:PHA02874 100 pCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179

                        170
                 ....*....|.
gi 50897294  221 KANLNALDRFG 231
Cdd:PHA02874 180 GAYANVKDNNG 190
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 100-244 1.25e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  100 RTALHLACANGNSEVVSLLLDRQCQLH-VFDSKKRTALIKAVQCQEDECALMLLQHGTDPNLPDMYGNTALHYAVYNEDK 178
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50897294  179 LMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKANLNALDRFGRICQLLSDYKENQ 244
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNK 214
Ank_2 pfam12796
Ankyrin repeats (3 copies);
169-228 1.30e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.04  E-value: 1.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   169 LHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIkKKANLNALD 228
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD 59
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-245 1.44e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.57  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   89 GPGINKRDKKKRTALH--LACANGNSEVVSLLLDRQCQLHVFDSKKRT---ALIKAVQCqEDECALMLLQHGTDPNLPDM 163
Cdd:PHA03095 107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLKSRNA-NVELLRLLIDAGADVYAVDD 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  164 YGNTALHY-AVY---NEDKLmaKTLLLYGADIESKNKGGLTPL-LLAVHGQKQR-MVKFLIKKKANLNALDRFGRICQLL 237
Cdd:PHA03095 186 RFRSLLHHhLQSfkpRARIV--RELIRAGCDPAATDMLGNTPLhSMATGSSCKRsLVLPLLIAGISINARNRYGQTPLHY 263


                 ....*...
gi 50897294  238 SDYKENQM 245
Cdd:PHA03095 264 AAVFNNPR 271
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 101-231 4.02e-08

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: 55.40  E-value: 4.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294 101 TALHLACANGNSEVVS-LLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQhgTDP---NLP---DMY-GNTALHYA 172
Cdd:cd22192  19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPelvNEPmtsDLYqGETALHIA 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50897294 173 VYNEDKLMAKTLLLYGADIES---------KNKGGLT-----PLLLAVHGQKQRMVKFLIKKKANLNALDRFG 231
Cdd:cd22192  97 VVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
165-218 7.52e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 7.52e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 50897294   165 GNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLI 218
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 143-228 1.21e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  143 QEDE--CALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKK 220
Cdd:PHA02876 154 QQDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233


                 ....*...
gi 50897294  221 KANLNALD 228
Cdd:PHA02876 234 RSNINKND 241
Ank_4 pfam13637
Ankyrin repeats (many copies);
133-185 3.68e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 3.68e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 50897294   133 RTALIKAVQCQEDECALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLL 185
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 112-226 3.69e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  112 SEVVSLLLDRQCQLHVFDSKK-RTALIKAVQCQEDECALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGAD 190
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 50897294  191 IESKNKGGLTPLLLAVHGQKQ-RMVKFLIKKKANLNA 226
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNA 263
Ank_5 pfam13857
Ankyrin repeats (many copies);
151-205 6.19e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 6.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 50897294   151 LLQHGT-DPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLA 205
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 101-221 9.93e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 9.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294 101 TALHLACANGNSEVVSLLLDRQCQLH------VFDSKKRTALIK--------AVQCQEDECALMLLQHGTDPNLPDMYGN 166
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50897294 167 TALHYAVYNEDKLMAKTL--LLYGADIES--------KNKGGLTPLLLAVHGQKQRMVKFLIKKK 221
Cdd:cd22192 171 TVLHILVLQPNKTFACQMydLILSYDKEDdlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 111-224 1.91e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  111 NSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGAD 190
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110
                 ....*....|....*....|....*....|....
gi 50897294  191 IESKNKGGLTPLLLAVHGQKQRMVKFLIKKKANL 224
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 148-273 3.06e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  148 ALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIkkkanlnal 227
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS--------- 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 50897294  228 drfgRICQLLSDYKENQMPNNSSGNSNPEQDLKLTSEEE-----PQRLKGS 273
Cdd:PTZ00322 169 ----RHSQCHFELGANAKPDSFTGKPPSLEDSPISSHHPdfsavPQPMMGS 215
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 69-206 3.34e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   69 LHRAAWWGEVPRADLIVMLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECA 148
Cdd:PHA02876 345 LHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMS 424

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  149 L-MLLQHGTDPNLPDMYGNTALHYAVYNEDKL-MAKTLLLYGADIESKNKGGLTPLLLAV 206
Cdd:PHA02876 425 VkTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPLLIAL 484
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 100-243 6.70e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 6.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  100 RTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQHGTDPNL--PDMY------------- 164
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVkyPDIEselhdaveegdvk 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  165 -------------------GNTALHYAVYNEDKLMAKTLLLYGADIESKNKGGLTPLLLAVHGQKQRMVKFLIKKKANLN 225
Cdd:PHA02875  83 aveelldlgkfaddvfykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                        170       180       190
                 ....*....|....*....|....*....|.
gi 50897294  226 ALDRFG-------------RICQLLSDYKEN 243
Cdd:PHA02875 163 IEDCCGctpliiamakgdiAICKMLLDSGAN 193
Ank_5 pfam13857
Ankyrin repeats (many copies);
117-172 8.09e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 8.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 50897294   117 LLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQHGTDPNLPDMYGNTALHYA 172
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 98-221 8.82e-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: 47.95  E-value: 8.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  98 KKRTALHLACANGNSEVVSLLLDRQCQLHV------FDSKKRTA-------LIKAVQCQEDECALMLLQHGTDP---NLP 161
Cdd:cd21882  72 QGQTALHIAIENRNLNLVRLLVENGADVSAratgrfFRKSPGNLfyfgelpLSLAACTNQEEIVRLLLENGAQPaalEAQ 151

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50897294 162 DMYGNTALHYAVYNEDKL---------MAKTLLLYGADI-------ESKNKGGLTPLLLAVHGQKQRMVKFLIKKK 221
Cdd:cd21882 152 DSLGNTVLHALVLQADNTpensafvcqMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 101-221 1.05e-05

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: 47.77  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   101 TALHLACANGNSEVVSLLLDRQCQLHV------FDSKKRTAL-------IKAVQC--QEDECALmLLQHGTDPNLPDMYG 165
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDSfyhgespLNAAAClgSPSIVAL-LSEDPADILTADSLG 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50897294   166 NTALHYAVYNED------KL---MAKTLLLYGADIESK-------NKGGLTPLLLAVHGQKQRMVKFLIKKK 221
Cdd:TIGR00870 209 NTLLHLLVMENEfkaeyeELscqMYNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKLAIK 280
Ank_4 pfam13637
Ankyrin repeats (many copies);
69-119 1.55e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 1.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 50897294    69 LHRAAWWGEVpraDLIVMLRGPG--INKRDKKKRTALHLACANGNSEVVSLLL 119
Cdd:pfam13637   5 LHAAAASGHL---ELLRLLLEKGadINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-139 2.38e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 2.38e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 50897294    92 INKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKA 139
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 164-196 3.08e-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: 40.74  E-value: 3.08e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 50897294   164 YGNTALHYAVYNEDKL-MAKTLLLYGADIESKNK 196
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 83-255 2.08e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   83 LIVMLRGPGINKRDKKKRTALHLACANG---NSEVVSLLLDRQCQLHVFDSKKRTALIKAVQ--CQED-ECALMLLQHGT 156
Cdd:PHA02798  93 KILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQsnHHIDiEIIKLLLEKGV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  157 DPNL-PDMYGNTALH-YAVYN---------------------EDKLMAKTLLLY---------------------GADIE 192
Cdd:PHA02798 173 DINThNNKEKYDTLHcYFKYNidridadilklfvdngfiinkENKSHKKKFMEYlnsllydnkrfkknildfifsYIDIN 252

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50897294  193 SKNKGGLTPLLLAVHGQKQRMVKFLIKKKANLNALDRFGRICQLLSDYKENQMPNNSSGNSNP 255
Cdd:PHA02798 253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKP 315
PHA02946 PHA02946
ankyin-like protein; Provisional
 103-232 2.76e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.12  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294  103 LHLACA--NGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQHGTDPNLPDMYGNTALHYAVYNEDKLM 180
Cdd:PHA02946  41 LHAYCGikGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVI 120

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 50897294  181 AKTLLL--YGADI-ESKNKGGLTPlLLAVHGQKQRMVKFLIKKKANLNALDRFGR 232
Cdd:PHA02946 121 ERINLLvqYGAKInNSVDEEGCGP-LLACTDPSERVFKKIMSIGFEARIVDKFGK 174
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 100-127 3.04e-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: 38.01  E-value: 3.04e-04
                          10        20
                  ....*....|....*....|....*...
gi 50897294   100 RTALHLACANGNSEVVSLLLDRQCQLHV 127
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 92-241 3.10e-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: 43.15  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294    92 INKRDKKKRTAL-HLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQHGTDPNLPDMY------ 164
Cdd:TIGR00870  45 INCPDRLGRSALfVAAIENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLELANdqytse 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   165 ---GNTALHYAVYNEDKLMAKTLLLYGADIESKNKG--------------GLTPLLLAVHGQKQRMVKFLIKKKANLNAL 227
Cdd:TIGR00870 125 ftpGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTA 204

                         170
                  ....*....|....*...
gi 50897294   228 DRFG----RICQLLSDYK 241
Cdd:TIGR00870 205 DSLGntllHLLVMENEFK 222
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 164-192 4.76e-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: 37.18  E-value: 4.76e-04
                           10        20
                   ....*....|....*....|....*....
gi 50897294    164 YGNTALHYAVYNEDKLMAKTLLLYGADIE 192
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 84-154 8.11e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.81  E-value: 8.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50897294   84 IVMLRGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQCQEDECALMLLQH 154
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 82-230 9.07e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 9.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294   82 DLIVML--RGPGINKRDKKKRTALHLACANGNSEVVSLLLDRQCQLHVFDSKKRTALIKAVQcqEDECALMLLQHGTDPN 159
Cdd:PHA02874 171 DIIKLLleKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASIN 248

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50897294  160 LPDMYGNTALHYAV-YNEDKLMAKTLLLYGADIESKNKGGLTPLLLAV-HGQKQRMVKFLIKKKANLNALDRF 230
Cdd:PHA02874 249 DQDIDGSTPLHHAInPPCDIDIIDILLYHKADISIKDNKGENPIDTAFkYINKDPVIKDIIANAVLIKEADKL 321
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 164-191 1.04e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|....*...
gi 50897294   164 YGNTALHYAVYNEDKLMAKTLLLYGADI 191
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 100-121 2.00e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.00e-03
                           10        20
                   ....*....|....*....|..
gi 50897294    100 RTALHLACANGNSEVVSLLLDR 121
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDK 24
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 198-229 2.00e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 2.00e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 50897294   198 GLTPLLLAV-HGQKQRMVKFLIKKKANLNALDR 229
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 133-228 2.72e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.25  E-value: 2.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50897294 133 RTALIKAV---QCQEDECALMLLQHGTDPNLPDMY-----------GNTALHYAVYNEDKLMAKTLLLYGADIESKNKG- 197
Cdd:cd21882  27 KTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARATGr 106

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 50897294 198 ------------GLTPLLLAVHGQKQRMVKFLIKKKANLNALD 228
Cdd:cd21882 107 ffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALE 149
 
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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