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Conserved domains on  [gi|53832024|ref|NP_001005474|]
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NF-kappa-B inhibitor zeta isoform b [Homo sapiens]

Protein Classification

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

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
328-592 6.99e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 6.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 328 KLANISQDQFLSKDADGDTFLHIAVAQGRRALSYVLARKMNALHMLDikeHNGQSAFQVAVAANQHLIVQDLVNIGAQVN 407
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD---DGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 408 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelll 486
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLlLEAGA-------DVNAQDNDGNTPLHLAAANGN---------------------- 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 487 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYRltql 566
Cdd:COG0666 166 -----LEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAG---ADVNAKDNDGKTALDLAAENGNL---- 232

                       250       260
                ....*....|....*....|....*.
gi 53832024 567 DAVRLLMRKGADPSTRNLENEQPVHL 592
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLL 258
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
328-592 6.99e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 6.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 328 KLANISQDQFLSKDADGDTFLHIAVAQGRRALSYVLARKMNALHMLDikeHNGQSAFQVAVAANQHLIVQDLVNIGAQVN 407
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD---DGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 408 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelll 486
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLlLEAGA-------DVNAQDNDGNTPLHLAAANGN---------------------- 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 487 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYRltql 566
Cdd:COG0666 166 -----LEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAG---ADVNAKDNDGKTALDLAAENGNL---- 232

                       250       260
                ....*....|....*....|....*.
gi 53832024 567 DAVRLLMRKGADPSTRNLENEQPVHL 592
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLL 258
PHA03095 PHA03095
ankyrin-like protein; Provisional
 395-591 1.59e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  395 IVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQ----KGAvgsnqfvDLEATNYDGLTPLHCaviahnavvhel 470
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRllleAGA-------DVNAPERCGFTPLHL------------ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  471 qrnqqphspevqelLLKNKSLVDTIKCLIQMGAAVEAKDrKSGRTALH--LAAEEANLELIRLFLELPSClsfVNAKAYN 548
Cdd:PHA03095  90 --------------YLYNATTLDVIKLLIKAGADVNAKD-KVGRTPLHvyLSGFNINPKVIRLLLRKGAD---VNALDLY 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 53832024  549 GNTALHVAasLQYRLTQLDAVRLLMRKGADPSTRNLENEQPVH 591
Cdd:PHA03095 152 GMTPLAVL--LKSRNANVELLRLLIDAGADVYAVDDRFRSLLH 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
492-583 7.72e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 7.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024   492 VDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKaYNGNTALHVAASLQYrltqLDAVRL 571
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD----VNLK-DNGRTALHYAARSGH----LEIVKL 79

                          90
                  ....*....|..
gi 53832024   572 LMRKGADPSTRN 583
Cdd:pfam12796  80 LLEKGADINVKD 91
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 489-582 1.22e-04

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: 45.26  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 489 KSLVDTIKCLIQMGAAVEAKDRKSGRTALHLAA---EEANLELIRLFLEL----PSCLSFVNAKA----YNGNTALHVAA 557
Cdd:cd21882   2 EELLGLLECLRWYLTDSAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAapdsGNPKELVNAPCtdefYQGQTALHIAI 81

                        90       100
                ....*....|....*....|....*
gi 53832024 558 SLQyrltQLDAVRLLMRKGADPSTR 582
Cdd:cd21882  82 ENR----NLNLVRLLVENGADVSAR 102
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 421-587 3.56e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024   421 AEKGHSQVLQAIQKGAVGSNQfvdlEATNYDGLTPLHCAVIAHNavvhelqrNQqphspEVQELLLKNKSLVDTIKCLIQ 500
Cdd:TIGR00870  25 AERGDLASVYRDLEEPKKLNI----NCPDRLGRSALFVAAIENE--------NL-----ELTELLLNLSCRGAVGDTLLH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024   501 MGA-----AVEA-------KDRKS----------------GRTALHLAAEEANLELIRLFLE----LP---SCLSFVNAK 545
Cdd:TIGR00870  88 AISleyvdAVEAillhllaAFRKSgplelandqytseftpGITALHLAAHRQNYEIVKLLLErgasVParaCGDFFVKSQ 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 53832024   546 ----AYNGNTALHVAASlqyrLTQLDAVRLLMRKGADPSTR-NLENE 587
Cdd:TIGR00870 168 gvdsFYHGESPLNAAAC----LGSPSIVALLSEDPADILTAdSLGNT 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 513-534 9.31e-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: 34.10  E-value: 9.31e-03
                           10        20
                   ....*....|....*....|..
gi 53832024    513 GRTALHLAAEEANLELIRLFLE 534
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLD 23
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
328-592 6.99e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 6.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 328 KLANISQDQFLSKDADGDTFLHIAVAQGRRALSYVLARKMNALHMLDikeHNGQSAFQVAVAANQHLIVQDLVNIGAQVN 407
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD---DGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 408 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelll 486
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLlLEAGA-------DVNAQDNDGNTPLHLAAANGN---------------------- 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 487 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYRltql 566
Cdd:COG0666 166 -----LEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAG---ADVNAKDNDGKTALDLAAENGNL---- 232

                       250       260
                ....*....|....*....|....*.
gi 53832024 567 DAVRLLMRKGADPSTRNLENEQPVHL 592
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
328-592 3.26e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 3.26e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 328 KLANISQDQFLSKDADGDTFLHIAVAQGRRALSYVLARKMNALHMLDIKEHNGQSAFQVAVAANQHLIVQDLVNIGAQVN 407
Cdd:COG0666   2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 408 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelll 486
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLlLEAGA-------DVNARDKDGETPLHLAAYNGN---------------------- 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 487 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYrltqL 566
Cdd:COG0666 133 -----LEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAG---ADVNARDNDGETPLHLAAENGH----L 199

                       250       260
                ....*....|....*....|....*.
gi 53832024 567 DAVRLLMRKGADPSTRNLENEQPVHL 592
Cdd:COG0666 200 EIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
340-587 4.67e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.20  E-value: 4.67e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 340 KDADGDTFLHIAVAQGRR-ALSYVLARKMNalhmLDIKEHNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLH 418
Cdd:COG0666  83 KDDGGNTLLHAAARNGDLeIVKLLLEAGAD----VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 419 VCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelllknkslVDTIKC 497
Cdd:COG0666 159 LAAANGNLEIVKLlLEAGA-------DVNARDNDGETPLHLAAENGH---------------------------LEIVKL 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 498 LIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELpscLSFVNAKAYNGNTALHVAASLQYrltqLDAVRLLMRKGA 577
Cdd:COG0666 205 LLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEA---GADLNAKDKDGLTALLLAAAAGA----ALIVKLLLLALL 276

                       250
                ....*....|
gi 53832024 578 DPSTRNLENE 587
Cdd:COG0666 277 LLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
340-550 2.77e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 2.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 340 KDADGDTFLHIAVAQGRRAL-SYVLARKMNalhmLDIKEHNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLH 418
Cdd:COG0666 116 RDKDGETPLHLAAYNGNLEIvKLLLEAGAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 419 VCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNAvvhelqrnqqphspevqelllknkslvDTIKC 497
Cdd:COG0666 192 LAAENGHLEIVKLlLEAGA-------DVNAKDNDGKTALDLAAENGNL---------------------------EIVKL 237

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 53832024 498 LIQMGAAVEAKDRKsGRTALHLAAEEANLELIRLFLELPSCLSFVNAKAYNGN 550
Cdd:COG0666 238 LLEAGADLNAKDKD-GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 395-591 1.59e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  395 IVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQ----KGAvgsnqfvDLEATNYDGLTPLHCaviahnavvhel 470
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRllleAGA-------DVNAPERCGFTPLHL------------ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  471 qrnqqphspevqelLLKNKSLVDTIKCLIQMGAAVEAKDrKSGRTALH--LAAEEANLELIRLFLELPSClsfVNAKAYN 548
Cdd:PHA03095  90 --------------YLYNATTLDVIKLLIKAGADVNAKD-KVGRTPLHvyLSGFNINPKVIRLLLRKGAD---VNALDLY 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 53832024  549 GNTALHVAasLQYRLTQLDAVRLLMRKGADPSTRNLENEQPVH 591
Cdd:PHA03095 152 GMTPLAVL--LKSRNANVELLRLLIDAGADVYAVDDRFRSLLH 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
492-583 7.72e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 7.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024   492 VDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKaYNGNTALHVAASLQYrltqLDAVRL 571
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD----VNLK-DNGRTALHYAARSGH----LEIVKL 79

                          90
                  ....*....|..
gi 53832024   572 LMRKGADPSTRN 583
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 395-593 5.03e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 5.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  395 IVQDLVNIGAQVNTTDCWGRTPLHVCAEK--GHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAhnavvhelq 471
Cdd:PHA03100  88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYlLDNGA-------NVNIKNSDGENLLHLYLES--------- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  472 rnqqphspevqelllkNKSLVDTIKCLIQMGAAVEAKDRksgrtalhlaaeeanlelIRLFLELPSclsFVNAKAYNGNT 551
Cdd:PHA03100 152 ----------------NKIDLKILKLLIDKGVDINAKNR------------------VNYLLSYGV---PINIKDVYGFT 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 53832024  552 ALHVAASLQYrltqLDAVRLLMRKGADPSTRNLENEQPVHLV 593
Cdd:PHA03100 195 PLHYAVYNNN----PEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 370-592 1.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  370 LHMLDIKEHNGQSA-------FQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLHV-CAE---KGHSQVLQAIQKGAVG 438
Cdd:PHA02878  20 IEYIDHTENYSTSAslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIiCKEpnkLGMKEMIRSINKCSVF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  439 SNQFVDLEATNYDGLTplhcavIAHNAVVHELQRNQQPHSPEVQELLLKNKSLVDTIKCLIQMGAAVEAKDRKSGRTALH 518
Cdd:PHA02878 100 YTLVAIKDAFNNRNVE------IFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGNTALH 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53832024  519 LAAEEANLELIRLFLelpSCLSFVNAKAYNGNTALHVAASlQYRltqLDAVRLLMRKGADPSTRNLENEQPVHL 592
Cdd:PHA02878 174 YATENKDQRLTELLL---SYGANVNIPDKTNNSPLHHAVK-HYN---KPIVHILLENGASTDARDKCGNTPLHI 240
Ank_2 pfam12796
Ankyrin repeats (3 copies);
384-470 2.45e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024   384 FQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQKgavgsnqFVDLEATNYdGLTPLHCAVIA- 462
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-------HADVNLKDN-GRTALHYAARSg 72


                  ....*...
gi 53832024   463 HNAVVHEL 470
Cdd:pfam12796  73 HLEIVKLL 80
PHA03095 PHA03095
ankyrin-like protein; Provisional
 395-590 2.50e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  395 IVQDLVNIGAQVNTTDCWGRTPLHVCAeKG---HSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNAvvhel 470
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLHVYL-SGfniNPKVIRLlLRKGA-------DVNALDLYGMTPLAVLLKSRNA----- 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  471 qrnqqphSPEVQELLLK-----------NKSLVDT-----------IKCLIQMGAAVEAKDRkSGRTALHLAAEEANLEL 528
Cdd:PHA03095 166 -------NVELLRLLIDagadvyavddrFRSLLHHhlqsfkprariVRELIRAGCDPAATDM-LGNTPLHSMATGSSCKR 237

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53832024  529 IRLFLELPSCLSfVNAKAYNGNTALHVAASlqYRLTQldAVRLLMRKGADPSTRNLENEQPV 590
Cdd:PHA03095 238 SLVLPLLIAGIS-INARNRYGQTPLHYAAV--FNNPR--ACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
417-534 2.19e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 2.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024   417 LHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelllknkslVDTI 495
Cdd:pfam12796   1 LHLAAKNGNLELVKLlLENGA-------DANLQDKNGRTALHLAAKNGH---------------------------LEIV 46

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 53832024   496 KCLIQmgaAVEAKDRKSGRTALHLAAEEANLELIRLFLE 534
Cdd:pfam12796  47 KLLLE---HADVNLKDNGRTALHYAARSGHLEIVKLLLE 82
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 340-520 2.97e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.51  E-value: 2.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  340 KDADGDTFLHIAVAQGrralsyvlarKMNALHML-------DIKEHNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDCW 412
Cdd:PHA02874 120 KDAELKTFLHYAIKKG----------DLESIKMLfeygadvNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  413 GRTPLHVCAEKGHSQVLQAIQKGavGSNQFVDLEatnyDGLTPLHCAVIAHNAVVHELQRNQQPHSPEVQ-----ELLLK 487
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDH--GNHIMNKCK----NGFTPLHNAIIHNRSAIELLINNASINDQDIDgstplHHAIN 263

                        170       180       190
                 ....*....|....*....|....*....|...
gi 53832024  488 NKSLVDTIKCLIQMGAAVEAKDRKsGRTALHLA 520
Cdd:PHA02874 264 PPCDIDIIDILLYHKADISIKDNK-GENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 388-591 5.59e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 5.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  388 VAANQHLIVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQ-AIQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNA- 465
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNlLLSYGA-------DVNIIALDDLSVLECAVDSKNId 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  466 VVHELQRNQQPHSPEVQELL--LKNKSLvDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLEliRLFLELPSCLSFVN 543
Cdd:PHA02876 226 TIKAIIDNRSNINKNDLSLLkaIRNEDL-ETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSLS--RLVPKLLERGADVN 301

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 53832024  544 AKAYNGNTALHVAASLQYrltQLDAVRLLMRKGADPSTRNLENEQPVH 591
Cdd:PHA02876 302 AKNIKGETPLYLMAKNGY---DTENIRTLIMLGADVNAADRLYITPLH 346
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 395-591 2.31e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 2.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  395 IVQDLVNIGAQVNTTDCWGRTPLHVCAEKGH--SQVLQAIQKGAvgsnqfvDLEATNYDGLTPLHCAviahnavvHELQR 472
Cdd:PHA02876 289 LVPKLLERGADVNAKNIKGETPLYLMAKNGYdtENIRTLIMLGA-------DVNAADRLYITPLHQA--------STLDR 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  473 NQqphspevqelllknkslvDTIKCLIQMGAAVEAKDRKSgRTALHLAAEEANLELIRLFLELPSCLSFVNAKAyngNTA 552
Cdd:PHA02876 354 NK------------------DIVITLLELGANVNARDYCD-KTPIHYAAVRNNVVIINTLLDYGADIEALSQKI---GTA 411

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 53832024  553 LHVAAslqYRLTQLDAVRLLMRKGADPSTRNLENEQPVH 591
Cdd:PHA02876 412 LHFAL---CGTNPYMSVKTLIDRGANVNSKNKDLSTPLH 447
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 365-616 2.50e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  365 RKMNALHMLDIKEHNGQSAFQVAVAAN--------QHLIVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQKGA 436
Cdd:PLN03192 502 KELHDLNVGDLLGDNGGEHDDPNMASNlltvastgNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  437 VGsnqfVDLEATNydGLTPLHCAVIA-HNA---VVHELQRNQQPHSPEVQELLLKNKSLVDTIKCLIQMGAAVEAKDRKs 512
Cdd:PLN03192 582 CN----VHIRDAN--GNTALWNAISAkHHKifrILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQ- 654

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  513 GRTALHLAAEEANLELIRLFLElpsclsfvnakayngNTALHVAASLQYRLTQLDAVRLLMRKGADPSTRNLENEQPVHL 592
Cdd:PLN03192 655 GATALQVAMAEDHVDMVRLLIM---------------NGADVDKANTDDDFSPTELRELLQKRELGHSITIVDSVPADEP 719

                        250       260
                 ....*....|....*....|....
gi 53832024  593 VPDGPVGEQIRRILKGKSIQQRAP 616
Cdd:PLN03192 720 DLGRDGGSRPGRLQGTSSDNQCRP 743
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 493-591 3.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  493 DTIKCLIQMGAAVEAKDRKSgRTALHLAAEEANLELIRLFLELPSClsfVNAKAYNGNTALHVAAslqyRLTQLDAVRLL 572
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAI----KHNFFDIIKLL 176

                         90
                 ....*....|....*....
gi 53832024  573 MRKGADPSTRNLENEQPVH 591
Cdd:PHA02874 177 LEKGAYANVKDNNGESPLH 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
348-436 2.29e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024   348 LHIAVAQGRRALSYVLARKMNALHMLDikeHNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDcwGRTPLHVCAEKGHSQ 427
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD---KNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75

                          90
                  ....*....|
gi 53832024   428 VLQA-IQKGA 436
Cdd:pfam12796  76 IVKLlLEKGA 85
Ank_4 pfam13637
Ankyrin repeats (many copies);
413-464 7.23e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 7.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 53832024   413 GRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHN 464
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLlLEKGA-------DINAVDGNGETALHFAASNGN 46
Ank_4 pfam13637
Ankyrin repeats (many copies);
513-558 9.90e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 9.90e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 53832024   513 GRTALHLAAEEANLELIRLFLELPSClsfVNAKAYNGNTALHVAAS 558
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAAS 43
Ank_4 pfam13637
Ankyrin repeats (many copies);
382-430 2.17e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 2.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 53832024   382 SAFQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQ 430
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 362-578 2.81e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  362 VLARKMNALHMLDIKEHNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIqkgaVGSNQ 441
Cdd:PHA02875  17 IARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL----LDLGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  442 FVDlEATNYDGLTPLHCAVIAHNAVVHE--LQRNQQPHSPEVQE-----LLLKNKSlVDTIKCLIQMGAAVEAKDrKSGR 514
Cdd:PHA02875  93 FAD-DVFYKDGMTPLHLATILKKLDIMKllIARGADPDIPNTDKfsplhLAVMMGD-IKGIELLIDHKACLDIED-CCGC 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 53832024  515 TALHLAAEEANLELIRLFLELPSCLSFVNAkayNGNTALHVAASLQYRltqLDAVRLLMRKGAD 578
Cdd:PHA02875 170 TPLIIAMAKGDIAICKMLLDSGANIDYFGK---NGCVAALCYAIENNK---IDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 478-592 2.88e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  478 SPEVQELLLKNkslVDTIKCLIQMGAAVEAKdRKSGRTALHLAAEEANLELIRLFLELPSclsFVNAKAY-NGNTALHVA 556
Cdd:PHA02875  37 SPIKLAMKFRD---SEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEELLDLGK---FADDVFYkDGMTPLHLA 109

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 53832024  557 ASLQyrltQLDAVRLLMRKGADPSTRNLENEQPVHL 592
Cdd:PHA02875 110 TILK----KLDIMKLLIARGADPDIPNTDKFSPLHL 141
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 489-582 1.22e-04

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: 45.26  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 489 KSLVDTIKCLIQMGAAVEAKDRKSGRTALHLAA---EEANLELIRLFLEL----PSCLSFVNAKA----YNGNTALHVAA 557
Cdd:cd21882   2 EELLGLLECLRWYLTDSAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAapdsGNPKELVNAPCtdefYQGQTALHIAI 81

                        90       100
                ....*....|....*....|....*
gi 53832024 558 SLQyrltQLDAVRLLMRKGADPSTR 582
Cdd:cd21882  82 ENR----NLNLVRLLVENGADVSAR 102
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 548-583 1.66e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 1.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 53832024   548 NGNTALHVAAslqYRLTQLDAVRLLMRKGADPSTRN 583
Cdd:pfam00023   1 DGNTPLHLAA---GRRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 337-528 2.54e-04

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: 44.23  E-value: 2.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 337 FLSKDADGDTFLHIAVAQGRRALSYVLARKMNALhmldIKE------HNGQSAFQVAVaANQHL-IVQDLVNIGAQVNT- 408
Cdd:cd22192  44 LFQRGALGETALHVAALYDNLEAAVVLMEAAPEL----VNEpmtsdlYQGETALHIAV-VNQNLnLVRELIARGADVVSp 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 409 ----------TDC---WGRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAViahnavvheLQRNQ 474
Cdd:cd22192 119 ratgtffrpgPKNliyYGEHPLSFAACVGNEEIVRLlIEHGA-------DIRAQDSLGNTVLHILV---------LQPNK 182

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 53832024 475 QPhSPEVQELLL-----KNKSLVDTIKcliqmgaaveakdRKSGRTALHLAAEEANLEL 528
Cdd:cd22192 183 TF-ACQMYDLILsydkeDDLQPLDLVP-------------NNQGLTPFKLAAKEGNIVM 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 513-581 3.26e-04

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: 43.85  E-value: 3.26e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53832024 513 GRTALHLAAEEANLELIRLFLELPSCLSF--VNAKAYNGNTALHVAASLQyrltQLDAVRLLMRKGADPST 581
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEAAPELVNepMTSDLYQGETALHIAVVNQ----NLNLVRELIARGADVVS 117
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 473-581 4.32e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.21  E-value: 4.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 473 NQQPHSPEVQELLLKNKSLVDTIKCLIQmgAAVEAKDRKsGRTALHLAAEEANLELIRLFLE------LPSCLSFVNAKA 546
Cdd:cd22194 104 NINENTKEIVRILLAFAEENGILDRFIN--AEYTEEAYE-GQTALNIAIERRQGDIVKLLIAkgadvnAHAKGVFFNPKY 180

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 53832024 547 -----YNGNTALHVAASLQyrltQLDAVRLLMRKGADPST 581
Cdd:cd22194 181 khegfYFGETPLALAACTN----QPEIVQLLMEKESTDIT 216
Ank_2 pfam12796
Ankyrin repeats (3 copies);
339-410 4.47e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.71  E-value: 4.47e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53832024   339 SKDADGDTFLHIAVAQGRRALSYVLARKMNalhmLDIKEhNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTD 410
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 395-591 5.58e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 5.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  395 IVQDLVNIGAQVNttdcwgrtplHVCAEKGHSqVLQAIQkgaVGSNQFVDLEATNYDGLTPLHCAVIAHNAV--VHELQR 472
Cdd:PHA02874  50 IVELFIKHGADIN----------HINTKIPHP-LLTAIK---IGAHDIIKLLIDNGVDTSILPIPCIEKDMIktILDCGI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  473 NQQPHSPEVQELL---LKNKSLvDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsFVNAKAYNG 549
Cdd:PHA02874 116 DVNIKDAELKTFLhyaIKKGDL-ESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGA---YANVKDNNG 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 53832024  550 NTALHVAAslqyRLTQLDAVRLLMRKGADPSTRNLENEQPVH 591
Cdd:PHA02874 191 ESPLHNAA----EYGDYACIKLLIDHGNHIMNKCKNGFTPLH 228
PHA03095 PHA03095
ankyrin-like protein; Provisional
 376-534 7.68e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 7.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  376 KEHNGQSAFqvavaaNQHL--------IVQDLVNIGAQVNTTDCWGRTPLHVCAEKG---HSQVLQAIQKGavgsnqfVD 444
Cdd:PHA03095 183 VDDRFRSLL------HHHLqsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAG-------IS 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024  445 LEATNYDGLTPLHCAVIAhnavvhelqrnqqphspevqelllKNKSLVDtikCLIQMGAAVEAKDRkSGRTALHLAAEEA 524
Cdd:PHA03095 250 INARNRYGQTPLHYAAVF------------------------NNPRACR---RLIALGADINAVSS-DGNTPLSLMVRNN 301

                        170
                 ....*....|
gi 53832024  525 NLELIRLFLE 534
Cdd:PHA03095 302 NGRAVRAALA 311
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 495-560 1.01e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.18  E-value: 1.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 53832024  495 IKCLIQMGAAVEAKDRKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKAYNG--NTALHVAASLQ 560
Cdd:PHA02743  76 IELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLG----VNLGAINYqhETAYHIAYKMR 139
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 344-472 1.09e-03

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: 41.92  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 344 GDTFLHIAVAQG---------RRALSYVLARKMNALHMLDIKE--HNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDCW 412
Cdd:cd22192  89 GETALHIAVVNQnlnlvreliARGADVVSPRATGTFFRPGPKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53832024 413 GRTPLHVCaekghsqVLQAIQKGA----------VGSNQFVDLE-ATNYDGLTPLHCAVIAHNAVV--HELQR 472
Cdd:cd22192 169 GNTVLHIL-------VLQPNKTFAcqmydlilsyDKEDDLQPLDlVPNNQGLTPFKLAAKEGNIVMfqHLVQK 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
542-593 2.98e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 2.98e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 53832024   542 VNAKAYNGNTALHVAASLQYrltqLDAVRLLMRKGADPSTRNLENEQPVHLV 593
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGA----LEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 421-587 3.56e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024   421 AEKGHSQVLQAIQKGAVGSNQfvdlEATNYDGLTPLHCAVIAHNavvhelqrNQqphspEVQELLLKNKSLVDTIKCLIQ 500
Cdd:TIGR00870  25 AERGDLASVYRDLEEPKKLNI----NCPDRLGRSALFVAAIENE--------NL-----ELTELLLNLSCRGAVGDTLLH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024   501 MGA-----AVEA-------KDRKS----------------GRTALHLAAEEANLELIRLFLE----LP---SCLSFVNAK 545
Cdd:TIGR00870  88 AISleyvdAVEAillhllaAFRKSgplelandqytseftpGITALHLAAHRQNYEIVKLLLErgasVParaCGDFFVKSQ 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 53832024   546 ----AYNGNTALHVAASlqyrLTQLDAVRLLMRKGADPSTR-NLENE 587
Cdd:TIGR00870 168 gvdsFYHGESPLNAAAC----LGSPSIVALLSEDPADILTAdSLGNT 210
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 413-555 8.33e-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: 39.09  E-value: 8.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 413 GRTPLHVCAEKGHSQVLQAIQ------KGAVGSNQFVDLEATN--YDGLTPLHCAVIAHNavvhelqrnqqphspevqel 484
Cdd:cd21882  26 GKTCLHKAALNLNDGVNEAIMllleaaPDSGNPKELVNAPCTDefYQGQTALHIAIENRN-------------------- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53832024 485 llknkslVDTIKCLIQMGAAVEAKD-----RKSGRTA-------LHLAAEEANLELIRLFLELPSCLSFVNAKAYNGNTA 552
Cdd:cd21882  86 -------LNLVRLLVENGADVSARAtgrffRKSPGNLfyfgelpLSLAACTNQEEIVRLLLENGAQPAALEAQDSLGNTV 158


                ...
gi 53832024 553 LHV 555
Cdd:cd21882 159 LHA 161
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 513-534 9.31e-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: 34.10  E-value: 9.31e-03
                           10        20
                   ....*....|....*....|..
gi 53832024    513 GRTALHLAAEEANLELIRLFLE 534
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLD 23
 
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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