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Conserved domains on  [gi|13899229|ref|NP_113607|]
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NF-kappa-B inhibitor zeta isoform a [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];
428-692 1.07e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 1.07e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 428 KLANISQDQFLSKDADGDTFLHIAVAQGRRALSYVLARKMNALHMLDikeHNGQSAFQVAVAANQHLIVQDLVNIGAQVN 507
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD---DGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 508 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelll 586
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLlLEAGA-------DVNAQDNDGNTPLHLAAANGN---------------------- 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 587 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYRltql 666
Cdd:COG0666 166 -----LEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAG---ADVNAKDNDGKTALDLAAENGNL---- 232

                       250       260
                ....*....|....*....|....*.
gi 13899229 667 DAVRLLMRKGADPSTRNLENEQPVHL 692
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLL 258
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
428-692 1.07e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 1.07e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 428 KLANISQDQFLSKDADGDTFLHIAVAQGRRALSYVLARKMNALHMLDikeHNGQSAFQVAVAANQHLIVQDLVNIGAQVN 507
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD---DGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 508 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelll 586
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLlLEAGA-------DVNAQDNDGNTPLHLAAANGN---------------------- 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 587 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYRltql 666
Cdd:COG0666 166 -----LEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAG---ADVNAKDNDGKTALDLAAENGNL---- 232

                       250       260
                ....*....|....*....|....*.
gi 13899229 667 DAVRLLMRKGADPSTRNLENEQPVHL 692
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLL 258
PHA03095 PHA03095
ankyrin-like protein; Provisional
 495-691 2.06e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  495 IVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQ----KGAvgsnqfvDLEATNYDGLTPLHCaviahnavvhel 570
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRllleAGA-------DVNAPERCGFTPLHL------------ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  571 qrnqqphspevqelLLKNKSLVDTIKCLIQMGAAVEAKDrKSGRTALH--LAAEEANLELIRLFLELPSClsfVNAKAYN 648
Cdd:PHA03095  90 --------------YLYNATTLDVIKLLIKAGADVNAKD-KVGRTPLHvyLSGFNINPKVIRLLLRKGAD---VNALDLY 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 13899229  649 GNTALHVAasLQYRLTQLDAVRLLMRKGADPSTRNLENEQPVH 691
Cdd:PHA03095 152 GMTPLAVL--LKSRNANVELLRLLIDAGADVYAVDDRFRSLLH 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
592-683 9.05e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 9.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229   592 VDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKaYNGNTALHVAASLQYrltqLDAVRL 671
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD----VNLK-DNGRTALHYAARSGH----LEIVKL 79

                          90
                  ....*....|..
gi 13899229   672 LMRKGADPSTRN 683
Cdd:pfam12796  80 LLEKGADINVKD 91
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 589-682 1.49e-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: 1.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 589 KSLVDTIKCLIQMGAAVEAKDRKSGRTALHLAA---EEANLELIRLFLEL----PSCLSFVNAKA----YNGNTALHVAA 657
Cdd:cd21882   2 EELLGLLECLRWYLTDSAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAapdsGNPKELVNAPCtdefYQGQTALHIAI 81

                        90       100
                ....*....|....*....|....*
gi 13899229 658 SLQyrltQLDAVRLLMRKGADPSTR 682
Cdd:cd21882  82 ENR----NLNLVRLLVENGADVSAR 102
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 521-687 4.31e-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: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229   521 AEKGHSQVLQAIQKGAVGSNQfvdlEATNYDGLTPLHCAVIAHNavvhelqrNQqphspEVQELLLKNKSLVDTIKCLIQ 600
Cdd:TIGR00870  25 AERGDLASVYRDLEEPKKLNI----NCPDRLGRSALFVAAIENE--------NL-----ELTELLLNLSCRGAVGDTLLH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229   601 MGA-----AVEA-------KDRKS----------------GRTALHLAAEEANLELIRLFLE----LP---SCLSFVNAK 645
Cdd:TIGR00870  88 AISleyvdAVEAillhllaAFRKSgplelandqytseftpGITALHLAAHRQNYEIVKLLLErgasVParaCGDFFVKSQ 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 13899229   646 ----AYNGNTALHVAASlqyrLTQLDAVRLLMRKGADPSTR-NLENE 687
Cdd:TIGR00870 168 gvdsFYHGESPLNAAAC----LGSPSIVALLSEDPADILTAdSLGNT 210
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
428-692 1.07e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 1.07e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 428 KLANISQDQFLSKDADGDTFLHIAVAQGRRALSYVLARKMNALHMLDikeHNGQSAFQVAVAANQHLIVQDLVNIGAQVN 507
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD---DGGNTLLHAAARNGDLEIVKLLLEAGADVN 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 508 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelll 586
Cdd:COG0666 115 ARDKDGETPLHLAAYNGNLEIVKLlLEAGA-------DVNAQDNDGNTPLHLAAANGN---------------------- 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 587 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYRltql 666
Cdd:COG0666 166 -----LEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLLLEAG---ADVNAKDNDGKTALDLAAENGNL---- 232

                       250       260
                ....*....|....*....|....*.
gi 13899229 667 DAVRLLMRKGADPSTRNLENEQPVHL 692
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
428-692 4.71e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 4.71e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 428 KLANISQDQFLSKDADGDTFLHIAVAQGRRALSYVLARKMNALHMLDIKEHNGQSAFQVAVAANQHLIVQDLVNIGAQVN 507
Cdd:COG0666   2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 508 TTDCWGRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelll 586
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLlLEAGA-------DVNARDKDGETPLHLAAYNGN---------------------- 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 587 knkslVDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPsclSFVNAKAYNGNTALHVAASLQYrltqL 666
Cdd:COG0666 133 -----LEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEAG---ADVNARDNDGETPLHLAAENGH----L 199

                       250       260
                ....*....|....*....|....*.
gi 13899229 667 DAVRLLMRKGADPSTRNLENEQPVHL 692
Cdd:COG0666 200 EIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
440-687 6.24e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.20  E-value: 6.24e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 440 KDADGDTFLHIAVAQGRR-ALSYVLARKMNalhmLDIKEHNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLH 518
Cdd:COG0666  83 KDDGGNTLLHAAARNGDLeIVKLLLEAGAD----VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 519 VCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelllknkslVDTIKC 597
Cdd:COG0666 159 LAAANGNLEIVKLlLEAGA-------DVNARDNDGETPLHLAAENGH---------------------------LEIVKL 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 598 LIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELpscLSFVNAKAYNGNTALHVAASLQYrltqLDAVRLLMRKGA 677
Cdd:COG0666 205 LLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEA---GADLNAKDKDGLTALLLAAAAGA----ALIVKLLLLALL 276

                       250
                ....*....|
gi 13899229 678 DPSTRNLENE 687
Cdd:COG0666 277 LLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
440-650 3.44e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 85.78  E-value: 3.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 440 KDADGDTFLHIAVAQGRRAL-SYVLARKMNalhmLDIKEHNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLH 518
Cdd:COG0666 116 RDKDGETPLHLAAYNGNLEIvKLLLEAGAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 519 VCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNAvvhelqrnqqphspevqelllknkslvDTIKC 597
Cdd:COG0666 192 LAAENGHLEIVKLlLEAGA-------DVNAKDNDGKTALDLAAENGNL---------------------------EIVKL 237

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 13899229 598 LIQMGAAVEAKDRKsGRTALHLAAEEANLELIRLFLELPSCLSFVNAKAYNGN 650
Cdd:COG0666 238 LLEAGADLNAKDKD-GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 495-691 2.06e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  495 IVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQ----KGAvgsnqfvDLEATNYDGLTPLHCaviahnavvhel 570
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRllleAGA-------DVNAPERCGFTPLHL------------ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  571 qrnqqphspevqelLLKNKSLVDTIKCLIQMGAAVEAKDrKSGRTALH--LAAEEANLELIRLFLELPSClsfVNAKAYN 648
Cdd:PHA03095  90 --------------YLYNATTLDVIKLLIKAGADVNAKD-KVGRTPLHvyLSGFNINPKVIRLLLRKGAD---VNALDLY 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 13899229  649 GNTALHVAasLQYRLTQLDAVRLLMRKGADPSTRNLENEQPVH 691
Cdd:PHA03095 152 GMTPLAVL--LKSRNANVELLRLLIDAGADVYAVDDRFRSLLH 192
Ank_2 pfam12796
Ankyrin repeats (3 copies);
592-683 9.05e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 9.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229   592 VDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKaYNGNTALHVAASLQYrltqLDAVRL 671
Cdd:pfam12796  10 LELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHAD----VNLK-DNGRTALHYAARSGH----LEIVKL 79

                          90
                  ....*....|..
gi 13899229   672 LMRKGADPSTRN 683
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 495-693 6.34e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  495 IVQDLVNIGAQVNTTDCWGRTPLHVCAEK--GHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAhnavvhelq 571
Cdd:PHA03100  88 IVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYlLDNGA-------NVNIKNSDGENLLHLYLES--------- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  572 rnqqphspevqelllkNKSLVDTIKCLIQMGAAVEAKDRksgrtalhlaaeeanlelIRLFLELPSclsFVNAKAYNGNT 651
Cdd:PHA03100 152 ----------------NKIDLKILKLLIDKGVDINAKNR------------------VNYLLSYGV---PINIKDVYGFT 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 13899229  652 ALHVAASLQYrltqLDAVRLLMRKGADPSTRNLENEQPVHLV 693
Cdd:PHA03100 195 PLHYAVYNNN----PEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 470-692 1.93e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.75  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  470 LHMLDIKEHNGQSA-------FQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLHV-CAE---KGHSQVLQAIQKGAVG 538
Cdd:PHA02878  20 IEYIDHTENYSTSAslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIiCKEpnkLGMKEMIRSINKCSVF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  539 SNQFVDLEATNYDGLTplhcavIAHNAVVHELQRNQQPHSPEVQELLLKNKSLVDTIKCLIQMGAAVEAKDRKSGRTALH 618
Cdd:PHA02878 100 YTLVAIKDAFNNRNVE------IFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGNTALH 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13899229  619 LAAEEANLELIRLFLelpSCLSFVNAKAYNGNTALHVAASlQYRltqLDAVRLLMRKGADPSTRNLENEQPVHL 692
Cdd:PHA02878 174 YATENKDQRLTELLL---SYGANVNIPDKTNNSPLHHAVK-HYN---KPIVHILLENGASTDARDKCGNTPLHI 240
Ank_2 pfam12796
Ankyrin repeats (3 copies);
484-570 2.87e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 2.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229   484 FQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQKgavgsnqFVDLEATNYdGLTPLHCAVIA- 562
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-------HADVNLKDN-GRTALHYAARSg 72


                  ....*...
gi 13899229   563 HNAVVHEL 570
Cdd:pfam12796  73 HLEIVKLL 80
PHA03095 PHA03095
ankyrin-like protein; Provisional
 495-690 3.15e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 3.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  495 IVQDLVNIGAQVNTTDCWGRTPLHVCAeKG---HSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNAvvhel 570
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLHVYL-SGfniNPKVIRLlLRKGA-------DVNALDLYGMTPLAVLLKSRNA----- 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  571 qrnqqphSPEVQELLLK-----------NKSLVDT-----------IKCLIQMGAAVEAKDRkSGRTALHLAAEEANLEL 628
Cdd:PHA03095 166 -------NVELLRLLIDagadvyavddrFRSLLHHhlqsfkprariVRELIRAGCDPAATDM-LGNTPLHSMATGSSCKR 237

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13899229  629 IRLFLELPSCLSfVNAKAYNGNTALHVAASlqYRLTQldAVRLLMRKGADPSTRNLENEQPV 690
Cdd:PHA03095 238 SLVLPLLIAGIS-INARNRYGQTPLHYAAV--FNNPR--ACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
517-634 2.57e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229   517 LHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNavvhelqrnqqphspevqelllknkslVDTI 595
Cdd:pfam12796   1 LHLAAKNGNLELVKLlLENGA-------DANLQDKNGRTALHLAAKNGH---------------------------LEIV 46

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 13899229   596 KCLIQmgaAVEAKDRKSGRTALHLAAEEANLELIRLFLE 634
Cdd:pfam12796  47 KLLLE---HADVNLKDNGRTALHYAARSGHLEIVKLLLE 82
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 440-620 3.70e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.51  E-value: 3.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  440 KDADGDTFLHIAVAQGrralsyvlarKMNALHML-------DIKEHNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDCW 512
Cdd:PHA02874 120 KDAELKTFLHYAIKKG----------DLESIKMLfeygadvNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  513 GRTPLHVCAEKGHSQVLQAIQKGavGSNQFVDLEatnyDGLTPLHCAVIAHNAVVHELQRNQQPHSPEVQ-----ELLLK 587
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDH--GNHIMNKCK----NGFTPLHNAIIHNRSAIELLINNASINDQDIDgstplHHAIN 263

                        170       180       190
                 ....*....|....*....|....*....|...
gi 13899229  588 NKSLVDTIKCLIQMGAAVEAKDRKsGRTALHLA 620
Cdd:PHA02874 264 PPCDIDIIDILLYHKADISIKDNK-GENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 488-691 6.98e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 6.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  488 VAANQHLIVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQ-AIQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHNA- 565
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNlLLSYGA-------DVNIIALDDLSVLECAVDSKNId 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  566 VVHELQRNQQPHSPEVQELL--LKNKSLvDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLEliRLFLELPSCLSFVN 643
Cdd:PHA02876 226 TIKAIIDNRSNINKNDLSLLkaIRNEDL-ETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSLS--RLVPKLLERGADVN 301

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 13899229  644 AKAYNGNTALHVAASLQYrltQLDAVRLLMRKGADPSTRNLENEQPVH 691
Cdd:PHA02876 302 AKNIKGETPLYLMAKNGY---DTENIRTLIMLGADVNAADRLYITPLH 346
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 495-691 2.88e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.91  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  495 IVQDLVNIGAQVNTTDCWGRTPLHVCAEKGH--SQVLQAIQKGAvgsnqfvDLEATNYDGLTPLHCAviahnavvHELQR 572
Cdd:PHA02876 289 LVPKLLERGADVNAKNIKGETPLYLMAKNGYdtENIRTLIMLGA-------DVNAADRLYITPLHQA--------STLDR 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  573 NQqphspevqelllknkslvDTIKCLIQMGAAVEAKDRKSgRTALHLAAEEANLELIRLFLELPSCLSFVNAKAyngNTA 652
Cdd:PHA02876 354 NK------------------DIVITLLELGANVNARDYCD-KTPIHYAAVRNNVVIINTLLDYGADIEALSQKI---GTA 411

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 13899229  653 LHVAAslqYRLTQLDAVRLLMRKGADPSTRNLENEQPVH 691
Cdd:PHA02876 412 LHFAL---CGTNPYMSVKTLIDRGANVNSKNKDLSTPLH 447
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 465-716 3.12e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  465 RKMNALHMLDIKEHNGQSAFQVAVAAN--------QHLIVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIQKGA 536
Cdd:PLN03192 502 KELHDLNVGDLLGDNGGEHDDPNMASNlltvastgNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  537 VGsnqfVDLEATNydGLTPLHCAVIA-HNA---VVHELQRNQQPHSPEVQELLLKNKSLVDTIKCLIQMGAAVEAKDRKs 612
Cdd:PLN03192 582 CN----VHIRDAN--GNTALWNAISAkHHKifrILYHFASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQ- 654

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  613 GRTALHLAAEEANLELIRLFLElpsclsfvnakayngNTALHVAASLQYRLTQLDAVRLLMRKGADPSTRNLENEQPVHL 692
Cdd:PLN03192 655 GATALQVAMAEDHVDMVRLLIM---------------NGADVDKANTDDDFSPTELRELLQKRELGHSITIVDSVPADEP 719

                        250       260
                 ....*....|....*....|....
gi 13899229  693 VPDGPVGEQIRRILKGKSIQQRAP 716
Cdd:PLN03192 720 DLGRDGGSRPGRLQGTSSDNQCRP 743
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 593-691 3.85e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  593 DTIKCLIQMGAAVEAKDRKSgRTALHLAAEEANLELIRLFLELPSClsfVNAKAYNGNTALHVAAslqyRLTQLDAVRLL 672
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAI----KHNFFDIIKLL 176

                         90
                 ....*....|....*....
gi 13899229  673 MRKGADPSTRNLENEQPVH 691
Cdd:PHA02874 177 LEKGAYANVKDNNGESPLH 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
448-536 2.68e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229   448 LHIAVAQGRRALSYVLARKMNALHMLDikeHNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDcwGRTPLHVCAEKGHSQ 527
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD---KNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75

                          90
                  ....*....|
gi 13899229   528 VLQA-IQKGA 536
Cdd:pfam12796  76 IVKLlLEKGA 85
Ank_4 pfam13637
Ankyrin repeats (many copies);
513-564 8.42e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 8.42e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 13899229   513 GRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAVIAHN 564
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLlLEKGA-------DINAVDGNGETALHFAASNGN 46
Ank_4 pfam13637
Ankyrin repeats (many copies);
613-658 1.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 13899229   613 GRTALHLAAEEANLELIRLFLELPSClsfVNAKAYNGNTALHVAAS 658
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAAS 43
Ank_4 pfam13637
Ankyrin repeats (many copies);
482-530 2.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 2.53e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 13899229   482 SAFQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQ 530
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 462-678 3.43e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  462 VLARKMNALHMLDIKEHNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDCWGRTPLHVCAEKGHSQVLQAIqkgaVGSNQ 541
Cdd:PHA02875  17 IARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL----LDLGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  542 FVDlEATNYDGLTPLHCAVIAHNAVVHE--LQRNQQPHSPEVQE-----LLLKNKSlVDTIKCLIQMGAAVEAKDrKSGR 614
Cdd:PHA02875  93 FAD-DVFYKDGMTPLHLATILKKLDIMKllIARGADPDIPNTDKfsplhLAVMMGD-IKGIELLIDHKACLDIED-CCGC 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13899229  615 TALHLAAEEANLELIRLFLELPSCLSFVNAkayNGNTALHVAASLQYRltqLDAVRLLMRKGAD 678
Cdd:PHA02875 170 TPLIIAMAKGDIAICKMLLDSGANIDYFGK---NGCVAALCYAIENNK---IDIVRLFIKRGAD 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 578-692 3.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  578 SPEVQELLLKNkslVDTIKCLIQMGAAVEAKdRKSGRTALHLAAEEANLELIRLFLELPSclsFVNAKAY-NGNTALHVA 656
Cdd:PHA02875  37 SPIKLAMKFRD---SEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEELLDLGK---FADDVFYkDGMTPLHLA 109

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 13899229  657 ASLQyrltQLDAVRLLMRKGADPSTRNLENEQPVHL 692
Cdd:PHA02875 110 TILK----KLDIMKLLIARGADPDIPNTDKFSPLHL 141
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 589-682 1.49e-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: 1.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 589 KSLVDTIKCLIQMGAAVEAKDRKSGRTALHLAA---EEANLELIRLFLEL----PSCLSFVNAKA----YNGNTALHVAA 657
Cdd:cd21882   2 EELLGLLECLRWYLTDSAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAapdsGNPKELVNAPCtdefYQGQTALHIAI 81

                        90       100
                ....*....|....*....|....*
gi 13899229 658 SLQyrltQLDAVRLLMRKGADPSTR 682
Cdd:cd21882  82 ENR----NLNLVRLLVENGADVSAR 102
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 648-683 1.79e-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: 1.79e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 13899229   648 NGNTALHVAAslqYRLTQLDAVRLLMRKGADPSTRN 683
Cdd:pfam00023   1 DGNTPLHLAA---GRRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 437-628 3.10e-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: 3.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 437 FLSKDADGDTFLHIAVAQGRRALSYVLARKMNALhmldIKE------HNGQSAFQVAVaANQHL-IVQDLVNIGAQVNT- 508
Cdd:cd22192  44 LFQRGALGETALHVAALYDNLEAAVVLMEAAPEL----VNEpmtsdlYQGETALHIAV-VNQNLnLVRELIARGADVVSp 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 509 ----------TDC---WGRTPLHVCAEKGHSQVLQA-IQKGAvgsnqfvDLEATNYDGLTPLHCAViahnavvheLQRNQ 574
Cdd:cd22192 119 ratgtffrpgPKNliyYGEHPLSFAACVGNEEIVRLlIEHGA-------DIRAQDSLGNTVLHILV---------LQPNK 182

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13899229 575 QPhSPEVQELLL-----KNKSLVDTIKcliqmgaaveakdRKSGRTALHLAAEEANLEL 628
Cdd:cd22192 183 TF-ACQMYDLILsydkeDDLQPLDLVP-------------NNQGLTPFKLAAKEGNIVM 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 613-681 3.98e-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: 3.98e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13899229 613 GRTALHLAAEEANLELIRLFLELPSCLSF--VNAKAYNGNTALHVAASLQyrltQLDAVRLLMRKGADPST 681
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEAAPELVNepMTSDLYQGETALHIAVVNQ----NLNLVRELIARGADVVS 117
Ank_2 pfam12796
Ankyrin repeats (3 copies);
439-510 5.24e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.71  E-value: 5.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13899229   439 SKDADGDTFLHIAVAQGRRALSYVLARKMNalhmLDIKEhNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTD 510
Cdd:pfam12796  25 LQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 573-681 5.27e-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: 5.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 573 NQQPHSPEVQELLLKNKSLVDTIKCLIQmgAAVEAKDRKsGRTALHLAAEEANLELIRLFLE------LPSCLSFVNAKA 646
Cdd:cd22194 104 NINENTKEIVRILLAFAEENGILDRFIN--AEYTEEAYE-GQTALNIAIERRQGDIVKLLIAkgadvnAHAKGVFFNPKY 180

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 13899229 647 -----YNGNTALHVAASLQyrltQLDAVRLLMRKGADPST 681
Cdd:cd22194 181 khegfYFGETPLALAACTN----QPEIVQLLMEKESTDIT 216
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 495-691 6.78e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  495 IVQDLVNIGAQVNttdcwgrtplHVCAEKGHSqVLQAIQkgaVGSNQFVDLEATNYDGLTPLHCAVIAHNAV--VHELQR 572
Cdd:PHA02874  50 IVELFIKHGADIN----------HINTKIPHP-LLTAIK---IGAHDIIKLLIDNGVDTSILPIPCIEKDMIktILDCGI 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  573 NQQPHSPEVQELL---LKNKSLvDTIKCLIQMGAAVEAKDrKSGRTALHLAAEEANLELIRLFLELPSclsFVNAKAYNG 649
Cdd:PHA02874 116 DVNIKDAELKTFLhyaIKKGDL-ESIKMLFEYGADVNIED-DNGCYPIHIAIKHNFFDIIKLLLEKGA---YANVKDNNG 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 13899229  650 NTALHVAAslqyRLTQLDAVRLLMRKGADPSTRNLENEQPVH 691
Cdd:PHA02874 191 ESPLHNAA----EYGDYACIKLLIDHGNHIMNKCKNGFTPLH 228
PHA03095 PHA03095
ankyrin-like protein; Provisional
 476-634 9.33e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.32  E-value: 9.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  476 KEHNGQSAFqvavaaNQHL--------IVQDLVNIGAQVNTTDCWGRTPLHVCAEKG---HSQVLQAIQKGavgsnqfVD 544
Cdd:PHA03095 183 VDDRFRSLL------HHHLqsfkprarIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAG-------IS 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229  545 LEATNYDGLTPLHCAVIAhnavvhelqrnqqphspevqelllKNKSLVDtikCLIQMGAAVEAKDRkSGRTALHLAAEEA 624
Cdd:PHA03095 250 INARNRYGQTPLHYAAVF------------------------NNPRACR---RLIALGADINAVSS-DGNTPLSLMVRNN 301

                        170
                 ....*....|
gi 13899229  625 NLELIRLFLE 634
Cdd:PHA03095 302 NGRAVRAALA 311
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 595-660 1.09e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.57  E-value: 1.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13899229  595 IKCLIQMGAAVEAKDRKSGRTALHLAAEEANLELIRLFLELPSclsfVNAKAYNG--NTALHVAASLQ 660
Cdd:PHA02743  76 IELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQLG----VNLGAINYqhETAYHIAYKMR 139
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 444-572 1.32e-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: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229 444 GDTFLHIAVAQG---------RRALSYVLARKMNALHMLDIKE--HNGQSAFQVAVAANQHLIVQDLVNIGAQVNTTDCW 512
Cdd:cd22192  89 GETALHIAVVNQnlnlvreliARGADVVSPRATGTFFRPGPKNliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13899229 513 GRTPLHVCaekghsqVLQAIQKGA----------VGSNQFVDLE-ATNYDGLTPLHCAVIAHNAVV--HELQR 572
Cdd:cd22192 169 GNTVLHIL-------VLQPNKTFAcqmydlilsyDKEDDLQPLDlVPNNQGLTPFKLAAKEGNIVMfqHLVQK 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
642-693 3.50e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13899229   642 VNAKAYNGNTALHVAASLQYrltqLDAVRLLMRKGADPSTRNLENEQPVHLV 693
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGA----LEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 521-687 4.31e-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: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229   521 AEKGHSQVLQAIQKGAVGSNQfvdlEATNYDGLTPLHCAVIAHNavvhelqrNQqphspEVQELLLKNKSLVDTIKCLIQ 600
Cdd:TIGR00870  25 AERGDLASVYRDLEEPKKLNI----NCPDRLGRSALFVAAIENE--------NL-----ELTELLLNLSCRGAVGDTLLH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13899229   601 MGA-----AVEA-------KDRKS----------------GRTALHLAAEEANLELIRLFLE----LP---SCLSFVNAK 645
Cdd:TIGR00870  88 AISleyvdAVEAillhllaAFRKSgplelandqytseftpGITALHLAAHRQNYEIVKLLLErgasVParaCGDFFVKSQ 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 13899229   646 ----AYNGNTALHVAASlqyrLTQLDAVRLLMRKGADPSTR-NLENE 687
Cdd:TIGR00870 168 gvdsFYHGESPLNAAAC----LGSPSIVALLSEDPADILTAdSLGNT 210
 
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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