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Protein

Transient receptor potential cation channel subfamily V member 5

Gene

Trpv5

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Constitutively active calcium selective cation channel thought to be involved in Ca2+ reabsorption in kidney and intestine. The channel is activated by low internal calcium level and the current exhibits an inward rectification. A Ca2+-dependent feedback regulation includes fast channel inactivation and slow current decay. Heteromeric assembly with TRPV6 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating.1 Publication

Enzyme regulationi

Activated by WNK3.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Calmodulin-binding

Protein family/group databases

TCDBi1.A.4.2.3. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily V member 5
Short name:
TrpV5
Alternative name(s):
Epithelial calcium channel 1
Short name:
ECaC1
Osm-9-like TRP channel 3
Short name:
OTRPC3
Gene namesi
Name:Trpv5
Synonyms:Ecac1
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 7

Subcellular locationi

  • Apical cell membrane By similarity; Multi-pass membrane protein By similarity

  • Note: Colocalized with S100A10 and ANAX2 along the apical domain of kidney distal tubular cells. The expression of the glycosylated form in the cell membrane is increased in the presence of WNK3 (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 327327CytoplasmicSequence analysisAdd
BLAST
Transmembranei328 – 34821HelicalSequence analysisAdd
BLAST
Topological domaini349 – 38739ExtracellularSequence analysisAdd
BLAST
Transmembranei388 – 40821HelicalSequence analysisAdd
BLAST
Topological domaini409 – 41911CytoplasmicSequence analysisAdd
BLAST
Transmembranei420 – 44021HelicalSequence analysisAdd
BLAST
Topological domaini441 – 4488ExtracellularSequence analysis
Transmembranei449 – 46921HelicalSequence analysisAdd
BLAST
Topological domaini470 – 49223CytoplasmicSequence analysisAdd
BLAST
Transmembranei493 – 51321HelicalSequence analysisAdd
BLAST
Intramembranei524 – 54421Pore-formingCuratedAdd
BLAST
Transmembranei557 – 57721HelicalSequence analysisAdd
BLAST
Topological domaini578 – 730153CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi535 – 5351E → A: Minor effects on Ca(2+) permeation. 1 Publication
Mutagenesisi542 – 5421D → A: Abolishes Ca(2+) permeation and Ca(2+)-dependent current decay; no effect on monovalent cations permeation. 1 Publication
Mutagenesisi542 – 5421D → E, N or M: Attenuates Ca(2+) permeation and Ca(2+)-dependent current decay. 1 Publication
Mutagenesisi542 – 5421D → K: Abolishes channel activity. 1 Publication
Mutagenesisi550 – 5501D → A: Minor effects on Ca(2+) permeation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 730730Transient receptor potential cation channel subfamily V member 5PRO_0000215352Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence analysis
Modified residuei685 – 6851PhosphothreonineBy similarity
Modified residuei689 – 6891PhosphoserineBy similarity

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

PTM databases

iPTMnetiQ9XSM3.

Interactioni

Subunit structurei

Homotetramer and probably heterotetramer with TRPV6. Interacts with TRPV6. Interacts with S100A10 and probably with the ANAX2-S100A10 heterotetramer. The interaction with S100A10 is required for the trafficking to the plasma membrane. Interacts with calmodulin. Interacts with BSPRY, which results in its inactivation (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-46154N.
STRINGi9986.ENSOCUP00000006536.

Structurei

3D structure databases

ProteinModelPortaliQ9XSM3.
SMRiQ9XSM3. Positions 44-266.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati44 – 7431ANK 1Add
BLAST
Repeati78 – 10730ANK 2Add
BLAST
Repeati116 – 14530ANK 3Add
BLAST
Repeati162 – 19130ANK 4Add
BLAST
Repeati239 – 26830ANK 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni598 – 6025Interaction with S100A10By similarity
Regioni650 – 6534Involved in Ca(2+)-dependent inactivation
Regioni701 – 73030Involved in Ca(2+)-dependent inactivationAdd
BLAST

Sequence similaritiesi

Contains 5 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3676. Eukaryota.
ENOG4110DG4. LUCA.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234397.
HOVERGENiHBG061442.
InParanoidiQ9XSM3.
KOiK04974.
OMAiVNLPFMF.
OrthoDBiEOG70087C.
TreeFamiTF314711.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008346. TRPV5.
IPR008344. TRPV5/TRPV6.
[Graphical view]
PANTHERiPTHR10582:SF11. PTHR10582:SF11. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
PR01765. ECACCHANNEL.
PR01767. ECACCHANNEL2.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9XSM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGACPPKAKG PWAQLQKLLI SWPVGEQDWE QYRDRVNMLQ QERIRDSPLL
60 70 80 90 100
QAAKENDLRL LKILLLNQSC DFQQRGAVGE TALHVAALYD NLEAATLLME
110 120 130 140 150
AAPELAKEPA LCEPFVGQTA LHIAVMNQNL NLVRALLARG ASVSARATGA
160 170 180 190 200
AFRRSPHNLI YYGEHPLSFA ACVGSEEIVR LLIEHGADIR AQDSLGNTVL
210 220 230 240 250
HILILQPNKT FACQMYNLLL SYDEHSDHLQ SLELVPNHQG LTPFKLAGVE
260 270 280 290 300
GNTVMFQHLM QKRKHVQWTC GPLTSTLYDL TEIDSWGEEL SFLELVVSSK
310 320 330 340 350
KREARQILEQ TPVKELVSFK WKKYGRPYFC VLASLYILYM ICFTTCCIYR
360 370 380 390 400
PLKLRDDNRT DPRDITILQQ KLLQEAYVTH QDNIRLVGEL VTVTGAVIIL
410 420 430 440 450
LLEIPDIFRV GASRYFGQTI LGGPFHVIII TYASLVLLTM VMRLTNMNGE
460 470 480 490 500
VVPLSFALVL GWCSVMYFAR GFQMLGPFTI MIQKMIFGDL MRFCWLMAVV
510 520 530 540 550
ILGFASAFHI TFQTEDPNNL GEFSDYPTAL FSTFELFLTI IDGPANYSVD
560 570 580 590 600
LPFMYCITYA AFAIIATLLM LNLFIAMMGD THWRVAQERD ELWRAQVVAT
610 620 630 640 650
TVMLERKMPR FLWPRSGICG YEYGLGDRWF LRVENHHDQN PLRVLRYVEA
660 670 680 690 700
FKCSDKEDGQ EQLSEKRPST VESGMLSRAS VAFQTPSLSR TTSQSSNSHR
710 720 730
GWEILRRNTL GHLNLGLDLG EGDGEEVYHF
Length:730
Mass (Da):82,814
Last modified:November 1, 1999 - v1
Checksum:i0CB9FBAD916B1400
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133128 mRNA. Translation: CAB40138.1.
RefSeqiNP_001076126.1. NM_001082657.1.
UniGeneiOcu.3235.

Genome annotation databases

EnsembliENSOCUT00000007559; ENSOCUP00000006536; ENSOCUG00000007559.
GeneIDi100009364.
KEGGiocu:100009364.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133128 mRNA. Translation: CAB40138.1.
RefSeqiNP_001076126.1. NM_001082657.1.
UniGeneiOcu.3235.

3D structure databases

ProteinModelPortaliQ9XSM3.
SMRiQ9XSM3. Positions 44-266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46154N.
STRINGi9986.ENSOCUP00000006536.

Protein family/group databases

TCDBi1.A.4.2.3. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

iPTMnetiQ9XSM3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000007559; ENSOCUP00000006536; ENSOCUG00000007559.
GeneIDi100009364.
KEGGiocu:100009364.

Organism-specific databases

CTDi56302.

Phylogenomic databases

eggNOGiKOG3676. Eukaryota.
ENOG4110DG4. LUCA.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234397.
HOVERGENiHBG061442.
InParanoidiQ9XSM3.
KOiK04974.
OMAiVNLPFMF.
OrthoDBiEOG70087C.
TreeFamiTF314711.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008346. TRPV5.
IPR008344. TRPV5/TRPV6.
[Graphical view]
PANTHERiPTHR10582:SF11. PTHR10582:SF11. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
PR01765. ECACCHANNEL.
PR01767. ECACCHANNEL2.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular identification of the apical Ca2+ channel in 1, 25-dihydroxyvitamin D3-responsive epithelia."
    Hoenderop J.G.J., van der Kemp A.W.C.M., Hartog A., van de Graaf S.F.J., van Os C.H., Willems P.H.G.M., Bindels R.J.M.
    J. Biol. Chem. 274:8375-8378(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: New Zealand white.
    Tissue: Kidney.
  2. "The single pore residue Asp542 determines Ca2+ permeation and Mg2+ block of the epithelial Ca2+ channel."
    Nilius B., Vennekens R., Prenen J., Hoenderop J.G., Droogmans G., Bindels R.J.M.
    J. Biol. Chem. 276:1020-1025(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF CHANNEL PORE, MUTAGENESIS OF GLU-535; ASP-542 AND ASP-550.
  3. "Homo- and heterotetrameric architecture of the epithelial Ca2+ channels TRPV5 and TRPV6."
    Hoenderop J.G., Voets T., Hoefs S., Weidema F., Prenen J., Nilius B., Bindels R.J.M.
    EMBO J. 22:776-785(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, GLYCOSYLATION.
  4. "The carboxyl terminus of the epithelial Ca(2+) channel ECaC1 is involved in Ca(2+)-dependent inactivation."
    Nilius B., Weidema F., Prenen J., Hoenderop J.G., Vennekens R., Hoefs S., Droogmans G., Bindels R.J.M.
    Pflugers Arch. 445:584-588(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.

Entry informationi

Entry nameiTRPV5_RABIT
AccessioniPrimary (citable) accession number: Q9XSM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1999
Last modified: June 8, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.