Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9NQA5 (TRPV5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transient receptor potential cation channel subfamily V member 5

Short name=TrpV5
Alternative name(s):
Calcium transport protein 2
Short name=CaT2
Epithelial calcium channel 1
Short name=ECaC
Short name=ECaC1
Osm-9-like TRP channel 3
Short name=OTRPC3
Gene names
Name:TRPV5
Synonyms:ECAC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. Ref.2

Enzyme regulation

Activated by WNK3. Ref.7

Subunit structure

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.

Subcellular location

Apical cell membrane; Multi-pass membrane protein. Note: Colocalized with S100A10 and ANAX2 along the apical domain of kidney distal tubular cells By similarity. The expression of the glycosylated form in the cell membrane is increased in the presence of WNK3. Ref.7

Tissue specificity

Expressed at high levels in kidney, small intestine and pancreas, and at lower levels in testis, prostate, placenta, brain, colon and rectum. Ref.1 Ref.2

Post-translational modification

Glycosylated. Ref.7

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV5 sub-subfamily. [View classification]

Contains 5 ANK repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CALB1P059374EBI-1053443,EBI-4286943

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 729729Transient receptor potential cation channel subfamily V member 5
PRO_0000215350

Regions

Topological domain1 – 327327Cytoplasmic Potential
Transmembrane328 – 34821Helical; Potential
Topological domain349 – 38739Extracellular Potential
Transmembrane388 – 40821Helical; Potential
Topological domain409 – 41911Cytoplasmic Potential
Transmembrane420 – 44021Helical; Potential
Topological domain441 – 4488Extracellular Potential
Transmembrane449 – 46921Helical; Potential
Topological domain470 – 49223Cytoplasmic Potential
Transmembrane493 – 51321Helical; Potential
Intramembrane524 – 54421Pore-forming; Probable
Transmembrane557 – 57721Helical; Potential
Topological domain578 – 729152Cytoplasmic Potential
Repeat44 – 7431ANK 1
Repeat78 – 10730ANK 2
Repeat116 – 14530ANK 3
Repeat162 – 19130ANK 4
Repeat239 – 26830ANK 5
Region598 – 6025Interaction with S100A10 By similarity
Region650 – 6534Involved in Ca(2+)-dependent inactivation By similarity
Region700 – 72930Involved in Ca(2+)-dependent inactivation By similarity

Amino acid modifications

Glycosylation3581N-linked (GlcNAc...) Ref.7

Natural variations

Natural variant81A → V. Ref.4
Corresponds to variant rs4252372 [ dbSNP | Ensembl ].
VAR_022247
Natural variant1541R → H. Ref.3 Ref.4
Corresponds to variant rs4236480 [ dbSNP | Ensembl ].
VAR_022248
Natural variant5631A → T. Ref.4
Corresponds to variant rs4252499 [ dbSNP | Ensembl ].
VAR_022249
Natural variant7121L → F. Ref.4
Corresponds to variant rs4252509 [ dbSNP | Ensembl ].
VAR_022250

Experimental info

Mutagenesis3581N → Q: Loss of glycosylation. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q9NQA5 [UniParc].

Last modified March 1, 2002. Version 2.
Checksum: A10FB80205FD0DBB

FASTA72982,551
        10         20         30         40         50         60 
MGGFLPKAEG PGSQLQKLLP SFLVREQDWD QHLDKLHMLQ QKRILESPLL RASKENDLSV 

        70         80         90        100        110        120 
LRQLLLDCTC DVRQRGALGE TALHIAALYD NLEAALVLME AAPELVFEPT TCEAFAGQTA 

       130        140        150        160        170        180 
LHIAVVNQNV NLVRALLTRR ASVSARATGT AFRRSPRNLI YFGEHPLSFA ACVNSEEIVR 

       190        200        210        220        230        240 
LLIEHGADIR AQDSLGNTVL HILILQPNKT FACQMYNLLL SYDGHGDHLQ PLDLVPNHQG 

       250        260        270        280        290        300 
LTPFKLAGVE GNTVMFQHLM QKRRHIQWTY GPLTSILYDL TEIDSWGEEL SFLELVVSSD 

       310        320        330        340        350        360 
KREARQILEQ TPVKELVSFK WNKYGRPYFC ILAALYLLYM ICFTTCCVYR PLKFRGGNRT 

       370        380        390        400        410        420 
HSRDITILQQ KLLQEAYETR EDIIRLVGEL VSIVGAVIIL LLEIPDIFRV GASRYFGKTI 

       430        440        450        460        470        480 
LGGPFHVIII TYASLVLVTM VMRLTNTNGE VVPMSFALVL GWCSVMYFTR GFQMLGPFTI 

       490        500        510        520        530        540 
MIQKMIFGDL MRFCWLMAVV ILGFASAFYI IFQTEDPTSL GQFYDYPMAL FTTFELFLTV 

       550        560        570        580        590        600 
IDAPANYDVD LPFMFSIVNF AFAIIATLLM LNLFIAMMGD THWRVAQERD ELWRAQVVAT 

       610        620        630        640        650        660 
TVMLERKLPR CLWPRSGICG CEFGLGDRWF LRVENHNDQN PLRVLRYVEV FKNSDKEDDQ 

       670        680        690        700        710        720 
EHPSEKQPSG AESGTLARAS LALPTSSLSR TASQSSSHRG WEILRQNTLG HLNLGLNLSE 


GDGEEVYHF 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, tissue distribution, and chromosomal mapping of the human epithelial calcium channel (ECAC1)."
Mueller D., Hoenderop J.G., Meij I.C., van den Heuvel L.P.J., Knoers N.V., den Hollander A.I., Eggert P., Garcia-Nieto V., Claverie-Martin F., Bindels R.J.M.
Genomics 67:48-53(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"Structural conservation of the genes encoding CaT1, CaT2, and related cation channels."
Peng J.-B., Brown E.M., Hediger M.A.
Genomics 76:99-109(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[3]Kelsell R.E.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-154.
[4]SeattleSNPs variation discovery resource
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-8; HIS-154; THR-563 AND PHE-712.
[5]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"WNK3 positively regulates epithelial calcium channels TRPV5 and TRPV6 via a kinase-dependent pathway."
Zhang W., Na T., Peng J.B.
Am. J. Physiol. 295:F1472-F1484(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-358, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF ASN-358.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ271207 mRNA. Translation: CAB96365.2.
AF304464 mRNA. Translation: AAL04015.1.
AJ487965 mRNA. Translation: CAD32312.2.
AY206695 Genomic DNA. Translation: AAO13488.1.
CH236959 Genomic DNA. Translation: EAL23777.1.
CH471198 Genomic DNA. Translation: EAW51896.1.
CCDSCCDS5875.1.
RefSeqNP_062815.2. NM_019841.5.
UniGeneHs.283369.

3D structure databases

ProteinModelPortalQ9NQA5.
SMRQ9NQA5. Positions 8-614.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121137. 3 interactions.
IntActQ9NQA5. 1 interaction.
MINTMINT-1470011.
STRING9606.ENSP00000265310.

Chemistry

ChEMBLCHEMBL1628474.
GuidetoPHARMACOLOGY511.

Protein family/group databases

TCDB1.A.4.2.10. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSiteQ9NQA5.

Polymorphism databases

DMDM62901471.

Proteomic databases

PaxDbQ9NQA5.
PRIDEQ9NQA5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265310; ENSP00000265310; ENSG00000127412.
ENST00000566839; ENSP00000457041; ENSG00000261264.
GeneID56302.
KEGGhsa:56302.
UCSCuc003wby.1. human.

Organism-specific databases

CTD56302.
GeneCardsGC07M142606.
HGNCHGNC:3145. TRPV5.
MIM606679. gene.
neXtProtNX_Q9NQA5.
PharmGKBPA35045.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278734.
HOGENOMHOG000234397.
HOVERGENHBG061442.
InParanoidQ9NQA5.
KOK04974.
OMALCEPFVG.
PhylomeDBQ9NQA5.
TreeFamTF314711.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9NQA5.
BgeeQ9NQA5.
CleanExHS_TRPV5.
GenevestigatorQ9NQA5.

Family and domain databases

Gene3D1.25.40.20. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008346. TRPV5.
IPR008344. TRPV5/TRPV6.
[Graphical view]
PANTHERPTHR10582:SF11. PTHR10582:SF11. 1 hit.
PfamPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
PR01765. ECACCHANNEL.
PR01767. ECACCHANNEL2.
SMARTSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
TIGRFAMsTIGR00870. trp. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiTRPV5.
GenomeRNAi56302.
NextBio61971.
PROQ9NQA5.
SOURCESearch...

Entry information

Entry nameTRPV5_HUMAN
AccessionPrimary (citable) accession number: Q9NQA5
Secondary accession number(s): A4D2H7 expand/collapse secondary AC list , Q8NDW5, Q8NDX7, Q8NDX8, Q96PM6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM