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Q9UL62 (TRPC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 126. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Short transient receptor potential channel 5

Short name=TrpC5
Alternative name(s):
Transient receptor protein 5
Short name=TRP-5
Short name=hTRP-5
Short name=hTRP5
Gene names
Name:TRPC5
Synonyms:TRP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length973 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective By similarity. May also be activated by intracellular calcium store depletion. Ref.9

Enzyme regulation

Calcium channel activity is enhanced by MYLK, that promotes its subcellular localization at the plasma membrane. Ref.9

Subunit structure

Interacts with TRPC4AP By similarity. Homotetramer and heterotetramer with TRPC1 and/or TRPC4. Interacts with NHERF By similarity. Interacts with MX1 and RNF24. Interacts (via C-terminus) with CABP1. Interacts with SESTD1 (via the spectrin 1 repeat). Ref.6 Ref.7 Ref.8 Ref.10 Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.9.

Tissue specificity

Expressed in brain with higher levels in fetal brain. Found in cerebellum and occipital pole. Ref.5

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. STrpC subfamily. TRPC5 sub-subfamily. [View classification]

Contains 4 ANK repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 973973Short transient receptor potential channel 5
PRO_0000215318

Regions

Topological domain1 – 330330Cytoplasmic Potential
Transmembrane331 – 35121Helical; Potential
Topological domain352 – 39847Extracellular Potential
Transmembrane399 – 41921Helical; Potential
Topological domain420 – 43718Cytoplasmic Potential
Transmembrane438 – 45821Helical; Potential
Topological domain459 – 47012Extracellular Potential
Transmembrane471 – 49121Helical; Potential
Topological domain492 – 51221Cytoplasmic Potential
Transmembrane513 – 53321Helical; Potential
Topological domain534 – 60370Extracellular Potential
Transmembrane604 – 62421Helical; Potential
Topological domain625 – 973349Cytoplasmic Potential
Repeat31 – 6030ANK 1
Repeat69 – 9729ANK 2
Repeat98 – 12427ANK 3
Repeat141 – 17030ANK 4
Region971 – 9733Essential for binding to NHERF PDZ domain By similarity

Amino acid modifications

Glycosylation4611N-linked (GlcNAc...) Potential

Natural variations

Natural variant6671P → T Found in a patient with severe delayed speech, autism spectrum and Gilles de la Tourette disorders. Ref.12
VAR_069415
Natural variant7021R → H.
Corresponds to variant rs36047478 [ dbSNP | Ensembl ].
VAR_052369

Sequences

Sequence LengthMass (Da)Tools
Q9UL62 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: FBC8CBF17BE42166

FASTA973111,412
        10         20         30         40         50         60 
MAQLYYKKVN YSPYRDRIPL QIVRAETELS AEEKAFLNAV EKGDYATVKQ ALQEAEIYYN 

        70         80         90        100        110        120 
VNINCMDPLG RSALLIAIEN ENLEIMELLL NHSVYVGDAL LYAIRKEVVG AVELLLSYRR 

       130        140        150        160        170        180 
PSGEKQVPTL MMDTQFSEFT PDITPIMLAA HTNNYEIIKL LVQKRVTIPR PHQIRCNCVE 

       190        200        210        220        230        240 
CVSSSEVDSL RHSRSRLNIY KALASPSLIA LSSEDPILTA FRLGWELKEL SKVENEFKAE 

       250        260        270        280        290        300 
YEELSQQCKL FAKDLLDQAR SSRELEIILN HRDDHSEELD PQKYHDLAKL KVAIKYHQKE 

       310        320        330        340        350        360 
FVAQPNCQQL LATLWYDGFP GWRRKHWVVK LLTCMTIGFL FPMLSIAYLI SPRSNLGLFI 

       370        380        390        400        410        420 
KKPFIKFICH TASYLTFLFM LLLASQHIVR TDLHVQGPPP TVVEWMILPW VLGFIWGEIK 

       430        440        450        460        470        480 
EMWDGGFTEY IHDWWNLMDF AMNSLYLATI SLKIVAYVKY NGSRPREEWE MWHPTLIAEA 

       490        500        510        520        530        540 
LFAISNILSS LRLISLFTAN SHLGPLQISL GRMLLDILKF LFIYCLVLLA FANGLNQLYF 

       550        560        570        580        590        600 
YYETRAIDEP NNCKGIRCEK QNNAFSTLFE TLQSLFWSVF GLLNLYVTNV KARHEFTEFV 

       610        620        630        640        650        660 
GATMFGTYNV ISLVVLLNML IAMMNNSYQL IADHADIEWK FARTKLWMSY FDEGGTLPPP 

       670        680        690        700        710        720 
FNIIPSPKSF LYLGNWFNNT FCPKRDPDGR RRRRNLRSFT ERNADSLIQN QHYQEVIRNL 

       730        740        750        760        770        780 
VKRYVAAMIR NSKTHEGLTE ENFKELKQDI SSFRYEVLDL LGNRKHPRSF STSSTELSQR 

       790        800        810        820        830        840 
DDNNDGSGGA RAKSKSVSFN LGCKKKTCHG PPLIRTMPRS SGAQGKSKAE SSSKRSFMGP 

       850        860        870        880        890        900 
SLKKLGLLFS KFNGHMSEPS SEPMYTISDG IVQQHCMWQD IRYSQMEKGK AEACSQSEIN 

       910        920        930        940        950        960 
LSEVELGEVQ GAAQSSECPL ACSSSLHCAS SICSSNSKLL DSSEDVFETW GEACDLLMHK 

       970 
WGDGQEEQVT TRL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of TRPC5 (HTRP5), the human homologue of a mouse brain receptor-activated capacitative Ca(2+) entry channel."
Sossey-Alaoui K., Lyon J.A., Jones L., Abidi F.E., Hartung A.J., Hane B., Schwartz C.E., Stevenson R.E., Srivastava A.K.
Genomics 60:330-340(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fetal brain.
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"A novel capacitative calcium entry channel expressed in excitable cells."
Philipp S., Hambrecht J., Braslavski L., Schroth G., Freichel M., Murakami M., Cavalie A., Flockerzi V.
EMBO J. 17:4274-4282(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Subunit composition of mammalian transient receptor potential channels in living cells."
Hofmann T., Schaefer M., Schultz G., Gudermann T.
Proc. Natl. Acad. Sci. U.S.A. 99:7461-7466(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[7]"MxA, a member of the dynamin superfamily, interacts with the ankyrin-like repeat domain of TRPC."
Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N., St-Hilaire M., Pinard M., Boulay G.
J. Biol. Chem. 280:19393-19400(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MX1.
[8]"Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus oocytes."
Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K., Zhu M.X.
Pflugers Arch. 450:345-354(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CABP1.
[9]"Ca2+-calmodulin-dependent myosin light chain kinase is essential for activation of TRPC5 channels expressed in HEK293 cells."
Shimizu S., Yoshida T., Wakamori M., Ishii M., Okada T., Takahashi M., Seto M., Sakurada K., Kiuchi Y., Mori Y.
J. Physiol. (Lond.) 570:219-235(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS CALCIUM CHANNEL, ENZYME REGULATION, SUBCELLULAR LOCATION.
[10]"RNF24, a new TRPC interacting protein, causes the intracellular retention of TRPC."
Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.
Cell Calcium 43:432-443(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF24.
[11]"The phospholipid-binding protein SESTD1 is a novel regulator of the transient receptor potential channels TRPC4 and TRPC5."
Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.
J. Biol. Chem. 285:12426-12434(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SESTD1.
[12]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-667.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF054568 mRNA. Translation: AAF00002.1.
AC005191 Genomic DNA. Translation: AAC24563.1.
AL049563, AC005191 Genomic DNA. Translation: CAI43017.1.
CH471120 Genomic DNA. Translation: EAX02630.1.
BC137271 mRNA. Translation: AAI37272.1.
BC137274 mRNA. Translation: AAI37275.1.
CCDSCCDS14561.1.
RefSeqNP_036603.1. NM_012471.2.
UniGeneHs.657709.

3D structure databases

ProteinModelPortalQ9UL62.
SMRQ9UL62. Positions 35-170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113075. 17 interactions.
IntActQ9UL62. 1 interaction.
STRING9606.ENSP00000262839.

Chemistry

ChEMBLCHEMBL1250411.
GuidetoPHARMACOLOGY490.

Protein family/group databases

TCDB1.A.4.1.7. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSiteQ9UL62.

Polymorphism databases

DMDM10720321.

Proteomic databases

PaxDbQ9UL62.
PRIDEQ9UL62.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262839; ENSP00000262839; ENSG00000072315.
GeneID7224.
KEGGhsa:7224.
UCSCuc004epl.1. human.

Organism-specific databases

CTD7224.
GeneCardsGC0XM111017.
HGNCHGNC:12337. TRPC5.
HPAHPA000510.
MIM300334. gene.
neXtProtNX_Q9UL62.
PharmGKBPA37010.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG254238.
HOGENOMHOG000020589.
HOVERGENHBG068337.
InParanoidQ9UL62.
KOK04968.
OMAPPLIRTM.
OrthoDBEOG72G17P.
PhylomeDBQ9UL62.
TreeFamTF313147.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

BgeeQ9UL62.
CleanExHS_TRPC5.
GenevestigatorQ9UL62.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR013555. TRP_dom.
IPR005461. TRPC5_channel.
IPR002153. TRPC_channel.
[Graphical view]
PANTHERPTHR10117. PTHR10117. 1 hit.
PTHR10117:SF24. PTHR10117:SF24. 1 hit.
PfamPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08344. TRP_2. 1 hit.
[Graphical view]
PRINTSPR01097. TRNSRECEPTRP.
PR01646. TRPCHANNEL5.
SMARTSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
TIGRFAMsTIGR00870. trp. 1 hit.
ProtoNetSearch...

Other

GeneWikiTRPC5.
GenomeRNAi7224.
NextBio28291.
PROQ9UL62.
SOURCESearch...

Entry information

Entry nameTRPC5_HUMAN
AccessionPrimary (citable) accession number: Q9UL62
Secondary accession number(s): B2RP53 expand/collapse secondary AC list , O75233, Q5JXY8, Q9Y514
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 126 of the entry and version 1 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 X

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