Q9UL62 (TRPC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	973 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Calcium transport Ion transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	ANK repeat Repeat Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Calcium channel Ionic channel
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	axon guidance Traceable author statement. Source: Reactome
Cellular component	calcium channel complex Inferred from direct assay Ref.11. Source: UniProtKB integral to plasma membrane Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction Ref.11. Source: UniProtKB store-operated calcium channel activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 973	973	Short transient receptor potential channel 5		PRO_0000215318
Regions
	Topological domain	1 – 330	330	Cytoplasmic Potential
	Transmembrane	331 – 351	21	Helical; Potential
	Topological domain	352 – 398	47	Extracellular Potential
	Transmembrane	399 – 419	21	Helical; Potential
	Topological domain	420 – 437	18	Cytoplasmic Potential
	Transmembrane	438 – 458	21	Helical; Potential
	Topological domain	459 – 470	12	Extracellular Potential
	Transmembrane	471 – 491	21	Helical; Potential
	Topological domain	492 – 512	21	Cytoplasmic Potential
	Transmembrane	513 – 533	21	Helical; Potential
	Topological domain	534 – 603	70	Extracellular Potential
	Transmembrane	604 – 624	21	Helical; Potential
	Topological domain	625 – 973	349	Cytoplasmic Potential
	Repeat	31 – 60	30	ANK 1
	Repeat	69 – 97	29	ANK 2
	Repeat	98 – 124	27	ANK 3
	Repeat	141 – 170	30	ANK 4
	Region	971 – 973	3	Essential for binding to NHERF PDZ domain By similarity
Amino acid modifications
	Glycosylation	461	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	702	1	R → H. Corresponds to variant rs36047478 [ dbSNP | Ensembl ].		VAR_052369

Sequences

	Sequence		Length	Mass (Da)
	Q9UL62 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: FBC8CBF17BE42166	FASTA	973	111,412
	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

References

	« Hide 'large scale' referencesShow '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: 10493832] [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. , 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: 15772651] [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. , 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: 15489334] [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: 9687496] [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: 12032305] [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: 15757897] [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: 15895247] [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: 16284075] [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: 17850865] [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: 20164195] [Abstract] Cited for: INTERACTION WITH SESTD1.
+	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.
IPI	IPI00007836.
RefSeq	NP_036603.1. NM_012471.2.
UniGene	Hs.657709.
3D structure databases
ProteinModelPortal	Q9UL62.
SMR	Q9UL62. Positions 36-167.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UL62. 1 interaction.
STRING	Q9UL62.
Protein family/group databases
TCDB	1.A.4.1.7. transient receptor potential Ca2+ channel (TRP-CC) family.
PTM databases
PhosphoSite	Q9UL62.
Polymorphism databases
DMDM	10720321.
Proteomic databases
PRIDE	Q9UL62.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262839; ENSP00000262839; ENSG00000072315.
GeneID	7224.
KEGG	hsa:7224.
UCSC	uc004epl.1. human.
Organism-specific databases
CTD	7224.
GeneCards	GC0XM111017.
H-InvDB	HIX0056125.
HGNC	HGNC:12337. TRPC5.
HPA	HPA000510.
MIM	300334. gene.
neXtProt	NX_Q9UL62.
PharmGKB	PA37010.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10918.
GeneTree	ENSGT00550000074237.
HOGENOM	HBG355804.
HOVERGEN	HBG068337.
InParanoid	Q9UL62.
OMA	PPLIRTM.
OrthoDB	EOG45MN4N.
PhylomeDB	Q9UL62.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology.
Gene expression databases
ArrayExpress	Q9UL62.
Bgee	Q9UL62.
CleanEx	HS_TRPC5.
Genevestigator	Q9UL62.
GermOnline	ENSG00000072315. Homo sapiens.
Family and domain databases
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR005821. Ion_trans. IPR013555. TRP_2. IPR004729. TRP_channel. IPR005461. TRPC5_channel. IPR002153. TRPC_channel. [Graphical view]
Gene3D	G3DSA:1.25.40.20. ANK. 1 hit.
KO	K04968.
Pfam	PF12796. Ank_2. 1 hit. PF00520. Ion_trans. 1 hit. PF08344. TRP_2. 1 hit. [Graphical view]
PRINTS	PR01097. TRNSRECEPTRP. PR01646. TRPCHANNEL5.
SMART	SM00248. ANK. 2 hits. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit.
TIGRFAMs	TIGR00870. Trp. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. False negative. PS50088. ANK_REPEAT. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	28291.
SOURCE	Search...

Entry information

Entry name

TRPC5_HUMAN

Accession

Primary (citable) accession number: Q9UL62
Secondary accession number(s): B2RP53 , O75233, Q5JXY8, Q9Y514

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.