ID   TRPC5_HUMAN             Reviewed;         973 AA.
AC   Q9UL62; B2RP53; O75233; Q5JXY8; Q9Y514;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Short transient receptor potential channel 5;
DE            Short=TrpC5;
DE   AltName: Full=Transient receptor protein 5;
DE            Short=TRP-5;
DE            Short=hTRP-5;
DE            Short=hTRP5;
GN   Name=TRPC5; Synonyms=TRP5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=10493832; DOI=10.1006/geno.1999.5924;
RA   Sossey-Alaoui K., Lyon J.A., Jones L., Abidi F.E., Hartung A.J., Hane B.,
RA   Schwartz C.E., Stevenson R.E., Srivastava A.K.;
RT   "Molecular cloning and characterization of TRPC5 (HTRP5), the human
RT   homologue of a mouse brain receptor-activated capacitative Ca(2+) entry
RT   channel.";
RL   Genomics 60:330-340(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=9687496; DOI=10.1093/emboj/17.15.4274;
RA   Philipp S., Hambrecht J., Braslavski L., Schroth G., Freichel M.,
RA   Murakami M., Cavalie A., Flockerzi V.;
RT   "A novel capacitative calcium entry channel expressed in excitable cells.";
RL   EMBO J. 17:4274-4282(1998).
RN   [6]
RP   SUBUNIT.
RX   PubMed=12032305; DOI=10.1073/pnas.102596199;
RA   Hofmann T., Schaefer M., Schultz G., Gudermann T.;
RT   "Subunit composition of mammalian transient receptor potential channels in
RT   living cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:7461-7466(2002).
RN   [7]
RP   INTERACTION WITH MX1.
RX   PubMed=15757897; DOI=10.1074/jbc.m500391200;
RA   Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N.,
RA   St-Hilaire M., Pinard M., Boulay G.;
RT   "MxA, a member of the dynamin superfamily, interacts with the ankyrin-like
RT   repeat domain of TRPC.";
RL   J. Biol. Chem. 280:19393-19400(2005).
RN   [8]
RP   INTERACTION WITH CABP1.
RX   PubMed=15895247; DOI=10.1007/s00424-005-1419-1;
RA   Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K., Zhu M.X.;
RT   "Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus
RT   oocytes.";
RL   Pflugers Arch. 450:345-354(2005).
RN   [9]
RP   FUNCTION AS CALCIUM CHANNEL, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=16284075; DOI=10.1113/jphysiol.2005.097998;
RA   Shimizu S., Yoshida T., Wakamori M., Ishii M., Okada T., Takahashi M.,
RA   Seto M., Sakurada K., Kiuchi Y., Mori Y.;
RT   "Ca2+-calmodulin-dependent myosin light chain kinase is essential for
RT   activation of TRPC5 channels expressed in HEK293 cells.";
RL   J. Physiol. (Lond.) 570:219-235(2006).
RN   [10]
RP   INTERACTION WITH RNF24.
RX   PubMed=17850865; DOI=10.1016/j.ceca.2007.07.009;
RA   Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.;
RT   "RNF24, a new TRPC interacting protein, causes the intracellular retention
RT   of TRPC.";
RL   Cell Calcium 43:432-443(2008).
RN   [11]
RP   INTERACTION WITH SESTD1.
RX   PubMed=20164195; DOI=10.1074/jbc.m109.068304;
RA   Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.;
RT   "The phospholipid-binding protein SESTD1 is a novel regulator of the
RT   transient receptor potential channels TRPC4 and TRPC5.";
RL   J. Biol. Chem. 285:12426-12434(2010).
RN   [12]
RP   INTERACTION WITH PLSCR1.
RX   PubMed=32110987; DOI=10.3390/cells9030547;
RA   Guo J., Li J., Xia L., Wang Y., Zhu J., Du J., Lu Y., Liu G., Yao X.,
RA   Shen B.;
RT   "Transient Receptor Potential Canonical 5-Scramblase Signaling Complex
RT   Mediates Neuronal Phosphatidylserine Externalization and Apoptosis.";
RL   Cells 9:0-0(2020).
RN   [13]
RP   VARIANT THR-667.
RX   PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA   de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA   Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA   del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA   Veltman J.A., Vissers L.E.;
RT   "Diagnostic exome sequencing in persons with severe intellectual
RT   disability.";
RL   N. Engl. J. Med. 367:1921-1929(2012).
CC   -!- FUNCTION: Thought to form a receptor-activated non-selective calcium
CC       permeant cation channel. Probably is operated by a phosphatidylinositol
CC       second messenger system activated by receptor tyrosine kinases or G-
CC       protein coupled receptors. Has also been shown to be calcium-selective
CC       (By similarity). May also be activated by intracellular calcium store
CC       depletion. Mediates calcium-dependent phosphatidylserine
CC       externalization and apoptosis in neurons via its association with
CC       PLSCR1 (By similarity). {ECO:0000250|UniProtKB:Q9QX29,
CC       ECO:0000269|PubMed:16284075}.
CC   -!- ACTIVITY REGULATION: Calcium channel activity is enhanced by MYLK, that
CC       promotes its subcellular localization at the plasma membrane.
CC       {ECO:0000269|PubMed:16284075}.
CC   -!- SUBUNIT: Interacts with TRPC4AP (By similarity). Homotetramer and
CC       heterotetramer with TRPC1 and/or TRPC4 (PubMed:12032305). Interacts
CC       with NHERF1 (By similarity). Interacts with MX1 and RNF24
CC       (PubMed:15757897, PubMed:17850865). Interacts (via C-terminus) with
CC       CABP1 (PubMed:15895247). Interacts with SESTD1 (via the spectrin 1
CC       repeat) (PubMed:20164195). Interacts with PLSCR1 (PubMed:32110987).
CC       {ECO:0000250|UniProtKB:Q9QX29, ECO:0000269|PubMed:12032305,
CC       ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:15895247,
CC       ECO:0000269|PubMed:17850865, ECO:0000269|PubMed:20164195,
CC       ECO:0000269|PubMed:32110987}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16284075};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:16284075}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain with higher levels in fetal
CC       brain. Found in cerebellum and occipital pole.
CC       {ECO:0000269|PubMed:9687496}.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC       subfamily. TRPC5 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AF054568; AAF00002.1; -; mRNA.
DR   EMBL; AC005191; AAC24563.1; -; Genomic_DNA.
DR   EMBL; AL049563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471120; EAX02630.1; -; Genomic_DNA.
DR   EMBL; BC137271; AAI37272.1; -; mRNA.
DR   EMBL; BC137274; AAI37275.1; -; mRNA.
DR   CCDS; CCDS14561.1; -.
DR   RefSeq; NP_036603.1; NM_012471.2.
DR   RefSeq; XP_016885263.1; XM_017029774.1.
DR   PDB; 6YSN; EM; 3.00 A; A/B/C/D=1-765.
DR   PDB; 7D4P; EM; 2.70 A; A/B/C/D=1-764.
DR   PDB; 7D4Q; EM; 2.74 A; A/B/C/D=1-764.
DR   PDB; 7E4T; EM; 3.00 A; A/B/C/D=1-764.
DR   PDB; 7WDB; EM; 2.40 A; A/B/C/D=1-764.
DR   PDB; 7X6C; EM; 3.15 A; A/B/C/D=1-765.
DR   PDB; 7X6I; EM; 3.93 A; A/B/C/D=1-765.
DR   PDB; 8GVW; EM; 3.59 A; A/B/C/D=1-765.
DR   PDB; 8GVX; EM; 3.91 A; A/B/C/D=1-765.
DR   PDBsum; 6YSN; -.
DR   PDBsum; 7D4P; -.
DR   PDBsum; 7D4Q; -.
DR   PDBsum; 7E4T; -.
DR   PDBsum; 7WDB; -.
DR   PDBsum; 7X6C; -.
DR   PDBsum; 7X6I; -.
DR   PDBsum; 8GVW; -.
DR   PDBsum; 8GVX; -.
DR   AlphaFoldDB; Q9UL62; -.
DR   EMDB; EMD-30575; -.
DR   EMDB; EMD-30576; -.
DR   EMDB; EMD-30987; -.
DR   EMDB; EMD-32436; -.
DR   EMDB; EMD-33021; -.
DR   EMDB; EMD-33022; -.
DR   EMDB; EMD-34300; -.
DR   EMDB; EMD-34301; -.
DR   SMR; Q9UL62; -.
DR   BioGRID; 113075; 21.
DR   IntAct; Q9UL62; 3.
DR   STRING; 9606.ENSP00000262839; -.
DR   BindingDB; Q9UL62; -.
DR   ChEMBL; CHEMBL1250411; -.
DR   DrugCentral; Q9UL62; -.
DR   GuidetoPHARMACOLOGY; 490; -.
DR   TCDB; 1.A.4.1.7; the transient receptor potential ca2+/cation channel (trp-cc) family.
DR   GlyCosmos; Q9UL62; 1 site, No reported glycans.
DR   GlyGen; Q9UL62; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UL62; -.
DR   PhosphoSitePlus; Q9UL62; -.
DR   SwissPalm; Q9UL62; -.
DR   BioMuta; TRPC5; -.
DR   DMDM; 10720321; -.
DR   EPD; Q9UL62; -.
DR   jPOST; Q9UL62; -.
DR   MassIVE; Q9UL62; -.
DR   MaxQB; Q9UL62; -.
DR   PaxDb; 9606-ENSP00000262839; -.
DR   PeptideAtlas; Q9UL62; -.
DR   ProteomicsDB; 84958; -.
DR   ABCD; Q9UL62; 1 sequenced antibody.
DR   Antibodypedia; 356; 337 antibodies from 32 providers.
DR   DNASU; 7224; -.
DR   Ensembl; ENST00000262839.3; ENSP00000262839.2; ENSG00000072315.4.
DR   GeneID; 7224; -.
DR   KEGG; hsa:7224; -.
DR   MANE-Select; ENST00000262839.3; ENSP00000262839.2; NM_012471.3; NP_036603.1.
DR   UCSC; uc004epl.2; human.
DR   AGR; HGNC:12337; -.
DR   CTD; 7224; -.
DR   DisGeNET; 7224; -.
DR   GeneCards; TRPC5; -.
DR   HGNC; HGNC:12337; TRPC5.
DR   HPA; ENSG00000072315; Tissue enhanced (brain).
DR   MIM; 300334; gene.
DR   neXtProt; NX_Q9UL62; -.
DR   OpenTargets; ENSG00000072315; -.
DR   PharmGKB; PA37010; -.
DR   VEuPathDB; HostDB:ENSG00000072315; -.
DR   eggNOG; KOG3609; Eukaryota.
DR   GeneTree; ENSGT01060000248594; -.
DR   HOGENOM; CLU_005716_4_1_1; -.
DR   InParanoid; Q9UL62; -.
DR   OMA; LCKWIHK; -.
DR   OrthoDB; 5406916at2759; -.
DR   PhylomeDB; Q9UL62; -.
DR   TreeFam; TF313147; -.
DR   PathwayCommons; Q9UL62; -.
DR   Reactome; R-HSA-3295583; TRP channels.
DR   Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
DR   SignaLink; Q9UL62; -.
DR   SIGNOR; Q9UL62; -.
DR   BioGRID-ORCS; 7224; 15 hits in 769 CRISPR screens.
DR   ChiTaRS; TRPC5; human.
DR   GeneWiki; TRPC5; -.
DR   GenomeRNAi; 7224; -.
DR   Pharos; Q9UL62; Tchem.
DR   PRO; PR:Q9UL62; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9UL62; Protein.
DR   Bgee; ENSG00000072315; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 25 other cell types or tissues.
DR   GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
DR   GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR   GO; GO:0042805; F:actinin binding; IEA:Ensembl.
DR   GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR   GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
DR   GO; GO:0030276; F:clathrin binding; IEA:Ensembl.
DR   GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR   GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006816; P:calcium ion transport; TAS:ProtInc.
DR   GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   GO; GO:0070782; P:phosphatidylserine exposure on apoptotic cell surface; ISS:UniProtKB.
DR   GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:1902630; P:regulation of membrane hyperpolarization; IEA:Ensembl.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR013555; TRP_dom.
DR   InterPro; IPR005461; TRPC5_channel.
DR   InterPro; IPR002153; TRPC_channel.
DR   NCBIfam; TIGR00870; trp; 1.
DR   PANTHER; PTHR10117:SF76; SHORT TRANSIENT RECEPTOR POTENTIAL CHANNEL 5; 1.
DR   PANTHER; PTHR10117; TRANSIENT RECEPTOR POTENTIAL CHANNEL; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF08344; TRP_2; 1.
DR   PRINTS; PR01097; TRNSRECEPTRP.
DR   PRINTS; PR01646; TRPCHANNEL5.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM01420; TRP_2; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   Genevisible; Q9UL62; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
KW   Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..973
FT                   /note="Short transient receptor potential channel 5"
FT                   /id="PRO_0000215318"
FT   TOPO_DOM        1..330
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        352..398
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        420..437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        459..470
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        492..512
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        513..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        534..603
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        604..624
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        625..973
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          31..60
FT                   /note="ANK 1"
FT   REPEAT          69..97
FT                   /note="ANK 2"
FT   REPEAT          98..124
FT                   /note="ANK 3"
FT   REPEAT          141..170
FT                   /note="ANK 4"
FT   REGION          766..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          810..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          971..973
FT                   /note="Essential for binding to NHERF1 PDZ domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QX29"
FT   COMPBIAS        820..837
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        461
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         667
FT                   /note="P -> T (found in a patient with severe delayed
FT                   speech, autism spectrum and Gilles de la Tourette
FT                   disorders)"
FT                   /evidence="ECO:0000269|PubMed:23033978"
FT                   /id="VAR_069415"
FT   VARIANT         702
FT                   /note="R -> H (in dbSNP:rs36047478)"
FT                   /id="VAR_052369"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           31..42
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           45..58
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           73..79
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           83..91
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           99..106
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           109..116
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           145..152
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           155..162
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           179..187
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           189..203
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           206..210
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           216..233
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   STRAND          234..237
FT                   /evidence="ECO:0007829|PDB:6YSN"
FT   HELIX           238..257
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           262..269
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           288..295
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           299..302
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           305..315
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   STRAND          316..318
FT                   /evidence="ECO:0007829|PDB:7E4T"
FT   TURN            320..323
FT                   /evidence="ECO:0007829|PDB:6YSN"
FT   HELIX           327..339
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           341..350
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   STRAND          352..354
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   TURN            355..357
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   STRAND          360..362
FT                   /evidence="ECO:0007829|PDB:7D4P"
FT   HELIX           363..383
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           402..425
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           428..431
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           435..459
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           466..468
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           474..491
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           492..499
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   TURN            501..503
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           504..539
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           540..542
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           546..548
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           550..552
FT                   /evidence="ECO:0007829|PDB:6YSN"
FT   STRAND          558..560
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   STRAND          564..567
FT                   /evidence="ECO:0007829|PDB:6YSN"
FT   HELIX           568..579
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           585..588
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           595..614
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           616..632
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           635..649
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   STRAND          651..653
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   TURN            659..662
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           707..733
FT                   /evidence="ECO:0007829|PDB:7WDB"
FT   HELIX           740..760
FT                   /evidence="ECO:0007829|PDB:7WDB"
SQ   SEQUENCE   973 AA;  111412 MW;  FBC8CBF17BE42166 CRC64;
     MAQLYYKKVN YSPYRDRIPL QIVRAETELS AEEKAFLNAV EKGDYATVKQ ALQEAEIYYN
     VNINCMDPLG RSALLIAIEN ENLEIMELLL NHSVYVGDAL LYAIRKEVVG AVELLLSYRR
     PSGEKQVPTL MMDTQFSEFT PDITPIMLAA HTNNYEIIKL LVQKRVTIPR PHQIRCNCVE
     CVSSSEVDSL RHSRSRLNIY KALASPSLIA LSSEDPILTA FRLGWELKEL SKVENEFKAE
     YEELSQQCKL FAKDLLDQAR SSRELEIILN HRDDHSEELD PQKYHDLAKL KVAIKYHQKE
     FVAQPNCQQL LATLWYDGFP GWRRKHWVVK LLTCMTIGFL FPMLSIAYLI SPRSNLGLFI
     KKPFIKFICH TASYLTFLFM LLLASQHIVR TDLHVQGPPP TVVEWMILPW VLGFIWGEIK
     EMWDGGFTEY IHDWWNLMDF AMNSLYLATI SLKIVAYVKY NGSRPREEWE MWHPTLIAEA
     LFAISNILSS LRLISLFTAN SHLGPLQISL GRMLLDILKF LFIYCLVLLA FANGLNQLYF
     YYETRAIDEP NNCKGIRCEK QNNAFSTLFE TLQSLFWSVF GLLNLYVTNV KARHEFTEFV
     GATMFGTYNV ISLVVLLNML IAMMNNSYQL IADHADIEWK FARTKLWMSY FDEGGTLPPP
     FNIIPSPKSF LYLGNWFNNT FCPKRDPDGR RRRRNLRSFT ERNADSLIQN QHYQEVIRNL
     VKRYVAAMIR NSKTHEGLTE ENFKELKQDI SSFRYEVLDL LGNRKHPRSF STSSTELSQR
     DDNNDGSGGA RAKSKSVSFN LGCKKKTCHG PPLIRTMPRS SGAQGKSKAE SSSKRSFMGP
     SLKKLGLLFS KFNGHMSEPS SEPMYTISDG IVQQHCMWQD IRYSQMEKGK AEACSQSEIN
     LSEVELGEVQ GAAQSSECPL ACSSSLHCAS SICSSNSKLL DSSEDVFETW GEACDLLMHK
     WGDGQEEQVT TRL
//