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Database: UniProt
Entry: F1LRB9_RAT
LinkDB: F1LRB9_RAT
Original site: F1LRB9_RAT 
ID   F1LRB9_RAT              Unreviewed;       775 AA.
AC   F1LRB9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Short transient receptor potential channel 1 {ECO:0000256|ARBA:ARBA00013302};
GN   Name=Trpc1 {ECO:0000313|Ensembl:ENSRNOP00000072139.2,
GN   ECO:0000313|RGD:619783};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000072139.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000072139.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000072139.2,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000072139.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000072139.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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. Seems to be also activated by intracellular
CC       calcium store depletion. {ECO:0000256|ARBA:ARBA00003698}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC       subfamily. TRPC1 sub-subfamily. {ECO:0000256|ARBA:ARBA00009944}.
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DR   AlphaFoldDB; F1LRB9; -.
DR   Ensembl; ENSRNOT00000079965.2; ENSRNOP00000072139.2; ENSRNOG00000054902.2.
DR   RGD; 619783; Trpc1.
DR   VEuPathDB; HostDB:ENSRNOG00000054902; -.
DR   GeneTree; ENSGT01060000248594; -.
DR   HOGENOM; CLU_005716_4_1_1; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000054902; Expressed in cerebellum and 20 other cell types or tissues.
DR   ExpressionAtlas; F1LRB9; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005262; F:calcium channel activity; IEA:InterPro.
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; IPR005457; TRPC1_channel.
DR   InterPro; IPR002153; TRPC_channel.
DR   NCBIfam; TIGR00870; trp; 1.
DR   PANTHER; PTHR10117:SF56; SHORT TRANSIENT RECEPTOR POTENTIAL CHANNEL 1; 1.
DR   PANTHER; PTHR10117; TRANSIENT RECEPTOR POTENTIAL CHANNEL; 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; PR01642; TRPCHANNEL1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM01420; TRP_2; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          175..237
FT                   /note="Transient receptor ion channel"
FT                   /evidence="ECO:0000259|SMART:SM01420"
SQ   SEQUENCE   775 AA;  89131 MW;  99C4F80B7AD98823 CRC64;
     MGAPPPSPGL PPSWAAMMAA LYPSTDLSGV SSSSLPSSPS SSSPNEVMAL KDVREVKEEN
     TLNEKLFLLA CDKGDYYMVK KILEENSSGD LNINCVDVLG RNAVTITIEN ESLDILQLLL
     DYGCQKLMER IQNPEYSTTM DVAPVILAAH RNNYEILTML LKQDVALPKP HAVGCECTLC
     SAKNKKDSLR HSRFRLDIYR CLASPALIML TEEDPILRAF ELSADLKELS LVEVEFRNDY
     EELARQCKMF AKDLLAQARN SRELEVILNH TSSDEPLDKR GLLEERMNLS RLKLAIKYNQ
     KEFVSQSNCQ QFLNTVWFGQ MSGYRRKPTC KKIMTVLTVG IFWPVLSLCY LIAPKSQFGR
     IIHTPFMKFI IHGASYFTFL LLLNLYSLVY NEDKKNTMGP ALERIDYLLI LWIIGMIWSD
     IKRLWYEGLE DFLEESRNQL SFVMNSLYLA TFALKVVAHN KFHDFADRKD WDAFHPTLVA
     EGLFAFANVL SYLRLFFMYT TSSILGPLQI SMGQMLQDFG KFLGMFLLVL FSFTIGLTQL
     YDKGYTSKEQ KDCVGIFCEQ QSNDTFHSFI GTCFALFWYI FSLAHVAIFV TRFSYGEELQ
     SFVGAVIVGT YNVVVVIVLT KLLVAMLHKS FQLIANHEDK EWKFARAKLW LSYFDDKCTL
     PPPFNIIPSP KTICYMISSL SKWVCSHTSK GKVRRQNSLK EWRNLKQKRD ENYQKVMCCL
     VHRYLTSMRQ KMQSTDQATV ENLNELRQDL SKFRNEIRDL LGFRTSKYAM FYPRN
//
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