TRPC3_RAT
ID TRPC3_RAT Reviewed; 909 AA.
AC Q9JMI9; F1LNQ7;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 4.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Short transient receptor potential channel 3;
DE Short=TrpC3;
DE AltName: Full=Trp-related protein 3;
GN Name=Trpc3; Synonyms=Trrp3;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 206-909.
RC TISSUE=Heart;
RX PubMed=10984475; DOI=10.1074/jbc.m003606200;
RA Ohki G., Miyoshi T., Murata M., Ishibashi K., Imai M., Suzuki M.;
RT "A calcium-activated cation current by an alternatively spliced form of
RT Trp3 in the heart.";
RL J. Biol. Chem. 275:39055-39060(2000).
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. Activated by diacylglycerol (DAG) in a
CC membrane-delimited fashion, independently of protein kinase C, and by
CC inositol 1,4,5-triphosphate receptors (ITPR) with bound IP3 (By
CC similarity). May also be activated by internal calcium store depletion.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ITPR1, ITPR3, MX1 and RNF24 (By similarity).
CC Interacts with JPH2; the interaction is involved in maintaining Ca(2+)
CC homeostasis in skeletal muscle and is mediated by JPH2 'Ser-165'
CC phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q13507}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC3 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA93434.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; AABR03013307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03015957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB022331; BAA93434.1; ALT_SEQ; mRNA.
DR RefSeq; NP_068539.2; NM_021771.2.
DR AlphaFoldDB; Q9JMI9; -.
DR SMR; Q9JMI9; -.
DR DIP; DIP-59688N; -.
DR IntAct; Q9JMI9; 1.
DR STRING; 10116.ENSRNOP00000046270; -.
DR ChEMBL; CHEMBL4105916; -.
DR GlyGen; Q9JMI9; 1 site.
DR iPTMnet; Q9JMI9; -.
DR PhosphoSitePlus; Q9JMI9; -.
DR PaxDb; Q9JMI9; -.
DR PRIDE; Q9JMI9; -.
DR Ensembl; ENSRNOT00000046700.6; ENSRNOP00000046270.5; ENSRNOG00000016070.8.
DR GeneID; 60395; -.
DR KEGG; rno:60395; -.
DR CTD; 7222; -.
DR RGD; 61973; Trpc3.
DR VEuPathDB; HostDB:ENSRNOG00000016070; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244831; -.
DR InParanoid; Q9JMI9; -.
DR OrthoDB; 1018075at2759; -.
DR PhylomeDB; Q9JMI9; -.
DR TreeFam; TF313147; -.
DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-RNO-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-RNO-3295583; TRP channels.
DR PRO; PR:Q9JMI9; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Proteomes; UP000002494; Unplaced.
DR Bgee; ENSRNOG00000016070; Expressed in cerebellum and 16 other tissues.
DR ExpressionAtlas; Q9JMI9; baseline and differential.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0005227; F:calcium activated cation channel activity; IDA:RGD.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISO:RGD.
DR GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:RGD.
DR GO; GO:1903244; P:positive regulation of cardiac muscle hypertrophy in response to stress; ISO:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0033198; P:response to ATP; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
DR GO; GO:0007338; P:single fertilization; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 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; IPR005459; TRPC3_channel.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR10117; PTHR10117; 1.
DR PANTHER; PTHR10117:SF8; PTHR10117:SF8; 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; PR01644; TRPCHANNEL3.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..909
FT /note="Short transient receptor potential channel 3"
FT /id="PRO_0000215312"
FT TOPO_DOM 1..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..491
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..596
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..710
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 711..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..909
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 99..128
FT /note="ANK 1"
FT REPEAT 134..163
FT /note="ANK 2"
FT REPEAT 165..191
FT /note="ANK 3"
FT REPEAT 220..249
FT /note="ANK 4"
FT REPEAT 622..651
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 408
FT /note="A -> S (in Ref. 2; BAA93434)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="S -> T (in Ref. 2; BAA93434)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="D -> H (in Ref. 2; BAA93434)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="Q -> H (in Ref. 2; BAA93434)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="E -> K (in Ref. 2; BAA93434)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="K -> E (in Ref. 2; BAA93434)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="K -> Q (in Ref. 2; BAA93434)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 909 AA; 103499 MW; 7E6D9DDA31441BA7 CRC64;
MSTKVKKCRE PARVTLPAPE EEDGEAEGAE PQRRRRGWRG VNGGLEPPCP RAPPSPGPDA
SSEGSPSRWR TAGMRDKGRR QAVRGPAFMF GARGPSLTAE EERFLDAAEY GNIPVVRKML
EESRTLNVNC VDYMGQNALQ LAVGNEHLEV TELLLKKENL ARIGDALLLA ISKGYVRIVE
AILGHPGFAA SRRLTLSPCE QELRDDDFYA YDEDGTRFSP DITPIILAAH CHKYEVVHLL
LLKGARIERP HDYFCRCADC AEKQRLDAFS HSRSRINAYK GLASPAYLSL SSEDPVLTAL
ELSNELAKLA NIEKEFKNDY RKLSMQCKDF VVGVLDLCRD SEEVEAILNG DLESVEPLER
HGHKASLSRV KLAIKYEVKK FVAHPNCQQQ LLTIWYENLS GLREQTIAIK CLVVLVVALG
LPFLAIGYWI APCSRLGKIL RSPFMKFVAH AASFIIFLGL LVFNASDRFE GITTLPNITV
IDYPKQIFRV KTTQFTWTEM LIMVWVLGMM WSECKELWLE GPREYIVQLW NVLDFGMLSI
FIAAFTARFL AFLQATKAQQ YVDSHVQESD LSEVTLPPEV QYFTYARDKW LPSDPQIISE
GLYAIAVVLS FSRIAYILPA NESFGPLQIS LGRTVKDIFK FMVLFIMVFL AFMIGMFILY
SYYLGAKVNP AFTTVEESFK TLFWSIFGLS EVTSVVLKYD HKFIENIGYV LYGIYNVTMV
VVLLNMLIAM INSSYQEIED DSDVEWKFAR SKLWLSYFDD GKTLPPPFSL VPSPKSFVYF
IMRITNFSKC RRRRLQKDLE LGMGNSKSRL NLFTQSNSRV FESHSFNSIL NQPTRYQQIM
KRLIKRYVLK AQVDKENDEV NEGELKEIKQ DISSLRYELL EDKSQATEEL AILIHKLSEK
LNPSALRCE
