ID TRPC2_MOUSE Reviewed; 1172 AA.
AC Q9R244; Q9ES59; Q9ES60; Q9R243;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 24-JAN-2024, entry version 183.
DE RecName: Full=Short transient receptor potential channel 2;
DE Short=TrpC2;
DE AltName: Full=Transient receptor protein 2;
DE Short=TRP-2;
DE Short=mTrp2;
GN Name=Trpc2; Synonyms=Trp2, Trrp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=10051594; DOI=10.1073/pnas.96.5.2060;
RA Vannier B., Peyton M., Boulay G., Brown D., Qin N., Jiang M., Zhu X.,
RA Birnbaumer L.;
RT "Mouse trp2, the homologue of the human trpc2 pseudogene, encodes mTrp2, a
RT store depletion-activated capacitative Ca2+ entry channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2060-2064(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RX PubMed=10998353; DOI=10.1042/0264-6021:3510115;
RA Hofmann T., Schaefer M., Schultz G., Gudermann T.;
RT "Cloning, expression and subcellular localization of two novel splice
RT variants of mouse transient receptor potential channel 2.";
RL Biochem. J. 351:115-122(2000).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11972034; DOI=10.1073/pnas.082127599;
RA Leypold B.G., Yu C.R., Leinders-Zufall T., Kim M.M., Zufall F., Axel R.;
RT "Altered sexual and social behaviors in trp2 mutant mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6376-6381(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11823606; DOI=10.1126/science.1069259;
RA Stowers L., Holy T.E., Meister M., Dulac C., Koentges G.;
RT "Loss of sex discrimination and male-male aggression in mice deficient for
RT TRP2.";
RL Science 295:1493-1500(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20596023; DOI=10.1038/nature09142;
RA Haga S., Hattori T., Sato T., Sato K., Matsuda S., Kobayakawa R.,
RA Sakano H., Yoshihara Y., Kikusui T., Touhara K.;
RT "The male mouse pheromone ESP1 enhances female sexual receptive behaviour
RT through a specific vomeronasal receptor.";
RL Nature 466:118-122(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24089208; DOI=10.1038/nature12579;
RA Ferrero D.M., Moeller L.M., Osakada T., Horio N., Li Q., Roy D.S.,
RA Cichy A., Spehr M., Touhara K., Liberles S.D.;
RT "A juvenile mouse pheromone inhibits sexual behaviour through the
RT vomeronasal system.";
RL Nature 502:368-371(2013).
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. May also be activated by intracellular
CC calcium store depletion. Plays a role in mediating responsivity to
CC pheromones that elicit aggressive and mating behaviors. Required for
CC response to the Esp1 pheromone which enhances female sexual receptive
CC behavior and to the Esp22 pheromone which inhibits adult male mating
CC behavior. {ECO:0000269|PubMed:11823606, ECO:0000269|PubMed:11972034,
CC ECO:0000269|PubMed:20596023, ECO:0000269|PubMed:24089208}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A;
CC IsoId=Q9R244-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9R244-2; Sequence=VSP_006562;
CC Name=3; Synonyms=Alpha;
CC IsoId=Q9R244-3; Sequence=VSP_006564;
CC Name=4; Synonyms=Beta;
CC IsoId=Q9R244-4; Sequence=VSP_006563, VSP_006565;
CC -!- TISSUE SPECIFICITY: Isoform 3 is ubiquitously expressed at low levels.
CC Isoform 4 is expressed exclusively in vomeronasal organ.
CC -!- DISRUPTION PHENOTYPE: Reduced electrophysiological response to
CC pheromone mixtures in the vomeronasal organ. Mutant males and nursing
CC females are docile and fail to initiate aggressive attacks on intruder
CC males. Males display normal mating behavior towards females but display
CC increased sexual behavior towards prepubescent females even when
CC presented simultaneously with adult estrus females and also show
CC increased sexual behavior towards juvenile and adult males. Lack of
CC response to Esp1. {ECO:0000269|PubMed:11823606,
CC ECO:0000269|PubMed:11972034, ECO:0000269|PubMed:20596023,
CC ECO:0000269|PubMed:24089208}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC2 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF111108; AAD17196.1; -; mRNA.
DR EMBL; AF111107; AAD17195.1; -; mRNA.
DR EMBL; AF230803; AAG29951.1; -; mRNA.
DR EMBL; AF230802; AAG29950.1; -; mRNA.
DR CCDS; CCDS52333.1; -. [Q9R244-4]
DR RefSeq; NP_001103367.1; NM_001109897.2. [Q9R244-4]
DR AlphaFoldDB; Q9R244; -.
DR SMR; Q9R244; -.
DR BioGRID; 204328; 1.
DR CORUM; Q9R244; -.
DR DIP; DIP-61090N; -.
DR IntAct; Q9R244; 2.
DR STRING; 10090.ENSMUSP00000081903; -.
DR iPTMnet; Q9R244; -.
DR PhosphoSitePlus; Q9R244; -.
DR PaxDb; 10090-ENSMUSP00000081903; -.
DR DNASU; 22064; -.
DR Ensembl; ENSMUST00000124189.3; ENSMUSP00000116934.3; ENSMUSG00000100254.2. [Q9R244-4]
DR GeneID; 22064; -.
DR KEGG; mmu:22064; -.
DR UCSC; uc009iqm.2; mouse. [Q9R244-3]
DR UCSC; uc009iqn.2; mouse. [Q9R244-2]
DR UCSC; uc012fqr.2; mouse. [Q9R244-1]
DR UCSC; uc012fqs.2; mouse. [Q9R244-4]
DR AGR; MGI:109527; -.
DR CTD; 7221; -.
DR MGI; MGI:109527; Trpc2.
DR VEuPathDB; HostDB:ENSMUSG00000100254; -.
DR eggNOG; KOG3609; Eukaryota.
DR HOGENOM; CLU_005716_2_0_1; -.
DR InParanoid; Q9R244; -.
DR OMA; MIDDMMF; -.
DR OrthoDB; 5406916at2759; -.
DR PhylomeDB; Q9R244; -.
DR BioGRID-ORCS; 22064; 2 hits in 80 CRISPR screens.
DR ChiTaRS; Dct; mouse.
DR PRO; PR:Q9R244; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9R244; Protein.
DR Bgee; ENSMUSG00000100254; Expressed in mesentery of urinary system and 45 other cell types or tissues.
DR Genevisible; Q9R244; MM.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0032590; C:dendrite membrane; IMP:MGI.
DR GO; GO:0012505; C:endomembrane system; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0019992; F:diacylglycerol binding; IMP:MGI.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:BHF-UCL.
DR GO; GO:0015279; F:store-operated calcium channel activity; IDA:MGI.
DR GO; GO:0007340; P:acrosome reaction; IMP:MGI.
DR GO; GO:0002118; P:aggressive behavior; IMP:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0008050; P:female courtship behavior; IMP:MGI.
DR GO; GO:0002121; P:inter-male aggressive behavior; IMP:MGI.
DR GO; GO:0048047; P:mating behavior, sex discrimination; IMP:MGI.
DR GO; GO:1902436; P:negative regulation of male mating behavior; IGI:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IPI:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0019236; P:response to pheromone; IMP:MGI.
DR GO; GO:0007338; P:single fertilization; IBA:GO_Central.
DR GO; GO:0000012; P:single strand break repair; IEA:InterPro.
DR GO; GO:0002124; P:territorial aggressive behavior; IMP:MGI.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR013555; TRP_dom.
DR InterPro; IPR005458; TRPC2_channel.
DR InterPro; IPR002153; TRPC_channel.
DR InterPro; IPR002706; Xrcc1_N.
DR PANTHER; PTHR10117:SF6; SHORT TRANSIENT RECEPTOR POTENTIAL CHANNEL 2; 1.
DR PANTHER; PTHR10117; TRANSIENT RECEPTOR POTENTIAL CHANNEL; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF08344; TRP_2; 1.
DR Pfam; PF01834; XRCC1_N; 1.
DR PRINTS; PR01097; TRNSRECEPTRP.
DR PRINTS; PR01643; TRPCHANNEL2.
DR SMART; SM01420; TRP_2; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ANK repeat; Calcium; Calcium channel;
KW Calcium transport; Ion channel; Ion transport; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1172
FT /note="Short transient receptor potential channel 2"
FT /id="PRO_0000215307"
FT TOPO_DOM 1..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 660..680
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 681..702
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..738
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 739..759
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 760..789
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 790..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..833
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 834..854
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 855..899
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 900..920
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 921..1172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 301..330
FT /note="ANK 1"
FT REPEAT 377..406
FT /note="ANK 2"
FT REPEAT 430..459
FT /note="ANK 3"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..111
FT /note="MLMSRTDSKSGKNRSGVRMFKDGDFLTPASGESWDRLRLTCSQPFTRHQSFG
FT LAFLRVRSSLGSLADPVVDPSAPGSSGLNQNSTDVLESDPRPWLTNPSIRRTFFPDPQT
FT -> MGTKTHPVVPW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10051594"
FT /id="VSP_006562"
FT VAR_SEQ 2..287
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10998353"
FT /id="VSP_006564"
FT VAR_SEQ 2..283
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10998353"
FT /id="VSP_006563"
FT VAR_SEQ 284..287
FT /note="LVPK -> DPLS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10998353"
FT /id="VSP_006565"
FT CONFLICT 628
FT /note="K -> R (in Ref. 1; AAD17195/AAD17196)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="F -> S (in Ref. 1; AAD17195/AAD17196)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="Q -> R (in Ref. 2; AAG29951/AAG29950)"
FT /evidence="ECO:0000305"
FT CONFLICT 774
FT /note="Y -> C (in Ref. 1; AAD17195/AAD17196)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="A -> T (in Ref. 1; AAD17195/AAD17196)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161
FT /note="L -> P (in Ref. 2; AAG29951/AAG29950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1172 AA; 130531 MW; D9A9A9FEE01D1536 CRC64;
MLMSRTDSKS GKNRSGVRMF KDGDFLTPAS GESWDRLRLT CSQPFTRHQS FGLAFLRVRS
SLGSLADPVV DPSAPGSSGL NQNSTDVLES DPRPWLTNPS IRRTFFPDPQ TSTKEISELK
GMLKQLQPGP LGRAARMVLS AARKAPPASV VSPNNSHGEP GPSRAESAEP RAEEPNRKTA
VGRRKRRKVQ EPRRSLSNSS SQPNRRTGRT RQRQHRPQTK SDDGGVQAAG QCPICAGFFS
IETLPQHAAT CGESPPPQPA SPASLSSSES VLRRHHVALT PVPLVPKPQP NWTEIVNKKL
KFPPTLLRAI QEGQLGLVQQ LLESSSDASG AGPGGPLRNV EESEDRSWRE ALNLAIRLGH
EVITDVLLAN VKFDFRQIHE ALLVAVDTNQ PAVVRRLLAR LEREKGRKVD TKSFSLAFFD
SSIDGSRFAP GVTPLTLACQ KDLYEIAQLL MDQGHTIARP HPVSCACLEC SNARRYDLLK
FSLSRINTYR GIASRAHLSL ASEDAMLAAF QLSRELRRLA RKEPEFKPQY IALESLCQDY
GFELLGMCRN QSEVTAVLND LGEDSETEPE AEGLGQAFEE GIPNLARLRL AVNYNQKQFV
AHPICQQVLS SIWCGNLAGW RGSTTIWKLF VAFLIFLTMP FLCIGYWLAP KSQLGRLLKI
PVLKFLLHSA SYLWFLIFLL GESLVMETQL STFKGRSQSV WETSLHMIWV TGFLWFECKE
VWIEGLRSYL LDWWNFLDVV ILSLYLASFA LRLLLAGLAY MHCRDASDST TCRYFTTAER
SEWRTEDPQF LAEVLFAVTS MLSFTRLAYI LPAHESLGTL QISIGKMIDD MIRFMFILMI
ILTAFLCGLN NIYVPYQESE KLGNFNETFQ FLFWTMFGME EHTVVDMPQF LVPEFVGRAM
YGIFTIVMVI VLLNMLIAMI TNSFQKIEDD ADVEWKFARS KLYLSYFREG LTLPVPFNIL
PSPKAAFYLV RRIFRFLCCG SSCCKAKKSD YPPIGTFTNP GARAGSAGEG ERVSYRLRVI
KALVQRYIET ARREFEETRR KDLGNRLTEL TKTVSRLQSE VASVQKNLAA GGAPRPPDGA
SILSRYITRV RNSFQNLGPP TSDTPAELTM PGIVETEVSL GDGLDGTGEA GAPAPGEPGS
SSSAHVLVHR EQEAEGSGDL LLEGDLETKG ES
//
