Trpc2
entrez
22064
canonical
uniprot
Q9R244
canonical
ensembl
ENSMUSG00000100254
resolver
ensp
ENSMUSP00000116934
resolver
genesymbol
Trpc2
resolver
genesymbol_syn
Trp2
resolver
genesymbol_syn
Trrp2
resolver
uniprot
Q9ES59
resolver
uniprot
Q9ES60
resolver
uniprot
Q9R243
resolver
uniprot_entry
TRPC2_MOUSE
resolver
uniprot_sec
Q9ES59
resolver
uniprot_sec
Q9ES60
resolver
uniprot_sec
Q9R243
resolver
amino_acid_sequence
MLMSRTDSKSGKNRSGVRMFKDGDFLTPASGESWDRLRLTCSQPFTRHQSFGLAFLRVRSSLGSLADPVVDPSAPGSSGLNQNSTDVLESDPRPWLTNPSIRRTFFPDPQTSTKEISELKGMLKQLQPGPLGRAARMVLSAARKAPPASVVSPNNSHGEPGPSRAESAEPRAEEPNRKTAVGRRKRRKVQEPRRSLSNSSSQPNRRTGRTRQRQHRPQTKSDDGGVQAAGQCPICAGFFSIETLPQHAATCGESPPPQPASPASLSSSESVLRRHHVALTPVPLVPKPQPNWTEIVNKKLKFPPTLLRAIQEGQLGLVQQLLESSSDASGAGPGGPLRNVEESEDRSWREALNLAIRLGHEVITDVLLANVKFDFRQIHEALLVAVDTNQPAVVRRLLARLEREKGRKVDTKSFSLAFFDSSIDGSRFAPGVTPLTLACQKDLYEIAQLLMDQGHTIARPHPVSCACLECSNARRYDLLKFSLSRINTYRGIASRAHLSLASEDAMLAAFQLSRELRRLARKEPEFKPQYIALESLCQDYGFELLGMCRNQSEVTAVLNDLGEDSETEPEAEGLGQAFEEGIPNLARLRLAVNYNQKQFVAHPICQQVLSSIWCGNLAGWRGSTTIWKLFVAFLIFLTMPFLCIGYWLAPKSQLGRLLKIPVLKFLLHSASYLWFLIFLLGESLVMETQLSTFKGRSQSVWETSLHMIWVTGFLWFECKEVWIEGLRSYLLDWWNFLDVVILSLYLASFALRLLLAGLAYMHCRDASDSTTCRYFTTAERSEWRTEDPQFLAEVLFAVTSMLSFTRLAYILPAHESLGTLQISIGKMIDDMIRFMFILMIILTAFLCGLNNIYVPYQESEKLGNFNETFQFLFWTMFGMEEHTVVDMPQFLVPEFVGRAMYGIFTIVMVIVLLNMLIAMITNSFQKIEDDADVEWKFARSKLYLSYFREGLTLPVPFNILPSPKAAFYLVRRIFRFLCCGSSCCKAKKSDYPPIGTFTNPGARAGSAGEGERVSYRLRVIKALVQRYIETARREFEETRRKDLGNRLTELTKTVSRLQSEVASVQKNLAAGGAPRPPDGASILSRYITRVRNSFQNLGPPTSDTPAELTMPGIVETEVSLGDGLDGTGEAGAPAPGEPGSSSSAHVLVHREQEAEGSGDLLLEGDLETKGES
uniprot
proteins
function
FUNCTION: Forms a Ca(2+)-permeable non-selective cation channel that mediates Ca(2+) influx upon activation. In vomeronasal sensory neurons, functions as the principal transduction channel gated by diacylglycerol (DAG) downstream of phospholipase C-coupled receptors (PubMed:14642279). Required for conditioned place aversion to hypoxic environments. In main olfactory epithelium type B cells, operates downstream of the soluble guanylate cyclase Gucy1b2 and cGMP-dependent protein kinase to mediate Ca(2+) entry in response to low environmental oxygen (PubMed:25701815, PubMed:27916458). Also plays roles in erythropoietin-stimulated Ca(2+) influx in erythroid cells and the sperm acrosome reaction (PubMed:11331878, PubMed:14642279). Required for pheromone-evoked social and reproductive behaviors including sex discrimination, male-male aggression, female sexual receptivity (Esp1-dependent), and inhibition of adult male mating behavior toward juveniles (Esp22-dependent) (PubMed:11823606, PubMed:11972034, PubMed:20596023, PubMed:24089208). {ECO:0000269|PubMed:11331878, ECO:0000269|PubMed:11823606, ECO:0000269|PubMed:11972034, ECO:0000269|PubMed:14642279, ECO:0000269|PubMed:20596023, ECO:0000269|PubMed:24089208, ECO:0000269|PubMed:25701815, ECO:0000269|PubMed:27916458}.
uniprot
proteins
mass_dalton
130531
uniprot
proteins
protein_family
STrpC subfamily
uniprot
proteins
protein_family
TRPC2 sub-subfamily
uniprot
proteins
protein_family
Transient receptor (TC 1.A.4) family
uniprot
proteins
pubmed
10051594
uniprot
proteins
pubmed
10998353
uniprot
proteins
pubmed
11331878
uniprot
proteins
pubmed
11823606
uniprot
proteins
pubmed
11972034
uniprot
proteins
pubmed
12167663
uniprot
proteins
pubmed
14642279
uniprot
proteins
pubmed
20596023
uniprot
proteins
pubmed
24089208
uniprot
proteins
pubmed
25701815
uniprot
proteins
pubmed
27916458
uniprot
proteins
pubmed
34186026
uniprot
proteins
sequence_length
1172
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:14642279}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 660..680; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 703..723; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 739..759; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 790..810; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 834..854; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 900..920; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins