Crhr2
entrez
64680
canonical
uniprot
P47866
canonical
ensembl
ENSRNOG00000011145
resolver
ensembl
ENSRNOG00055010798
resolver
ensembl
ENSRNOG00060021958
resolver
ensp
ENSRNOP00000035712
resolver
ensp
ENSRNOP00000079784
resolver
enst
ENSRNOT00000098668
resolver
genesymbol
Crhr2
resolver
genesymbol_syn
Crf2r
resolver
uniprot
A0A8I5ZNG6
resolver
uniprot
G3V948
resolver
uniprot_entry
A0A8I5ZNG6_RAT
resolver
uniprot_entry
CRHR2_RAT
resolver
uniprot_sec
G3V948
resolver
amino_acid_sequence
MDAALLLSLLEANCSLALAEELLLDGWGEPPDPEGPYSYCNTTLDQIGTCWPQSAPGALVERPCPEYFNGIKYNTTRNAYRECLENGTWASRVNYSHCEPILDDKQRKYDLHYRIALIINYLGHCVSVVALVAAFLLFLVLRSIRCLRNVIHWNLITTFILRNITWFLLQLIDHEVHEGNEVWCRCVTTIFNYFVVTNFFWMFVEGCYLHTAIVMTYSTEHLRKWLFLFIGWCIPCPIIVAWAVGKLYYENEQCWFGKEPGDLVDYIYQGPIILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDDLSQIVFIYFNSFLQSFQGFFVSVFYCFFNGEVRSALRKRWHRWQDHHALRVPVARAMSIPTSPTRISFHSIKQTAAV
uniprot
proteins
function
FUNCTION: G protein-coupled receptor for CRH, UCN, UCN2 and UCN3 stress hormones, which plays a central role in whole body adaptation to stress (PubMed:7846062, PubMed:8703220). Has highest affinity for UCN, and much lower affinity for CRH, UNC2 and UCN3 (PubMed:8703220). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and downstream effectors, such as adenylate cyclase (By similarity). CRHR2 is coupled to G(s) G protein (GNAS), mediating activation of adenylate cyclase activity and production of cAMP (By similarity). CRHR2-dependent signaling is a primary mediator of the neuroendocrine, autonomic (fight-or-flight) and behavioral responses to stress, acting as a key regulator of adaptation by activating the hypothalamus-pituitary-adrenal axis, leading to corticotropin hormone (ACTH) production (PubMed:7846062). {ECO:0000250|UniProtKB:Q13324, ECO:0000269|PubMed:7846062, ECO:0000269|PubMed:8703220}.
uniprot
proteins
mass_dalton
47693
uniprot
proteins
mutagenesis
MUTAGEN 13; /note="N->A,F,I: Allows cleavage of signal peptide."; /evidence="ECO:0000269|PubMed:16766521
uniprot
proteins
post_translational_modification
PTM: A N-glycosylation site within the signal peptide impedes its proper cleavage and function. {ECO:0000269|PubMed:16766521}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
16766521
uniprot
proteins
pubmed
7846062
uniprot
proteins
pubmed
8703220
uniprot
proteins
sequence_length
411
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16766521, ECO:0000269|PubMed:7846062}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 114..139; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:Q13324"; TRANSMEM 150..171; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:Q13324"; TRANSMEM 183..210; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:Q13324"; TRANSMEM 224..245; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:Q13324"; TRANSMEM 264..288; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:Q13324"; TRANSMEM 308..326; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:Q13324"; TRANSMEM 335..362; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:Q13324
uniprot
proteins