CRHR2
entrez
1395
canonical
uniprot
Q13324
canonical
ensembl
ENSG00000106113
resolver
ensp
ENSP00000340943
resolver
ensp
ENSP00000344304
resolver
ensp
ENSP00000418722
resolver
ensp
ENSP00000426498
resolver
ensp
ENSP00000612584
resolver
genesymbol
CRHR2
resolver
genesymbol_syn
CRF2R
resolver
genesymbol_syn
CRH2R
resolver
hgnc
HGNC:2358
resolver
uniprot
B2R967
resolver
uniprot
B3SXS6
resolver
uniprot
B3SXS7
resolver
uniprot
B3SXS8
resolver
uniprot
B3SXT0
resolver
uniprot
F8WA81
resolver
uniprot
O43461
resolver
uniprot
Q4QRJ4
resolver
uniprot
Q99431
resolver
uniprot_entry
CRHR2_HUMAN
resolver
uniprot_sec
B2R967
resolver
uniprot_sec
B3SXS6
resolver
uniprot_sec
B3SXS7
resolver
uniprot_sec
B3SXS8
resolver
uniprot_sec
B3SXT0
resolver
uniprot_sec
F8WA81
resolver
uniprot_sec
O43461
resolver
uniprot_sec
Q4QRJ4
resolver
uniprot_sec
Q99431
resolver
amino_acid_sequence
MDAALLHSLLEANCSLALAEELLLDGWGPPLDPEGPYSYCNTTLDQIGTCWPRSAAGALVERPCPEYFNGVKYNTTRNAYRECLENGTWASKINYSQCEPILDDKQRKYDLHYRIALVVNYLGHCVSVAALVAAFLLFLALRSIRCLRNVIHWNLITTFILRNVMWFLLQLVDHEVHESNEVWCRCITTIFNYFVVTNFFWMFVEGCYLHTAIVMTYSTERLRKCLFLFIGWCIPFPIIVAWAIGKLYYENEQCWFGKEPGDLVDYIYQGPIILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDDLSQIMFIYFNSFLQSFQGFFVSVFYCFFNGEVRSAVRKRWHRWQDHHSLRVPMARAMSIPTSPTRISFHSIKQTAAV
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:11329063, PubMed:11416224, PubMed:20966082, PubMed:22689579, PubMed:32004470, PubMed:36335102). Has highest affinity for UCN, and much lower affinity for CRH, UNC2 and UCN3 (PubMed:20966082, PubMed:22689579, PubMed:32004470, PubMed:36335102). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and downstream effectors, such as adenylate cyclase (PubMed:32004470, PubMed:36335102). CRHR2 is coupled to G(s) G protein (GNAS), mediating activation of adenylate cyclase activity and production of cAMP (PubMed:32004470, PubMed:36335102). 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 (By similarity). {ECO:0000250|UniProtKB:Q60748, ECO:0000269|PubMed:11329063, ECO:0000269|PubMed:11416224, ECO:0000269|PubMed:20966082, ECO:0000269|PubMed:22689579, ECO:0000269|PubMed:32004470, ECO:0000269|PubMed:36335102}.
uniprot
proteins
mass_dalton
47688
uniprot
proteins
mutagenesis
MUTAGEN 214; /note="V->A: Decreased G(s) GNAS-dependent signaling."; /evidence="ECO:0000269|PubMed:36335102"; MUTAGEN 216; /note="T->A: Decreased G(s) GNAS-dependent signaling."; /evidence="ECO:0000269|PubMed:36335102"; MUTAGEN 218; /note="S->A: Decreased G(s) GNAS-dependent signaling."; /evidence="ECO:0000269|PubMed:36335102"; MUTAGEN 220; /note="E->A: Decreased G(s) GNAS-dependent signaling."; /evidence="ECO:0000269|PubMed:36335102"; MUTAGEN 221; /note="R->A: Decreased G(s) GNAS-dependent signaling."; /evidence="ECO:0000269|PubMed:36335102"; MUTAGEN 222; /note="L->A: Decreased G(s) GNAS-dependent signaling."; /evidence="ECO:0000269|PubMed:36335102"; MUTAGEN 228..232; /note="LFIGW->AFIGA: Impaired cholesterol-binding, leading to decreased activation by CRH and UCN."; /evidence="ECO:0000269|PubMed:32004470"; MUTAGEN 247..255; /note="LYYENEQCW->AYYENEQCA: Impaired cholesterol-binding, leading to decreased activation by CRH and UCN."; /evidence="ECO:0000269|PubMed:32004470
uniprot
proteins
post_translational_modification
PTM: A N-glycosylation site within the signal peptide impedes its proper cleavage and function. {ECO:0000250|UniProtKB:P47866}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
11329063
uniprot
proteins
pubmed
11416224
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
20966082
uniprot
proteins
pubmed
22689579
uniprot
proteins
pubmed
32004470
uniprot
proteins
pubmed
36335102
uniprot
proteins
pubmed
8536644
uniprot
proteins
pubmed
9199241
uniprot
proteins
pubmed
9717834
uniprot
proteins
sequence_length
411
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22689579}; Multi-pass membrane protein {ECO:0000269|PubMed:22689579, ECO:0000269|PubMed:32004470, ECO:0000269|PubMed:36335102}.
uniprot
proteins
transmembrane_region
TRANSMEM 114..139; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:32004470, ECO:0000269|PubMed:36335102, ECO:0007744|PDB:6PB1, ECO:0007744|PDB:7TRY, ECO:0007744|PDB:7TS0"; TRANSMEM 150..171; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:32004470, ECO:0000269|PubMed:36335102, ECO:0007744|PDB:6PB1, ECO:0007744|PDB:7TRY, ECO:0007744|PDB:7TS0"; TRANSMEM 183..210; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:32004470, ECO:0000269|PubMed:36335102, ECO:0007744|PDB:6PB1, ECO:0007744|PDB:7TRY, ECO:0007744|PDB:7TS0"; TRANSMEM 224..245; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:32004470, ECO:0000269|PubMed:36335102, ECO:0007744|PDB:6PB1, ECO:0007744|PDB:7TRY, ECO:0007744|PDB:7TS0"; TRANSMEM 264..288; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:32004470, ECO:0000269|PubMed:36335102, ECO:0007744|PDB:6PB1, ECO:0007744|PDB:7TRY, ECO:0007744|PDB:7TS0"; TRANSMEM 308..326; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:32004470, ECO:0000269|PubMed:36335102, ECO:0007744|PDB:6PB1, ECO:0007744|PDB:7TRY, ECO:0007744|PDB:7TS0"; TRANSMEM 335..362; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:32004470, ECO:0000269|PubMed:36335102, ECO:0007744|PDB:6PB1, ECO:0007744|PDB:7TRY, ECO:0007744|PDB:7TS0
uniprot
proteins