CRHR1
entrez
1394
canonical
uniprot
P34998
canonical
ensembl
ENSG00000120088
resolver
ensembl
ENSG00000263715
resolver
ensembl
ENSG00000276191
resolver
ensembl
ENSG00000278232
resolver
ensp
ENSP00000326060
resolver
ensp
ENSP00000340522
resolver
ensp
ENSP00000344068
resolver
ensp
ENSP00000381333
resolver
ensp
ENSP00000462016
resolver
ensp
ENSP00000478252
resolver
ensp
ENSP00000481116
resolver
ensp
ENSP00000484097
resolver
ensp
ENSP00000484545
resolver
ensp
ENSP00000611121
resolver
enst
ENST00000339069
resolver
enst
ENST00000611599
resolver
enst
ENST00000618144
resolver
enst
ENST00000619154
resolver
enst
ENST00000621969
resolver
genesymbol
CRHR1
resolver
genesymbol_syn
CRFR
resolver
genesymbol_syn
CRFR1
resolver
genesymbol_syn
CRHR
resolver
hgnc
HGNC:2357
resolver
uniprot
A0A0G2JLZ3
resolver
uniprot
A0A0G2JND0
resolver
uniprot
B3SXS2
resolver
uniprot
B3TIK8
resolver
uniprot
B4DIE9
resolver
uniprot
F8W691
resolver
uniprot
G3CIS4
resolver
uniprot
K9J956
resolver
uniprot
Q13008
resolver
uniprot
Q4QRJ1
resolver
uniprot
Q9UK64
resolver
uniprot_entry
A0A0G2JLZ3_HUMAN
resolver
uniprot_entry
A0A0G2JND0_HUMAN
resolver
uniprot_entry
B3SXS2_HUMAN
resolver
uniprot_entry
B3TIK8_HUMAN
resolver
uniprot_entry
CRHR1_HUMAN
resolver
uniprot_entry
F8W691_HUMAN
resolver
uniprot_entry
G3CIS4_HUMAN
resolver
uniprot_entry
K9J956_HUMAN
resolver
uniprot_sec
B4DIE9
resolver
uniprot_sec
Q13008
resolver
uniprot_sec
Q4QRJ1
resolver
uniprot_sec
Q9UK64
resolver
amino_acid_sequence
MGGHPQLRLVKALLLLGLNPVSASLQDQHCESLSLASNISGLQCNASVDLIGTCWPRSPAGQLVVRPCPAFFYGVRYNTTNNGYRECLANGSWAARVNYSECQEILNEEKKSKVHYHVAVIINYLGHCISLVALLVAFVLFLRLRSIRCLRNIIHWNLISAFILRNATWFVVQLTMSPEVHQSNVGWCRLVTAAYNYFHVTNFFWMFGEGCYLHTAIVLTYSTDRLRKWMFICIGWGVPFPIIVAWAIGKLYYDNEKCWFGKRPGVYTDYIYQGPMILVLLINFIFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDEVSRVVFIYFNSFLESFQGFFVSVFYCFLNSEVRSAIRKRWHRWQDKHSIRARVARAMSIPTSPTRVSFHSIKQSTAV
uniprot
proteins
function
FUNCTION: G protein-coupled receptor for CRH and UCN stress hormones, which plays a central role in whole body adaptation to stress (PubMed:18292205, PubMed:18801728, PubMed:20966082, PubMed:23576434, PubMed:23863939, PubMed:24290358, PubMed:32004469, PubMed:32004470). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and downstream effectors, such as adenylate cyclase (PubMed:18292205, PubMed:32004469, PubMed:32004470). CRHR1 is mainly coupled to G(s) G protein (GNAS), mediating activation of adenylate cyclase activity and production of cAMP (PubMed:18292205, PubMed:32004469, PubMed:32004470). In some conditions, can also couple to G(q) G protein (GNAQ) and mediate production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) second messengers (PubMed:14657255). CRHR1-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). Mediates both anxiogenic and anxiolytic response to stress in glutamatergic and dopaminergic neurons, respectively (By similarity). CRHR1 also plays a critical role in addiction by mediating the brain's stress response, particularly during withdrawal and relapse: it drives the transition to compulsive drug seeking by increasing anxiety and negative emotional states (By similarity). {ECO:0000250|UniProtKB:P35347, ECO:0000269|PubMed:14657255, ECO:0000269|PubMed:18292205, ECO:0000269|PubMed:18801728, ECO:0000269|PubMed:20966082, ECO:0000269|PubMed:23576434, ECO:0000269|PubMed:23863939, ECO:0000269|PubMed:24290358, ECO:0000269|PubMed:32004469, ECO:0000269|PubMed:32004470}.; FUNCTION: [Isoform CRF-R3]: Does not bind to CRH with high affinity. {ECO:0000269|PubMed:7811272}.
uniprot
proteins
mass_dalton
47671
uniprot
proteins
mutagenesis
MUTAGEN 203; /note="F->A: Nearly abolishes antagonist binding."; /evidence="ECO:0000269|PubMed:23863939"; MUTAGEN 206; /note="M->A: Strongly reduces antagonist binding."; /evidence="ECO:0000269|PubMed:23863939"; MUTAGEN 232..236; /note="ICIGW->ACIGA: Impaired cholesterol-binding, leading to decreased activation by CRH and UCN."; /evidence="ECO:0000269|PubMed:32004470"; MUTAGEN 251..259; /note="LYYDNEKCW->AYYDNEKCA: Impaired cholesterol-binding, leading to decreased activation by CRH and UCN."; /evidence="ECO:0000269|PubMed:32004470"; MUTAGEN 280; /note="L->A: Nearly abolishes antagonist binding."; /evidence="ECO:0000269|PubMed:23863939"; MUTAGEN 283; /note="N->A: Nearly abolishes antagonist binding."; /evidence="ECO:0000269|PubMed:23863939"; MUTAGEN 284; /note="F->A: Slightly reduces antagonist binding."; /evidence="ECO:0000269|PubMed:23863939"; MUTAGEN 287; /note="L->A: Strongly reduces antagonist binding."; /evidence="ECO:0000269|PubMed:23863939"; MUTAGEN 290; /note="I->A: Strongly reduces antagonist binding."; /evidence="ECO:0000269|PubMed:23863939"; MUTAGEN 327; /note="Y->A: Strongly reduces antagonist binding."; /evidence="ECO:0000269|PubMed:23863939"; MUTAGEN 355; /note="Q->A: Increases antagonist binding."; /evidence="ECO:0000269|PubMed:23863939
uniprot
proteins
post_translational_modification
PTM: C-terminal Ser or Thr residues may be phosphorylated (PubMed:14657255). Phosphorylation at Ser-301 by PKA prevents maximal coupling to Gq-protein, and thereby negatively regulates downstream signaling (PubMed:14657255). {ECO:0000269|PubMed:14657255}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
10598591
uniprot
proteins
pubmed
11425856
uniprot
proteins
pubmed
14657255
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
18292205
uniprot
proteins
pubmed
18801728
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
20843795
uniprot
proteins
pubmed
20966082
uniprot
proteins
pubmed
23576434
uniprot
proteins
pubmed
23863939
uniprot
proteins
pubmed
24290358
uniprot
proteins
pubmed
32004469
uniprot
proteins
pubmed
32004470
uniprot
proteins
pubmed
7692441
uniprot
proteins
pubmed
7811272
uniprot
proteins
pubmed
8243652
uniprot
proteins
pubmed
9757017
uniprot
proteins
sequence_length
415
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18292205}; Multi-pass membrane protein {ECO:0000269|PubMed:32004469, ECO:0000269|PubMed:32004470}. Note=Agonist-binding promotes endocytosis. {ECO:0000269|PubMed:23576434}.
uniprot
proteins
transmembrane_region
TRANSMEM 114..139; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:32004469, ECO:0000269|PubMed:32004470, ECO:0007744|PDB:6P9X, ECO:0007744|PDB:6PB0"; TRANSMEM 153..176; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:32004469, ECO:0000269|PubMed:32004470, ECO:0007744|PDB:6P9X, ECO:0007744|PDB:6PB0"; TRANSMEM 186..215; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:32004469, ECO:0000269|PubMed:32004470, ECO:0007744|PDB:6P9X, ECO:0007744|PDB:6PB0"; TRANSMEM 228..249; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:32004469, ECO:0000269|PubMed:32004470, ECO:0007744|PDB:6P9X, ECO:0007744|PDB:6PB0"; TRANSMEM 268..292; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:32004469, ECO:0000269|PubMed:32004470, ECO:0007744|PDB:6P9X, ECO:0007744|PDB:6PB0"; TRANSMEM 312..329; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:32004469, ECO:0000269|PubMed:32004470, ECO:0007744|PDB:6P9X, ECO:0007744|PDB:6PB0"; TRANSMEM 339..365; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:32004469, ECO:0000269|PubMed:32004470, ECO:0007744|PDB:6P9X, ECO:0007744|PDB:6PB0
uniprot
proteins