CRFR1_CHICK
ID CRFR1_CHICK Reviewed; 420 AA.
AC Q90812;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Corticotropin-releasing factor receptor 1;
DE Short=CRF-R-1;
DE Short=CRF-R1;
DE Short=CRFR-1;
DE AltName: Full=Corticotropin-releasing hormone receptor 1;
DE Short=CRH-R-1;
DE Short=CRH-R1;
DE Flags: Precursor;
GN Name=CRHR1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=8536612; DOI=10.1210/endo.137.1.8536612;
RA Yu J., Xie L.Y., Abou-Samra A.-B.;
RT "Molecular cloning of a type A chicken corticotropin-releasing factor
RT receptor with high affinity for urotensin I.";
RL Endocrinology 137:192-197(1996).
CC -!- FUNCTION: G-protein coupled receptor for CRH (corticotropin-releasing
CC factor) and UCN (urocortin). Has high affinity for CRH and UCN. Ligand
CC binding causes a conformation change that triggers signaling via
CC guanine nucleotide-binding proteins (G proteins) and down-stream
CC effectors, such as adenylate cyclase. Promotes the activation of
CC adenylate cyclase, leading to increased intracellular cAMP levels.
CC {ECO:0000269|PubMed:8536612}.
CC -!- SUBUNIT: Interacts (via N-terminal extracellular domain) with CRF and
CC UCN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8536612};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8536612}.
CC -!- DOMAIN: The transmembrane domain is composed of seven transmembrane
CC helices that are arranged in V-shape. Transmembrane helix 7 assumes a
CC sharply kinked structure (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L41563; AAA96656.1; -; Genomic_DNA.
DR RefSeq; NP_989652.1; NM_204321.1.
DR AlphaFoldDB; Q90812; -.
DR SMR; Q90812; -.
DR STRING; 9031.ENSGALP00000000502; -.
DR PaxDb; Q90812; -.
DR GeneID; 374218; -.
DR KEGG; gga:374218; -.
DR CTD; 1394; -.
DR VEuPathDB; HostDB:geneid_374218; -.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; Q90812; -.
DR OrthoDB; 1163977at2759; -.
DR PhylomeDB; Q90812; -.
DR PRO; PR:Q90812; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0015056; F:corticotrophin-releasing factor receptor activity; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0071376; P:cellular response to corticotropin-releasing hormone stimulus; ISS:UniProtKB.
DR GO; GO:0051458; P:corticotropin secretion; ISS:UniProtKB.
DR GO; GO:2000852; P:regulation of corticosterone secretion; ISS:UniProtKB.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR003052; GPCR_2_CRF1_rcpt.
DR InterPro; IPR003051; GPCR_2_CRF_rcpt.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR01279; CRFRECEPTOR.
DR PRINTS; PR01280; CRFRECEPTOR1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..420
FT /note="Corticotropin-releasing factor receptor 1"
FT /id="PRO_0000012818"
FT TOPO_DOM 29..116
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 117..147
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 148..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 155..179
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 180..194
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 195..223
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 224..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 231..258
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 259..274
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 275..300
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 301..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 312..336
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 337..343
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 344..373
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 374..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..59
FT /evidence="ECO:0000250"
FT DISULFID 49..92
FT /evidence="ECO:0000250"
FT DISULFID 73..107
FT /evidence="ECO:0000250"
FT DISULFID 193..263
FT /evidence="ECO:0000250"
SQ SEQUENCE 420 AA; 48600 MW; 8C5C992925F62316 CRC64;
MVPGPRPALL LLLFLLQAFL LWDSPVAASI QEQYCESLLP TTNHTGPQCN ASVDLIGTCW
PRSAVGQLVA RPCPEYFYGV RYNTTNNGYR ECLANGSWAA RVNYSQCQEI LSEEKRSKLH
YHIAVIINYL GHCVSLGTLL VAFVLFMRLR SIRCLRNIIH WNLITAFILR NATWFVVQLT
MNPEVHESNV VWCRLVTAAY NYFHVTNFFW MFGEGCYLHT AIVLTYSTDK LRKWMFICIG
WCIPFPIIVA WAIGKLYYDN EKCWFGKRAG VYTDYIYQGP MILVLLINFI FLFNIVRILM
TKLRASTTSE TIQYRKAVKA TLVLLSLLGI TYMLFFVNPG EDEISRIVFI YFNSFLESFQ
GFFVSVFYCF LNSEVRSAVR KRWHRWQDKH SIRARVARAM SIPTSPTRVS FHSIKQSSAV
