ID F1RRS6_PIG Unreviewed; 415 AA.
AC F1RRS6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Corticotropin-releasing factor receptor 1 {ECO:0000256|ARBA:ARBA00021828};
GN Name=CRHR1 {ECO:0000313|Ensembl:ENSSSCP00000018346.2,
GN ECO:0000313|VGNC:VGNC:98983};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000018346.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000018346.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000018346.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000018346.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Inhibits the activity of the calcium channel CACNA1H. Required for
CC normal embryonic development of the adrenal gland and for normal
CC hormonal responses to stress. Plays a role in the response to
CC anxiogenic stimuli. {ECO:0000256|ARBA:ARBA00001996}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000256|ARBA:ARBA00005314}.
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 AlphaFoldDB; F1RRS6; -.
DR SMR; F1RRS6; -.
DR STRING; 9823.ENSSSCP00000018346; -.
DR PaxDb; 9823-ENSSSCP00000018346; -.
DR Ensembl; ENSSSCT00000018849.5; ENSSSCP00000018346.2; ENSSSCG00000017313.5.
DR VGNC; VGNC:98983; CRHR1.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000158410; -.
DR HOGENOM; CLU_002753_4_1_1; -.
DR InParanoid; F1RRS6; -.
DR OMA; NTTSQWS; -.
DR TreeFam; TF315710; -.
DR Reactome; R-SSC-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-SSC-418555; G alpha (s) signalling events.
DR Proteomes; UP000008227; Chromosome 12.
DR Bgee; ENSSSCG00000017313; Expressed in oocyte and 21 other cell types or tissues.
DR ExpressionAtlas; F1RRS6; baseline and differential.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015056; F:corticotrophin-releasing factor receptor activity; IBA:GO_Central.
DR GO; GO:0051424; F:corticotropin-releasing hormone binding; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
DR GO; GO:0048149; P:behavioral response to ethanol; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0051458; P:corticotropin secretion; IEA:Ensembl.
DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
DR GO; GO:0042596; P:fear response; IEA:Ensembl.
DR GO; GO:0051867; P:general adaptation syndrome, behavioral process; IEA:Ensembl.
DR GO; GO:2000852; P:regulation of corticosterone secretion; IEA:Ensembl.
DR CDD; cd15445; 7tmB1_CRF-R1; 1.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR017981; GPCR_2-like_7TM.
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 PANTHER; PTHR45620:SF2; CORTICOTROPIN-RELEASING FACTOR RECEPTOR 1; 1.
DR PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 1.
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; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF111418; Hormone receptor domain; 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 {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR603051-50};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..415
FT /note="Corticotropin-releasing factor receptor 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003269690"
FT TRANSMEM 121..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..106
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 119..367
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT DISULFID 30..54
FT /evidence="ECO:0000256|PIRSR:PIRSR603051-50"
FT DISULFID 44..87
FT /evidence="ECO:0000256|PIRSR:PIRSR603051-50"
FT DISULFID 68..102
FT /evidence="ECO:0000256|PIRSR:PIRSR603051-50"
FT DISULFID 188..258
FT /evidence="ECO:0000256|PIRSR:PIRSR603051-50"
SQ SEQUENCE 415 AA; 47749 MW; DEA9F494F0383ADE CRC64;
MGRRPQLRLV KALLLLGLNS ISASLQDQHC ESLSLASNVS GLQCNASVDL IGTCWPQSPA
GQLVVRPCPA YFYGVRYNTT NNGYRECLAN GTWAARVNYS ECHEILSEEK KSKVHYHVAV
IINYLGHCVS LVALLVAFVL FLRLRSIRCL RNIIHWNLIS AFILRNATWF VVQLTMSPEV
HQSNVGWCRL VTAAYNYFHV TNFFWMFGEG CYLHTAIVLT YSTDRLRKWM FICIGWGVPF
PIIVAWAIGK LYYDNEKCWF GKRPGVYTDY IYQGPMILVL LINFIFLFNI VRILMTKLRA
STTSETIQYR KAVKATLVLL PLLGITYMLF FVNPGEDEVS RVVFIYFNSF LESFQGFFVS
VFYCFLNSEV RSAIRKRWHR WQDKHSIRAR VARAMSIPTS PTRVSFHSIK QSTAV
//
