CRFR1_XENLA
ID CRFR1_XENLA Reviewed; 415 AA.
AC O42602;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
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; Synonyms=crf1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=9326293; DOI=10.1046/j.1471-4159.1997.69041640.x;
RA Dautzenberg F.M., Dietrich K., Palchaudhuri M.R., Spiess J.;
RT "Identification of two corticotropin-releasing factor receptors from
RT Xenopus laevis with high ligand selectivity: unusual pharmacology of the
RT type 1 receptor.";
RL J. Neurochem. 69:1640-1649(1997).
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:9326293}.
CC -!- SUBUNIT: Interacts (via N-terminal extracellular domain) with CRF and
CC UCN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9326293};
CC Multi-pass membrane protein {ECO:0000269|PubMed:9326293}.
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}.
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DR EMBL; Y14036; CAA74363.1; -; mRNA.
DR RefSeq; NP_001079049.1; NM_001085580.1.
DR AlphaFoldDB; O42602; -.
DR SMR; O42602; -.
DR GeneID; 373580; -.
DR KEGG; xla:373580; -.
DR CTD; 373580; -.
DR Xenbase; XB-GENE-968270; crhr1.2.S.
DR OrthoDB; 1163977at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 373580; Expressed in brain and 3 other tissues.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..415
FT /note="Corticotropin-releasing factor receptor 1"
FT /id="PRO_0000012819"
FT TOPO_DOM 25..111
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 112..142
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 143..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 150..174
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 175..189
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 190..218
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 219..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 226..253
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 254..269
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 270..295
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 296..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 307..331
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 332..338
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 339..368
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 369..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..54
FT /evidence="ECO:0000250"
FT DISULFID 44..87
FT /evidence="ECO:0000250"
FT DISULFID 68..102
FT /evidence="ECO:0000250"
FT DISULFID 188..258
FT /evidence="ECO:0000250"
SQ SEQUENCE 415 AA; 47786 MW; 74ED24C17907B74D CRC64;
MLLAKTPCLL LVQVIAAGIS FALTSLQDQC ETLQHNSNFT GLACNASIDM IGTCWPSTAA
GQMVARPCPE YFHGVQYNTT GNVYRECHLN GSWAGRGDYA QCQEILKQEK KTKVHYHIAI
VINFLGHSIS LCALLVAFIL FLRLRSIRCL RNIIHWNLIT AFILRNVTWF VMQLTLSHEA
HDSNVVWCRL VTIAHNYFYV TNFFWMFGEG CYLHTAIVLT YSTDKLRKWM FICIGWCIPF
PIIVAWAIGK LYYDNEKCWF GKKAGVYTDF IYQGPVILVL LINFIFLFNI VRILMTKLRA
STTSETIQYR KAVKATLVLL PLLGITYMLF FVTPGEDEIS RIVFIYFNSF LQSFQGFFVS
VFYCFLNSEV RSAVRKRWHR WQDKHSIRAR VARAMSIPTS PTRISFHSIK QSSAI
