CRFR2_XENLA
ID CRFR2_XENLA Reviewed; 413 AA.
AC O42603;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Corticotropin-releasing factor receptor 2;
DE Short=CRF-R-2;
DE Short=CRF-R2;
DE Short=CRFR-2;
DE AltName: Full=Corticotropin-releasing hormone receptor 2;
DE Short=CRH-R-2;
DE Short=CRH-R2;
GN Name=crhr2; Synonyms=crf2;
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].
RC TISSUE=Brain, and Heart;
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), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN.
CC Ligand 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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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 -!- DOMAIN: The uncleaved pseudo signal peptide prevents receptor's
CC oligomerization and coupling to G(i) subunits. It is also responsible
CC for the rather low receptor localization at the plasma membrane (By
CC similarity). {ECO:0000250}.
CC -!- PTM: A N-glycosylation site within the signal peptide impedes its
CC proper cleavage and function. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; Y14037; CAA74364.1; -; mRNA.
DR RefSeq; NP_001079300.1; NM_001085831.1.
DR AlphaFoldDB; O42603; -.
DR SMR; O42603; -.
DR GeneID; 378608; -.
DR KEGG; xla:378608; -.
DR CTD; 378608; -.
DR Xenbase; XB-GENE-990954; crhr2.S.
DR OrthoDB; 1163977at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 378608; Expressed in brain and 6 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR003053; GPCR_2_CRF2_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; PR01281; CRFRECEPTOR2.
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 CHAIN 1..413
FT /note="Corticotropin-releasing factor receptor 2"
FT /id="PRO_0000012823"
FT SIGNAL 1..22
FT /note="Not cleaved"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1..110
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 111..141
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 142..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 149..173
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 174..187
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 188..216
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 217..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 224..251
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 252..267
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 268..293
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 294..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 305..329
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 330..336
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 337..366
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 367..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 17..53
FT /evidence="ECO:0000250"
FT DISULFID 43..86
FT /evidence="ECO:0000250"
FT DISULFID 67..101
FT /evidence="ECO:0000250"
FT DISULFID 186..256
FT /evidence="ECO:0000250"
SQ SEQUENCE 413 AA; 48459 MW; DAD422F0A96C4626 CRC64;
MDSTIFEIII DEFDANCSLL DAFQDSFLHS ESSSFFGFEG PYCSATIDQI GTCWPRSLAG
ELVERPCPDS FNGIRYNTTR NVYRECFENG TWASWMNYSQ CVPILDNKRK YALHYKIALI
INYLGHCISI LALVIAFLLF LCLRSIRCLR NIIHWNLITT FILRNIMWFL LQMIDHNIHE
SNEVWCRCIT TIYNYFVVTN FFWMFVEGCY LHTAIVMTYS TDKLRKWVFL FIGWCIPSPI
IVTWAICKLF YENEQCWIGK EPGKYIDYIY QGRVILVLLI NFVFLFNIVR ILMTKLRAST
TSETIQYRKA VKATLVLLPL LGITYMLFFV NPGEDDVSQI VFIYFNSFLQ SFQGFFVSVF
YCFLNGEVRS AARKRWHRWQ DHHSLRVRVA RAMSIPTSPT RISFHSIKQT AAV
