CALRL_XENTR
ID CALRL_XENTR Reviewed; 472 AA.
AC Q0P4Y4; Q28DX2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Calcitonin gene-related peptide type 1 receptor;
DE Short=CGRP type 1 receptor;
DE AltName: Full=Calcitonin receptor-like receptor;
DE Flags: Precursor;
GN Name=calcrl; ORFNames=TEgg071c13.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for calcitonin-gene-related peptide (CGRP) (By
CC similarity). Receptor specificity may be modulated by accessory
CC proteins. The activity of this receptor is mediated by G proteins which
CC activate adenylyl cyclase (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAJ81879.1; Type=Erroneous initiation; Evidence={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; CR848554; CAJ81879.1; ALT_INIT; mRNA.
DR EMBL; BC121843; AAI21844.1; -; mRNA.
DR RefSeq; NP_001016893.1; NM_001016893.3.
DR RefSeq; XP_012825895.1; XM_012970441.2.
DR RefSeq; XP_012825896.1; XM_012970442.2.
DR AlphaFoldDB; Q0P4Y4; -.
DR SMR; Q0P4Y4; -.
DR PaxDb; Q0P4Y4; -.
DR Ensembl; ENSXETT00000074242; ENSXETP00000066641; ENSXETG00000013895.
DR GeneID; 549647; -.
DR KEGG; xtr:549647; -.
DR CTD; 10203; -.
DR Xenbase; XB-GENE-5736126; calcrl.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; Q0P4Y4; -.
DR OrthoDB; 1005634at2759; -.
DR Reactome; R-XTR-419812; Calcitonin-like ligand receptors.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000013895; Expressed in heart and 14 other tissues.
DR ExpressionAtlas; Q0P4Y4; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001605; F:adrenomedullin receptor activity; IBA:GO_Central.
DR GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004948; F:calcitonin receptor activity; IEA:InterPro.
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:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR003287; GCPR_2_calcitonin_rcpt_fam.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR003289; GPCR_2_CGRP1_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; PR01351; CGRPRECEPTOR.
DR PRINTS; PR01350; CTRFAMILY.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..472
FT /note="Calcitonin gene-related peptide type 1 receptor"
FT /id="PRO_0000373837"
FT TOPO_DOM 29..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..176
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..203
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..246
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..283
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..323
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..364
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..398
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..84
FT /evidence="ECO:0000250"
FT DISULFID 75..115
FT /evidence="ECO:0000250"
FT DISULFID 98..137
FT /evidence="ECO:0000250"
SQ SEQUENCE 472 AA; 54404 MW; 9B87E6D6DB280AB8 CRC64;
MGLLLRSALF KYIIIVLIML NLRGYVLAEQ EQGSQIPLEE IIQVGVTRNK IMTAQYECYQ
KIMQEPANGK EGHFCNRTWD GWLCWGDVSA GVISEQRCPD YFQDFDPSEK VTKECGKNGH
WFRHPDSNRT WTNYTRCNTF THEKVKTALN LYYLTIIGHG LSIASLLISL GIFFYFKNLS
CQRITLHKNL FFSFVCNSII TIISLSAVAN NQALVATNPV SCKISQFIHL YLMGCNYFWM
LCEGIYLHTL IVVAVFAEKQ HLMWYYLLGW GFPLIPACIH AVARSLYYND NCWISSETHL
LYIIHGPICA ALLVNLFFLL NIVRVLITKL KVTHQAESNL YMKAVRATLI LVPLLGIEFV
LFPWKPEGRI AEEIYDYVMH ILMHYQGLLV ATIFCFFNGE VQAVLKRHWN QYKIQFGSSF
AHSEGLRSAS YTVSSISEIQ GTTYTHDYSE QSNGKNCHDM ENVFFKTEKQ YM