CALRL_XENLA
ID CALRL_XENLA Reviewed; 476 AA.
AC Q7ZXS8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
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;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) 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}.
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DR EMBL; BC044269; AAH44269.1; -; mRNA.
DR RefSeq; NP_001080206.1; NM_001086737.1.
DR AlphaFoldDB; Q7ZXS8; -.
DR SMR; Q7ZXS8; -.
DR DNASU; 379898; -.
DR GeneID; 379898; -.
DR KEGG; xla:379898; -.
DR CTD; 379898; -.
DR Xenbase; XB-GENE-5736144; calcrl.L.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 379898; Expressed in spleen and 19 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:0004948; F:calcitonin receptor activity; IEA:InterPro.
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..33
FT /evidence="ECO:0000255"
FT CHAIN 34..476
FT /note="Calcitonin gene-related peptide type 1 receptor"
FT /id="PRO_0000373836"
FT TOPO_DOM 34..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..181
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..208
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..251
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..288
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..328
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..369
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..381
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..403
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..89
FT /evidence="ECO:0000250"
FT DISULFID 80..120
FT /evidence="ECO:0000250"
FT DISULFID 103..142
FT /evidence="ECO:0000250"
SQ SEQUENCE 476 AA; 54982 MW; 79A839A8F46551B3 CRC64;
METLQMGLLS RSALFKYIII FLIMINTRGY VLASQEQEAK TSVPEERQVG VTQNKIMTAQ
YECYQKIMQE PAHGKEGQFC NRTWDGWLCW GDVAAGIISE QRCPDYFQDF DPSEKVTKEC
GKNGHWFRHP DSNRTWTNYT RCNTFTHEKV KTALNLYYLT IIGHGLSIAS LLISLGIFFY
FKNLSCQRIT LHKNLFFSFV CNSIITIISL SAVANNQALV ATNPVICKIS QFIHLYLMGC
NYFWMLCEGI YLHTLIVVAV FAEKQHLMWY YLLGWGFPLI PACIHAVARS LYYNDNCWIS
SETHLLYIIH GPICAALLVN LFFLLNIVRV LITKLKVTHQ AESNLYMKAV RATLILVPLL
GIEFVLFPWK PEGRIAEEIY DYVMHILMHY QGLLVATIFC FFNGEVQAVL KRHWNQYRIQ
FGSFAHSEGL RSASYTVSSI SEIQGTTYTH DYSEHSNGKN CHDMENVFFK TEKQYM
