CALRL_RAT
ID CALRL_RAT Reviewed; 464 AA.
AC Q63118;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
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; Synonyms=Cgrpr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Lung;
RX PubMed=8222502; DOI=10.1042/cs0850385;
RA Njuki F., Nicholl C.G., Howard A., Mak J.C., Barnes P.J., Girgis S.I.,
RA Legon S.;
RT "A new calcitonin-receptor-like sequence in rat pulmonary blood vessels.";
RL Clin. Sci. 85:385-388(1993).
CC -!- FUNCTION: Receptor for calcitonin-gene-related peptide (CGRP) together
CC with RAMP1 and receptor for adrenomedullin together with RAMP2 or
CC RAMP3. The activity of this receptor is mediated by G proteins which
CC activate adenylyl cyclase. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of CALCRL and RAMP1, RAMP2 or RAMP3.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; X70658; CAA49997.1; -; mRNA.
DR PIR; I60194; I60194.
DR RefSeq; NP_036849.1; NM_012717.1.
DR RefSeq; XP_006234500.1; XM_006234438.3.
DR RefSeq; XP_006234501.1; XM_006234439.3.
DR AlphaFoldDB; Q63118; -.
DR SMR; Q63118; -.
DR BioGRID; 247109; 4.
DR ComplexPortal; CPX-244; Adrenomedullin receptor AM1 complex.
DR ComplexPortal; CPX-245; Adrenomedullin receptor AM2 complex.
DR ComplexPortal; CPX-248; CGRP receptor complex.
DR STRING; 10116.ENSRNOP00000006462; -.
DR BindingDB; Q63118; -.
DR ChEMBL; CHEMBL4755; -.
DR GuidetoPHARMACOLOGY; 47; -.
DR GlyGen; Q63118; 6 sites.
DR iPTMnet; Q63118; -.
DR PhosphoSitePlus; Q63118; -.
DR PaxDb; Q63118; -.
DR Ensembl; ENSRNOT00000078645; ENSRNOP00000074452; ENSRNOG00000054695.
DR GeneID; 25029; -.
DR KEGG; rno:25029; -.
DR UCSC; RGD:2255; rat.
DR CTD; 10203; -.
DR RGD; 2255; Calcrl.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000159898; -.
DR HOGENOM; CLU_002753_4_2_1; -.
DR InParanoid; Q63118; -.
DR OMA; CVALHII; -.
DR OrthoDB; 1005634at2759; -.
DR PhylomeDB; Q63118; -.
DR TreeFam; TF315710; -.
DR Reactome; R-RNO-419812; Calcitonin-like ligand receptors.
DR PRO; PR:Q63118; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000054695; Expressed in lung and 18 other tissues.
DR Genevisible; Q63118; RN.
DR GO; GO:1903143; C:adrenomedullin receptor complex; ISO:RGD.
DR GO; GO:1990406; C:CGRP receptor complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:1990409; F:adrenomedullin binding; ISO:RGD.
DR GO; GO:0001605; F:adrenomedullin receptor activity; ISO:RGD.
DR GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1990410; P:adrenomedullin receptor signaling pathway; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:1990408; P:calcitonin gene-related peptide receptor signaling pathway; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0071329; P:cellular response to sucrose stimulus; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:RGD.
DR GO; GO:0045986; P:negative regulation of smooth muscle contraction; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; ISO:RGD.
DR GO; GO:0031623; P:receptor internalization; ISO:RGD.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IEA:Ensembl.
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; Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..464
FT /note="Calcitonin gene-related peptide type 1 receptor"
FT /id="PRO_0000012813"
FT TOPO_DOM 24..146
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..166
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..193
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..236
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..273
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..313
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..354
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..366
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..388
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1W5"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1W5"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
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 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..74
FT /evidence="ECO:0000250"
FT DISULFID 65..105
FT /evidence="ECO:0000250"
FT DISULFID 88..127
FT /evidence="ECO:0000250"
SQ SEQUENCE 464 AA; 53329 MW; 7373EC94B0FBC33C CRC64;
MMDKKCTLCF LFLLLLNMAL IAAESEEGAN QTDLGVTRNK IMTAQYECYQ KIMQDPIQQG
EGLYCNRTWD GWLCWNDVAA GTESMQYCPD YFQDFDPSEK VTKICDQDGN WFRHPDSNRT
WTNYTLCNNS THEKVKTALN LFYLTIIGHG LSIASLIISL IIFFYFKSLS CQRITLHKNL
FFSFVCNSIV TIIHLTAVAN NQALVATNPV SCKVSQFIHL YLMGCNYFWM LCEGIYLHTL
IVVAVFAEKQ HLMWYYFLGW GFPLLPACIH AIARSLYYND NCWISSDTHL LYIIHGPICA
ALLVNLFFLL NIVRVLITKL KVTHQAESNL YMKAVRATLI LVPLLGIEFV LFPWRPEGKV
AEEVYDYVMH ILMHYQGLLV STIFCFFNGE VQAILRRNWN QYKIQFGNGF SHSDALRSAS
YTVSTISDVQ GYSHDCPTEH LNGKSIQDIE NVALKPEKMY DLVM
