CALRL_PIG
ID CALRL_PIG Reviewed; 462 AA.
AC Q8WN93; Q867C1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 114.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Coronary artery;
RX PubMed=11714898;
RA Rorabaugh B.R., Scofield M.A., Smith D.D., Jeffries W.B., Abel P.W.;
RT "Functional calcitonin gene-related peptide subtype 2 receptors in porcine
RT coronary arteries are identified as calcitonin gene-related peptide subtype
RT 1 receptors by radioligand binding and reverse transcription-polymerase
RT chain reaction.";
RL J. Pharmacol. Exp. Ther. 299:1086-1094(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH RAMP1; RAMP2 AND
RP RAMP3.
RX PubMed=12630807; DOI=10.1291/hypres.26.s15;
RA Kikumoto K., Katafuchi T., Minamino N.;
RT "Specificity of porcine calcitonin receptor and calcitonin receptor-like
RT receptor in the presence of receptor-activity-modifying proteins.";
RL Hypertens. Res. 26:S15-S23(2003).
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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11714898, ECO:0000269|PubMed:12630807}.
CC -!- SUBUNIT: Heterodimer of CALCRL and RAMP3 (By similarity). Heterodimer
CC of CALCRL and RAMP1 or CALCRL and RAMP2 (By similarity).
CC {ECO:0000250|UniProtKB:Q16602}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11714898};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11714898}.
CC -!- TISSUE SPECIFICITY: Detected in lung and coronary artery.
CC {ECO:0000269|PubMed:11714898}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC54960.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF419317; AAL37725.1; -; mRNA.
DR EMBL; AB090162; BAC54960.1; ALT_INIT; mRNA.
DR RefSeq; NP_999260.1; NM_214095.1.
DR RefSeq; XP_005672071.1; XM_005672014.2.
DR RefSeq; XP_005672072.1; XM_005672015.2.
DR RefSeq; XP_013839785.1; XM_013984331.1.
DR AlphaFoldDB; Q8WN93; -.
DR SMR; Q8WN93; -.
DR STRING; 9823.ENSSSCP00000016986; -.
DR BindingDB; Q8WN93; -.
DR PaxDb; Q8WN93; -.
DR PeptideAtlas; Q8WN93; -.
DR PRIDE; Q8WN93; -.
DR GeneID; 397172; -.
DR KEGG; ssc:397172; -.
DR CTD; 10203; -.
DR eggNOG; KOG4564; Eukaryota.
DR HOGENOM; CLU_002753_4_2_1; -.
DR InParanoid; Q8WN93; -.
DR OMA; CVALHII; -.
DR TreeFam; TF315710; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q8WN93; SS.
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; IPI:UniProtKB.
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; IPI:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:1990408; P:calcitonin gene-related peptide receptor signaling pathway; IPI:UniProtKB.
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 1: Evidence at protein 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..462
FT /note="Calcitonin gene-related peptide type 1 receptor"
FT /id="PRO_0000373832"
FT TOPO_DOM 23..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..167
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..194
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..237
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..274
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..314
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..355
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..389
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1W5"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1W5"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..75
FT /evidence="ECO:0000250"
FT DISULFID 66..106
FT /evidence="ECO:0000250"
FT DISULFID 89..128
FT /evidence="ECO:0000250"
SQ SEQUENCE 462 AA; 53656 MW; 4585B314015B43AC CRC64;
MEKKYILYFL FLLPFFMILV IAETEEENPD DLIQLTVTRN KIMTAQYECY QKIMQDPIQQ
TEGIYCNRTW DGWLCWNDVA AGTESMQHCP DYFQDFDPSE KVTKICDQDG NWFRHPESNR
TWTNYTQCNI NTHEKVQTAL NLFYLTIIGH GLSIASLLIS LGIFFYFKSL SCQRITLHKN
LFFSFVCNSI VTIIHLTAVA NNQALVATNP VSCKVFQFIH LYLMGCNYFW MLCEGIYLHT
LIVVAVFAEK QHLMWYYFLG WGFPLIPACI HAVARRLYYN DNCWISSDTH LLYIIHGPIC
AALLVNLFFL LNIVRVLITK LKVTHQAESN LYMKAVRATL ILVPLLGIEF VLIPWRPEGK
IAEEVYDYIM HILVHYQGLL VSTIYCFFNG EVQAILRRNW NQYKIQFGNS FSHSDALRSA
SYTVSTISDG AGYSHDYPSE HLNGKSIHDM ENIVIKPEKL YD
