CALRL_HUMAN
ID CALRL_HUMAN Reviewed; 461 AA.
AC Q16602; A8K6G5; A8KAD3; Q53S02; Q53TS5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Calcitonin gene-related peptide type 1 receptor {ECO:0000305};
DE Short=CGRP type 1 receptor;
DE AltName: Full=Calcitonin receptor-like receptor;
DE Flags: Precursor;
GN Name=CALCRL {ECO:0000312|HGNC:HGNC:16709}; Synonyms=CGRPR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-8.
RC TISSUE=Lung;
RX PubMed=8626685; DOI=10.1074/jbc.271.19.11325;
RA Aiyar N., Rand K., Elshourbagy N.A., Zeng Z., Adamou J.E., Bergsma D.J.,
RA Li Y.;
RT "A cDNA encoding the calcitonin gene-related peptide type 1 receptor.";
RL J. Biol. Chem. 271:11325-11329(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-8.
RC TISSUE=Cerebellum;
RX PubMed=7818539; DOI=10.1006/bbrc.1995.1047;
RA Fluehmann B., Muff R., Hunziker W., Fischer J.A., Born W.;
RT "A human orphan calcitonin receptor-like structure.";
RL Biochem. Biophys. Res. Commun. 206:341-347(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-8.
RC TISSUE=Heart;
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP PROTEIN SEQUENCE OF 23-37.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAMP2, INVOLVEMENT IN
RP LMPHM8, VARIANT LMPHM8 VAL-205 DEL, AND CHARACTERIZATION OF VARIANT LMPHM8
RP VAL-205 DEL.
RX PubMed=30115739; DOI=10.1084/jem.20180528;
RA Mackie D.I., Al Mutairi F., Davis R.B., Kechele D.O., Nielsen N.R.,
RA Snyder J.C., Caron M.G., Kliman H.J., Berg J.S., Simms J., Poyner D.R.,
RA Caron K.M.;
RT "hCALCRL mutation causes autosomal recessive nonimmune hydrops fetalis with
RT lymphatic dysplasia.";
RL J. Exp. Med. 215:2339-2353(2018).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-133 IN COMPLEX WITH RAMP1 AND
RP ANTAGONIST, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=20826335; DOI=10.1016/j.str.2010.05.014;
RA ter Haar E., Koth C.M., Abdul-Manan N., Swenson L., Coll J.T., Lippke J.A.,
RA Lepre C.A., Garcia-Guzman M., Moore J.M.;
RT "Crystal structure of the ectodomain complex of the CGRP receptor, a class-
RT B GPCR, reveals the site of drug antagonism.";
RL Structure 18:1083-1093(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 23-136 IN COMPLEX WITH RAMP2,
RP FUNCTION, MUTAGENESIS OF TRP-72; PHE-92 AND TRP-121, AND DISULFIDE BONDS.
RX PubMed=22102369; DOI=10.1002/pro.2003;
RA Kusano S., Kukimoto-Niino M., Hino N., Ohsawa N., Okuda K., Sakamoto K.,
RA Shirouzu M., Shindo T., Yokoyama S.;
RT "Structural basis for extracellular interactions between calcitonin
RT receptor-like receptor and receptor activity-modifying protein 2 for
RT adrenomedullin-specific binding.";
RL Protein Sci. 21:199-210(2012).
CC -!- FUNCTION: Receptor for calcitonin-gene-related peptide (CGRP) together
CC with RAMP1 and receptor for adrenomedullin together with RAMP3 (By
CC similarity). Receptor for adrenomedullin together with RAMP2
CC (PubMed:22102369, PubMed:30115739). The activity of this receptor is
CC mediated by G proteins which activate adenylyl cyclase
CC (PubMed:22102369, PubMed:30115739). {ECO:0000250,
CC ECO:0000269|PubMed:22102369, ECO:0000269|PubMed:30115739}.
CC -!- SUBUNIT: Heterodimer of CALCRL and RAMP3 (By similarity). Heterodimer
CC of CALCRL and RAMP1 or CALCRL and RAMP2. {ECO:0000250,
CC ECO:0000269|PubMed:20826335, ECO:0000269|PubMed:22102369,
CC ECO:0000269|PubMed:30115739}.
CC -!- INTERACTION:
CC Q16602; P06881: CALCA; NbExp=5; IntAct=EBI-962878, EBI-962928;
CC Q16602; O60894: RAMP1; NbExp=4; IntAct=EBI-962878, EBI-962893;
CC Q16602; O60895: RAMP2; NbExp=6; IntAct=EBI-962878, EBI-9009040;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30115739};
CC Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the lung and heart.
CC -!- DISEASE: Lymphatic malformation 8 (LMPHM8) [MIM:618773]: A form of
CC primary lymphedema, a disease characterized by swelling of body parts
CC due to developmental anomalies and functional defects of the lymphatic
CC system. Adult patients with lymphedema may suffer from recurrent local
CC infections. Impaired lymphatic drainage in the fetus can develop into
CC hydrops fetalis, a severe condition characterized by excessive fluid
CC accumulation in more than two fetal extra-vascular compartments and
CC body cavities, placental enlargement and edema, pericardial or pleural
CC effusion, or ascites. LMPHM8 is an autosomal recessive form
CC characterized by onset in utero and fetal death due to non-immune
CC hydrops fetalis. {ECO:0000269|PubMed:30115739}. Note=The disease may be
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF84319.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L76380; AAC41994.1; -; mRNA.
DR EMBL; U17473; AAA62158.1; -; mRNA.
DR EMBL; AY389506; AAQ91332.1; -; mRNA.
DR EMBL; AK291630; BAF84319.1; ALT_INIT; mRNA.
DR EMBL; AK292998; BAF85687.1; -; mRNA.
DR EMBL; AC007319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074020; AAY14996.1; -; Genomic_DNA.
DR CCDS; CCDS2293.1; -.
DR PIR; JC2477; JC2477.
DR RefSeq; NP_001258680.1; NM_001271751.1.
DR RefSeq; NP_005786.1; NM_005795.5.
DR PDB; 3AQF; X-ray; 2.60 A; B=23-136.
DR PDB; 3N7P; X-ray; 2.80 A; A/B/C/J=23-133.
DR PDB; 3N7R; X-ray; 2.90 A; A/B=23-133.
DR PDB; 3N7S; X-ray; 2.10 A; A/B=23-133.
DR PDB; 4RWF; X-ray; 1.76 A; A=31-116.
DR PDB; 4RWG; X-ray; 2.44 A; A/B/C=31-114.
DR PDB; 5V6Y; X-ray; 2.80 A; A/B/C/D=29-144.
DR PDB; 6D1U; X-ray; 2.05 A; A/B/C=29-144.
DR PDB; 6E3Y; EM; 3.30 A; R=22-461.
DR PDB; 6UMG; X-ray; 2.70 A; C/c=23-133.
DR PDB; 6UUN; EM; 3.00 A; R=22-461.
DR PDB; 6UUS; EM; 2.40 A; R=22-461.
DR PDB; 6UVA; EM; 2.30 A; R=22-461.
DR PDB; 6V2E; X-ray; 1.83 A; A=29-144.
DR PDB; 6ZHO; X-ray; 1.60 A; A=34-144.
DR PDB; 6ZIS; X-ray; 1.73 A; A=31-139.
DR PDB; 7KNT; EM; 3.15 A; R=22-461.
DR PDB; 7KNU; EM; 3.49 A; R=22-461.
DR PDBsum; 3AQF; -.
DR PDBsum; 3N7P; -.
DR PDBsum; 3N7R; -.
DR PDBsum; 3N7S; -.
DR PDBsum; 4RWF; -.
DR PDBsum; 4RWG; -.
DR PDBsum; 5V6Y; -.
DR PDBsum; 6D1U; -.
DR PDBsum; 6E3Y; -.
DR PDBsum; 6UMG; -.
DR PDBsum; 6UUN; -.
DR PDBsum; 6UUS; -.
DR PDBsum; 6UVA; -.
DR PDBsum; 6V2E; -.
DR PDBsum; 6ZHO; -.
DR PDBsum; 6ZIS; -.
DR PDBsum; 7KNT; -.
DR PDBsum; 7KNU; -.
DR AlphaFoldDB; Q16602; -.
DR SMR; Q16602; -.
DR BioGRID; 115498; 7.
DR ComplexPortal; CPX-2189; CGRP receptor complex.
DR ComplexPortal; CPX-2191; Adrenomedullin receptor AM1 complex.
DR ComplexPortal; CPX-3148; Adrenomedullin receptor AM2 complex.
DR CORUM; Q16602; -.
DR DIP; DIP-37674N; -.
DR IntAct; Q16602; 4.
DR STRING; 9606.ENSP00000386972; -.
DR BindingDB; Q16602; -.
DR ChEMBL; CHEMBL3798; -.
DR DrugBank; DB16098; Atogepant.
DR DrugBank; DB14039; Erenumab.
DR DrugBank; DB04869; Olcegepant.
DR DrugBank; DB12457; Rimegepant.
DR DrugBank; DB12228; Telcagepant.
DR DrugBank; DB15328; Ubrogepant.
DR DrugBank; DB15688; Vazegepant.
DR DrugCentral; Q16602; -.
DR GuidetoPHARMACOLOGY; 47; -.
DR TCDB; 9.A.14.4.12; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q16602; 4 sites.
DR iPTMnet; Q16602; -.
DR PhosphoSitePlus; Q16602; -.
DR BioMuta; CALCRL; -.
DR DMDM; 226693507; -.
DR EPD; Q16602; -.
DR jPOST; Q16602; -.
DR MassIVE; Q16602; -.
DR PaxDb; Q16602; -.
DR PeptideAtlas; Q16602; -.
DR PRIDE; Q16602; -.
DR ProteomicsDB; 60942; -.
DR ABCD; Q16602; 1 sequenced antibody.
DR Antibodypedia; 1959; 240 antibodies from 32 providers.
DR DNASU; 10203; -.
DR Ensembl; ENST00000392370.8; ENSP00000376177.3; ENSG00000064989.13.
DR Ensembl; ENST00000409998.5; ENSP00000386972.1; ENSG00000064989.13.
DR Ensembl; ENST00000410068.5; ENSP00000387190.1; ENSG00000064989.13.
DR GeneID; 10203; -.
DR KEGG; hsa:10203; -.
DR MANE-Select; ENST00000392370.8; ENSP00000376177.3; NM_005795.6; NP_005786.1.
DR UCSC; uc002upv.6; human.
DR CTD; 10203; -.
DR DisGeNET; 10203; -.
DR GeneCards; CALCRL; -.
DR HGNC; HGNC:16709; CALCRL.
DR HPA; ENSG00000064989; Tissue enhanced (adipose tissue, lung).
DR MalaCards; CALCRL; -.
DR MIM; 114190; gene.
DR MIM; 618773; phenotype.
DR neXtProt; NX_Q16602; -.
DR OpenTargets; ENSG00000064989; -.
DR PharmGKB; PA26033; -.
DR VEuPathDB; HostDB:ENSG00000064989; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000159898; -.
DR HOGENOM; CLU_002753_4_2_1; -.
DR InParanoid; Q16602; -.
DR PhylomeDB; Q16602; -.
DR TreeFam; TF315710; -.
DR PathwayCommons; Q16602; -.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-419812; Calcitonin-like ligand receptors.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; Q16602; -.
DR BioGRID-ORCS; 10203; 11 hits in 1065 CRISPR screens.
DR ChiTaRS; CALCRL; human.
DR EvolutionaryTrace; Q16602; -.
DR GeneWiki; CALCRL; -.
DR GenomeRNAi; 10203; -.
DR Pharos; Q16602; Tclin.
DR PRO; PR:Q16602; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q16602; protein.
DR Bgee; ENSG00000064989; Expressed in right lung and 148 other tissues.
DR ExpressionAtlas; Q16602; baseline and differential.
DR Genevisible; Q16602; HS.
DR GO; GO:1903143; C:adrenomedullin receptor complex; IDA:UniProtKB.
DR GO; GO:1990406; C:CGRP receptor complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:1990409; F:adrenomedullin binding; IPI:UniProtKB.
DR GO; GO:0001605; F:adrenomedullin receptor activity; IPI:UniProtKB.
DR GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; IPI:UniProtKB.
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:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
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; IDA:UniProtKB.
DR GO; GO:1990408; P:calcitonin gene-related peptide receptor signaling pathway; IPI:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0071329; P:cellular response to sucrose stimulus; IDA:UniProtKB.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0045986; P:negative regulation of smooth muscle contraction; IEA:Ensembl.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IDA:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disease variant;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 23..461
FT /note="Calcitonin gene-related peptide type 1 receptor"
FT /id="PRO_0000012811"
FT TOPO_DOM 23..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..461
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 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 DISULFID 48..74
FT DISULFID 65..105
FT DISULFID 88..127
FT VARIANT 8
FT /note="Y -> N (in dbSNP:rs698577)"
FT /evidence="ECO:0000269|PubMed:7818539,
FT ECO:0000269|PubMed:8626685, ECO:0000269|Ref.3"
FT /id="VAR_054822"
FT VARIANT 16
FT /note="F -> L (in dbSNP:rs13391909)"
FT /id="VAR_049453"
FT VARIANT 205
FT /note="Missing (in LMPHM8; unknown pathological
FT significance; decreased function in adenylate cyclase-
FT modulating G protein-coupled receptor signaling pathway;
FT decreased interaction with RAMP2; decreased protein levels
FT at the cell membrane)"
FT /evidence="ECO:0000269|PubMed:30115739"
FT /id="VAR_083775"
FT VARIANT 274
FT /note="R -> I (in dbSNP:rs34010553)"
FT /id="VAR_049454"
FT MUTAGEN 72
FT /note="W->A: Strongly reduced affinity for adrenomedullin."
FT /evidence="ECO:0000269|PubMed:22102369"
FT MUTAGEN 92
FT /note="F->A: Strongly reduced affinity for adrenomedullin."
FT /evidence="ECO:0000269|PubMed:22102369"
FT MUTAGEN 121
FT /note="W->A: Strongly reduced affinity for adrenomedullin."
FT /evidence="ECO:0000269|PubMed:22102369"
FT CONFLICT 144
FT /note="L -> Q (in Ref. 4; BAF84319)"
FT /evidence="ECO:0000305"
FT HELIX 35..54
FT /evidence="ECO:0007829|PDB:6ZHO"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:4RWF"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3N7S"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6ZHO"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6UUN"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6ZHO"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6V2E"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:6ZHO"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:6UUN"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6ZHO"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7KNT"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:6ZHO"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6ZIS"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:6ZHO"
FT HELIX 148..165
FT /evidence="ECO:0007829|PDB:7KNT"
FT HELIX 172..197
FT /evidence="ECO:0007829|PDB:6UVA"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:6UVA"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:6UVA"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:6UVA"
FT HELIX 211..241
FT /evidence="ECO:0007829|PDB:6UVA"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:7KNT"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:6UVA"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6UVA"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:6UVA"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:6UVA"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:6UVA"
FT HELIX 292..320
FT /evidence="ECO:0007829|PDB:6UVA"
FT HELIX 331..345
FT /evidence="ECO:0007829|PDB:6UVA"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:6UVA"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:6E3Y"
FT HELIX 364..384
FT /evidence="ECO:0007829|PDB:6UVA"
FT TURN 385..387
FT /evidence="ECO:0007829|PDB:7KNT"
FT HELIX 389..398
FT /evidence="ECO:0007829|PDB:6UVA"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:6UVA"
SQ SEQUENCE 461 AA; 52979 MW; DAD6253283088CB4 CRC64;
MEKKCTLYFL VLLPFFMILV TAELEESPED SIQLGVTRNK IMTAQYECYQ KIMQDPIQQA
EGVYCNRTWD GWLCWNDVAA GTESMQLCPD YFQDFDPSEK VTKICDQDGN WFRHPASNRT
WTNYTQCNVN THEKVKTALN LFYLTIIGHG LSIASLLISL GIFFYFKSLS CQRITLHKNL
FFSFVCNSVV TIIHLTAVAN NQALVATNPV SCKVSQFIHL YLMGCNYFWM LCEGIYLHTL
IVVAVFAEKQ HLMWYYFLGW GFPLIPACIH AIARSLYYND NCWISSDTHL LYIIHGPICA
ALLVNLFFLL NIVRVLITKL KVTHQAESNL YMKAVRATLI LVPLLGIEFV LIPWRPEGKI
AEEVYDYIMH ILMHFQGLLV STIFCFFNGE VQAILRRNWN QYKIQFGNSF SNSEALRSAS
YTVSTISDGP GYSHDCPSEH LNGKSIHDIE NVLLKPENLY N
