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 24-JAN-2024, entry version 199. 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}; 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; 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 PDB; 7P0F; X-ray; 1.85 A; A=29-144. DR PDB; 7P0I; X-ray; 2.30 A; A=29-144. DR PDB; 8AX5; X-ray; 2.75 A; A=29-144. DR PDB; 8AX6; X-ray; 1.90 A; A=29-144. DR PDB; 8AX7; X-ray; 1.65 A; A=29-144. 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 PDBsum; 7P0F; -. DR PDBsum; 7P0I; -. DR PDBsum; 8AX5; -. DR PDBsum; 8AX6; -. DR PDBsum; 8AX7; -. DR AlphaFoldDB; Q16602; -. DR EMDB; EMD-20883; -. DR EMDB; EMD-20901; -. DR EMDB; EMD-20906; -. DR EMDB; EMD-22962; -. DR EMDB; EMD-22963; -. DR EMDB; EMD-8978; -. 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.ENSP00000376177; -. 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; Zavegepant. DR DrugCentral; Q16602; -. DR GuidetoPHARMACOLOGY; 47; -. DR TCDB; 9.A.14.4.12; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; Q16602; 3 sites, No reported glycans. 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; 9606-ENSP00000386972; -. DR PeptideAtlas; Q16602; -. DR ProteomicsDB; 60942; -. DR ABCD; Q16602; 1 sequenced antibody. DR Antibodypedia; 1959; 309 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 AGR; HGNC:16709; -. 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 Orphanet; 363999; Non-immune hydrops fetalis. 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 OMA; AIVICIY; -. DR OrthoDB; 5345963at2759; -. 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 SignaLink; Q16602; -. DR BioGRID-ORCS; 10203; 12 hits in 1145 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 150 other cell types or tissues. DR ExpressionAtlas; Q16602; baseline and differential. 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: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: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: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: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 CDD; cd15274; 7tmB1_calcitonin_R; 1. DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR003287; GCPR_2_calcitonin_rcpt_fam. DR InterPro; IPR017981; GPCR_2-like_7TM. 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 PANTHER; PTHR45620:SF21; CALCITONIN GENE-RELATED PEPTIDE TYPE 1 RECEPTOR; 1. DR PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 1. 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; SSF81321; Family A G protein-coupled receptor-like; 1. DR SUPFAM; SSF111418; Hormone receptor domain; 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. DR Genevisible; Q16602; HS. 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; uncertain significance; FT decreased function in adenylate cyclase-modulating G FT protein-coupled receptor signaling pathway; decreased FT interaction with RAMP2; decreased protein levels at the FT 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 //