ID RAMP1_HUMAN Reviewed; 148 AA. AC O60894; Q6FGS5; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 24-JAN-2024, entry version 185. DE RecName: Full=Receptor activity-modifying protein 1; DE AltName: Full=Calcitonin-receptor-like receptor activity-modifying protein 1; DE Short=CRLR activity-modifying protein 1; DE Flags: Precursor; GN Name=RAMP1; 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], FUNCTION, TISSUE SPECIFICITY, AND TOPOLOGY. RC TISSUE=Neuroblastoma; RX PubMed=9620797; DOI=10.1038/30666; RA McLatchie L.M., Fraser N.J., Main M.J., Wise A., Brown J., Thompson N., RA Solari R., Lee M.G., Foord S.M.; RT "RAMPs regulate the transport and ligand specificity of the calcitonin- RT receptor-like receptor."; RL Nature 393:333-339(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-112, SUBUNIT, AND DISULFIDE RP BONDS. RX PubMed=18725456; DOI=10.1110/ps.036012.108; RA Kusano S., Kukimoto-Niino M., Akasaka R., Toyama M., Terada T., RA Shirouzu M., Shindo T., Yokoyama S.; RT "Crystal structure of the human receptor activity-modifying protein 1 RT extracellular domain."; RL Protein Sci. 17:1907-1914(2008). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 26-117 IN COMPLEX WITH CALRL 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). CC -!- FUNCTION: Transports the calcitonin gene-related peptide type 1 CC receptor (CALCRL) to the plasma membrane. Acts as a receptor for CC calcitonin-gene-related peptide (CGRP) together with CALCRL. CC {ECO:0000269|PubMed:9620797}. CC -!- SUBUNIT: Heterodimer of CALCRL and RAMP1. {ECO:0000269|PubMed:18725456, CC ECO:0000269|PubMed:20826335}. CC -!- INTERACTION: CC O60894; Q16602: CALCRL; NbExp=4; IntAct=EBI-962893, EBI-962878; CC O60894; P21145: MAL; NbExp=3; IntAct=EBI-962893, EBI-3932027; CC O60894; Q5J8X5: MS4A13; NbExp=3; IntAct=EBI-962893, EBI-12070086; CC O60894; Q16617: NKG7; NbExp=3; IntAct=EBI-962893, EBI-3919611; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in many tissues including the uterus, CC bladder, brain, pancreas and gastro-intestinal tract. CC {ECO:0000269|PubMed:9620797}. CC -!- SIMILARITY: Belongs to the RAMP family. {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; AJ001014; CAA04472.1; -; mRNA. DR EMBL; AY265457; AAP23298.1; -; mRNA. DR EMBL; CR542032; CAG46829.1; -; mRNA. DR EMBL; CR542044; CAG46841.1; -; mRNA. DR EMBL; CH471063; EAW71127.1; -; Genomic_DNA. DR EMBL; BC000548; AAH00548.1; -; mRNA. DR CCDS; CCDS2522.1; -. DR RefSeq; NP_005846.1; NM_005855.3. DR PDB; 2YX8; X-ray; 2.40 A; A=27-112. DR PDB; 3N7P; X-ray; 2.80 A; D/E/F/R=26-117. DR PDB; 3N7R; X-ray; 2.90 A; C/D=26-117. DR PDB; 3N7S; X-ray; 2.10 A; C/D=26-117. DR PDB; 4RWG; X-ray; 2.44 A; A/B/C=24-108. DR PDB; 5V6Y; X-ray; 2.80 A; A/B/C/D=24-111. DR PDB; 6D1U; X-ray; 2.05 A; A/B/C=24-111. DR PDB; 6E3Y; EM; 3.30 A; E=27-148. DR PDB; 6UMG; X-ray; 2.70 A; R/r=26-117. DR PDB; 6ZHO; X-ray; 1.60 A; A=24-109. DR PDB; 6ZIS; X-ray; 1.73 A; A=24-111. DR PDB; 7KNT; EM; 3.15 A; E=27-148. DR PDB; 7KNU; EM; 3.49 A; E=27-148. DR PDB; 7P0F; X-ray; 1.85 A; A=24-111. DR PDB; 7P0I; X-ray; 2.30 A; A=24-111. DR PDB; 7TYF; EM; 2.20 A; E=27-148. DR PDB; 7TYW; EM; 3.00 A; E=27-148. DR PDB; 8AX5; X-ray; 2.75 A; A=24-111. DR PDB; 8AX6; X-ray; 1.90 A; A=24-111. DR PDB; 8AX7; X-ray; 1.65 A; A=24-111. DR PDBsum; 2YX8; -. DR PDBsum; 3N7P; -. DR PDBsum; 3N7R; -. DR PDBsum; 3N7S; -. DR PDBsum; 4RWG; -. DR PDBsum; 5V6Y; -. DR PDBsum; 6D1U; -. DR PDBsum; 6E3Y; -. DR PDBsum; 6UMG; -. DR PDBsum; 6ZHO; -. DR PDBsum; 6ZIS; -. DR PDBsum; 7KNT; -. DR PDBsum; 7KNU; -. DR PDBsum; 7P0F; -. DR PDBsum; 7P0I; -. DR PDBsum; 7TYF; -. DR PDBsum; 7TYW; -. DR PDBsum; 8AX5; -. DR PDBsum; 8AX6; -. DR PDBsum; 8AX7; -. DR AlphaFoldDB; O60894; -. DR EMDB; EMD-22962; -. DR EMDB; EMD-22963; -. DR EMDB; EMD-26178; -. DR EMDB; EMD-26196; -. DR EMDB; EMD-8978; -. DR SMR; O60894; -. DR BioGRID; 115558; 46. DR ComplexPortal; CPX-2173; Amylin receptor 1 complex. DR ComplexPortal; CPX-2189; CGRP receptor complex. DR CORUM; O60894; -. DR DIP; DIP-37675N; -. DR IntAct; O60894; 5. DR STRING; 9606.ENSP00000254661; -. DR BindingDB; O60894; -. DR ChEMBL; CHEMBL2107838; -. DR ChEMBL; CHEMBL2111189; -. DR DrugBank; DB01278; Pramlintide. DR DrugCentral; O60894; -. DR GuidetoPHARMACOLOGY; 51; -. DR TCDB; 8.A.127.1.1; the receptor activity-modifying protein (ramp) family. DR iPTMnet; O60894; -. DR PhosphoSitePlus; O60894; -. DR BioMuta; RAMP1; -. DR MassIVE; O60894; -. DR PaxDb; 9606-ENSP00000254661; -. DR PeptideAtlas; O60894; -. DR ProteomicsDB; 49657; -. DR Antibodypedia; 34486; 262 antibodies from 39 providers. DR DNASU; 10267; -. DR Ensembl; ENST00000254661.5; ENSP00000254661.4; ENSG00000132329.11. DR GeneID; 10267; -. DR KEGG; hsa:10267; -. DR MANE-Select; ENST00000254661.5; ENSP00000254661.4; NM_005855.4; NP_005846.1. DR UCSC; uc002vxj.4; human. DR AGR; HGNC:9843; -. DR CTD; 10267; -. DR DisGeNET; 10267; -. DR GeneCards; RAMP1; -. DR HGNC; HGNC:9843; RAMP1. DR HPA; ENSG00000132329; Tissue enhanced (endometrium). DR MIM; 605153; gene. DR neXtProt; NX_O60894; -. DR OpenTargets; ENSG00000132329; -. DR PharmGKB; PA34202; -. DR VEuPathDB; HostDB:ENSG00000132329; -. DR eggNOG; ENOG502S0TC; Eukaryota. DR GeneTree; ENSGT00940000159224; -. DR InParanoid; O60894; -. DR OMA; CYWPNRM; -. DR OrthoDB; 4199890at2759; -. DR PhylomeDB; O60894; -. DR TreeFam; TF333286; -. DR PathwayCommons; O60894; -. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR Reactome; R-HSA-419812; Calcitonin-like ligand receptors. DR SignaLink; O60894; -. DR BioGRID-ORCS; 10267; 11 hits in 1153 CRISPR screens. DR ChiTaRS; RAMP1; human. DR EvolutionaryTrace; O60894; -. DR GeneWiki; RAMP1; -. DR GenomeRNAi; 10267; -. DR Pharos; O60894; Tclin. DR PRO; PR:O60894; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; O60894; Protein. DR Bgee; ENSG00000132329; Expressed in body of uterus and 193 other cell types or tissues. DR ExpressionAtlas; O60894; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:1990406; C:CGRP receptor complex; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0043235; C:receptor complex; IDA:UniProtKB. DR GO; GO:0097643; F:amylin receptor activity; IPI:UniProtKB. DR GO; GO:1990407; F:calcitonin gene-related peptide binding; IPI:UniProtKB. DR GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; IPI:UniProtKB. DR GO; GO:0015026; F:coreceptor activity; IBA:GO_Central. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0097647; P:amylin receptor signaling pathway; IDA: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:0032870; P:cellular response to hormone stimulus; IBA:GO_Central. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0060050; P:positive regulation of protein glycosylation; IDA:UniProtKB. DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB. DR GO; GO:0015031; P:protein transport; IDA:UniProtKB. DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB. DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro. DR Gene3D; 1.10.150.510; Receptor activity modifying family; 1. DR InterPro; IPR006985; RAMP. DR InterPro; IPR038126; RAMP_sf. DR PANTHER; PTHR14076; RECEPTOR ACTIVITY MODIFYING PROTEIN RAMP; 1. DR PANTHER; PTHR14076:SF3; RECEPTOR ACTIVITY-MODIFYING PROTEIN 1; 1. DR Pfam; PF04901; RAMP; 1. DR Genevisible; O60894; HS. PE 1: Evidence at protein level; KW 3D-structure; Disulfide bond; Membrane; Receptor; Reference proteome; KW Signal; Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1..26 FT /evidence="ECO:0000255" FT CHAIN 27..148 FT /note="Receptor activity-modifying protein 1" FT /id="PRO_0000030168" FT TOPO_DOM 27..117 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 118..138 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 139..148 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DISULFID 27..82 FT DISULFID 40..72 FT DISULFID 57..104 FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:6D1U" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:6ZHO" FT HELIX 32..39 FT /evidence="ECO:0007829|PDB:6ZHO" FT HELIX 41..51 FT /evidence="ECO:0007829|PDB:6ZHO" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:6ZHO" FT HELIX 59..79 FT /evidence="ECO:0007829|PDB:6ZHO" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:7TYF" FT HELIX 87..100 FT /evidence="ECO:0007829|PDB:6ZHO" FT TURN 101..103 FT /evidence="ECO:0007829|PDB:6ZIS" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:3N7S" FT HELIX 116..142 FT /evidence="ECO:0007829|PDB:7TYF" SQ SEQUENCE 148 AA; 16988 MW; 8530DD590BAEBE5C CRC64; MARALCRLPR RGLWLLLAHH LFMTTACQEA NYGALLRELC LTQFQVDMEA VGETLWCDWG RTIRSYRELA DCTWHMAEKL GCFWPNAEVD RFFLAVHGRY FRSCPISGRA VRDPPGSILY PFIVVPITVT LLVTALVVWQ SKRTEGIV //