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 13-FEB-2019, entry version 159. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND RP 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., RA Thompson N., Solari R., Lee M.G., Foord S.M.; RT "RAMPs regulate the transport and ligand specificity of the RT calcitonin-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 RT sequenced by 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RP DISULFIDE 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 RP AND 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., RA Lippke J.A., Lepre C.A., Garcia-Guzman M., Moore J.M.; RT "Crystal structure of the ectodomain complex of the CGRP receptor, a RT class-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. CC {ECO:0000269|PubMed:18725456, ECO:0000269|PubMed:20826335}. CC -!- INTERACTION: CC Q16602:CALCRL; NbExp=3; IntAct=EBI-962893, EBI-962878; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- TISSUE SPECIFICITY: Expressed in many tissues including the CC uterus, 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 UniGene; Hs.471783; -. 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 PDBsum; 2YX8; -. DR PDBsum; 3N7P; -. DR PDBsum; 3N7R; -. DR PDBsum; 3N7S; -. DR PDBsum; 4RWG; -. DR PDBsum; 5V6Y; -. DR PDBsum; 6D1U; -. DR PDBsum; 6E3Y; -. DR ProteinModelPortal; O60894; -. DR SMR; O60894; -. DR BioGrid; 115558; 23. 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; 1. DR STRING; 9606.ENSP00000254661; -. DR BindingDB; O60894; -. DR ChEMBL; CHEMBL2107838; -. DR DrugBank; DB01278; Pramlintide. DR GuidetoPHARMACOLOGY; 51; -. DR iPTMnet; O60894; -. DR PhosphoSitePlus; O60894; -. DR BioMuta; RAMP1; -. DR PaxDb; O60894; -. DR PeptideAtlas; O60894; -. DR PRIDE; O60894; -. DR ProteomicsDB; 49657; -. DR DNASU; 10267; -. DR Ensembl; ENST00000254661; ENSP00000254661; ENSG00000132329. DR GeneID; 10267; -. DR KEGG; hsa:10267; -. DR UCSC; uc002vxj.4; human. DR CTD; 10267; -. DR DisGeNET; 10267; -. DR EuPathDB; HostDB:ENSG00000132329.10; -. DR GeneCards; RAMP1; -. DR HGNC; HGNC:9843; RAMP1. DR HPA; HPA057814; -. DR MIM; 605153; gene. DR neXtProt; NX_O60894; -. DR OpenTargets; ENSG00000132329; -. DR PharmGKB; PA34202; -. DR eggNOG; ENOG410IZHQ; Eukaryota. DR eggNOG; ENOG4111NGJ; LUCA. DR GeneTree; ENSGT00940000159224; -. DR HOGENOM; HOG000253018; -. DR HOVERGEN; HBG061268; -. DR InParanoid; O60894; -. DR KO; K08447; -. DR OMA; WRSKRPE; -. DR OrthoDB; 1432933at2759; -. DR PhylomeDB; O60894; -. DR TreeFam; TF333286; -. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR Reactome; R-HSA-419812; Calcitonin-like ligand receptors. DR ChiTaRS; RAMP1; human. DR EvolutionaryTrace; O60894; -. DR GeneWiki; RAMP1; -. DR GenomeRNAi; 10267; -. DR PRO; PR:O60894; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000132329; Expressed in 216 organ(s), highest expression level in myometrium. DR ExpressionAtlas; O60894; baseline and differential. DR Genevisible; O60894; HS. DR GO; GO:0150056; C:amylin receptor complex 1; IDA:ARUK-UCL. DR GO; GO:0005623; C:cell; IDA:ARUK-UCL. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:1990406; C:CGRP receptor complex; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. 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:0008565; F:protein transporter activity; IDA:UniProtKB. 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; -; 1. DR InterPro; IPR006985; RAMP. DR InterPro; IPR038126; RAMP_sf. DR PANTHER; PTHR14076; PTHR14076; 1. DR Pfam; PF04901; RAMP; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Membrane; Receptor; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Transport. FT SIGNAL 1 26 {ECO:0000255}. FT CHAIN 27 148 Receptor activity-modifying protein 1. FT /FTId=PRO_0000030168. FT TOPO_DOM 27 117 Extracellular. {ECO:0000255}. FT TRANSMEM 118 138 Helical. {ECO:0000255}. FT TOPO_DOM 139 148 Cytoplasmic. {ECO:0000255}. FT DISULFID 27 82 FT DISULFID 40 72 FT DISULFID 57 104 FT HELIX 26 28 {ECO:0000244|PDB:6D1U}. FT HELIX 30 51 {ECO:0000244|PDB:6D1U}. FT HELIX 53 55 {ECO:0000244|PDB:6D1U}. FT HELIX 59 79 {ECO:0000244|PDB:6D1U}. FT HELIX 87 100 {ECO:0000244|PDB:6D1U}. FT STRAND 101 103 {ECO:0000244|PDB:2YX8}. FT STRAND 111 113 {ECO:0000244|PDB:3N7S}. FT HELIX 119 142 {ECO:0000244|PDB:6E3Y}. SQ SEQUENCE 148 AA; 16988 MW; 8530DD590BAEBE5C CRC64; MARALCRLPR RGLWLLLAHH LFMTTACQEA NYGALLRELC LTQFQVDMEA VGETLWCDWG RTIRSYRELA DCTWHMAEKL GCFWPNAEVD RFFLAVHGRY FRSCPISGRA VRDPPGSILY PFIVVPITVT LLVTALVVWQ SKRTEGIV //