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Database: UniProt
Entry: O60894
LinkDB: O60894
Original site: O60894 
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   07-OCT-2020, entry version 170.
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=3; 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}.
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   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   SMR; O60894; -.
DR   BioGRID; 115558; 27.
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; 4.
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; O60894; -.
DR   PeptideAtlas; O60894; -.
DR   PRIDE; O60894; -.
DR   ProteomicsDB; 49657; -.
DR   Antibodypedia; 34486; 228 antibodies.
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; ENSG00000132329; Tissue enhanced (endometrium, pancreas).
DR   MIM; 605153; gene.
DR   neXtProt; NX_O60894; -.
DR   OpenTargets; ENSG00000132329; -.
DR   PharmGKB; PA34202; -.
DR   eggNOG; ENOG502S0TC; Eukaryota.
DR   GeneTree; ENSGT00940000159224; -.
DR   InParanoid; O60894; -.
DR   KO; K08447; -.
DR   OMA; HRHYFHD; -.
DR   OrthoDB; 1432933at2759; -.
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   Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR   BioGRID-ORCS; 10267; 6 hits in 872 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 myometrium and 230 other tissues.
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: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: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:0032092; P:positive regulation of protein binding; IEA:Ensembl.
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; 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:0000244|PDB:6D1U"
FT   HELIX           30..51
FT                   /evidence="ECO:0000244|PDB:6D1U"
FT   HELIX           53..55
FT                   /evidence="ECO:0000244|PDB:6D1U"
FT   HELIX           59..79
FT                   /evidence="ECO:0000244|PDB:6D1U"
FT   HELIX           87..100
FT                   /evidence="ECO:0000244|PDB:6D1U"
FT   STRAND          101..103
FT                   /evidence="ECO:0000244|PDB:2YX8"
FT   STRAND          111..113
FT                   /evidence="ECO:0000244|PDB:3N7S"
FT   HELIX           119..142
FT                   /evidence="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
//
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