RAMP1_HUMAN
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 03-AUG-2022, entry version 178.
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}.
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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; 7TYF; EM; 2.20 A; E=27-148.
DR PDB; 7TYW; EM; 3.00 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 PDBsum; 6UMG; -.
DR PDBsum; 6ZHO; -.
DR PDBsum; 6ZIS; -.
DR PDBsum; 7KNT; -.
DR PDBsum; 7KNU; -.
DR PDBsum; 7TYF; -.
DR PDBsum; 7TYW; -.
DR AlphaFoldDB; O60894; -.
DR SMR; O60894; -.
DR BioGRID; 115558; 45.
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; O60894; -.
DR PeptideAtlas; O60894; -.
DR PRIDE; O60894; -.
DR ProteomicsDB; 49657; -.
DR Antibodypedia; 34486; 234 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 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; 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 SignaLink; O60894; -.
DR BioGRID-ORCS; 10267; 11 hits in 1069 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 191 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: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: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: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 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 119..141
FT /evidence="ECO:0007829|PDB:7KNT"
SQ SEQUENCE 148 AA; 16988 MW; 8530DD590BAEBE5C CRC64;
MARALCRLPR RGLWLLLAHH LFMTTACQEA NYGALLRELC LTQFQVDMEA VGETLWCDWG
RTIRSYRELA DCTWHMAEKL GCFWPNAEVD RFFLAVHGRY FRSCPISGRA VRDPPGSILY
PFIVVPITVT LLVTALVVWQ SKRTEGIV
