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Receptor activity-modifying protein 1 (Calcitonin-receptor-like receptor activity-modifying protein 1) (CRLR activity-modifying protein 1)

 RAMP1_HUMAN             Reviewed;         148 AA.
O60894; Q6FGS5;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
28-MAR-2018, entry version 150.
RecName: Full=Receptor activity-modifying protein 1;
AltName: Full=Calcitonin-receptor-like receptor activity-modifying protein 1;
Short=CRLR activity-modifying protein 1;
Flags: Precursor;
Name=RAMP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
TOPOLOGY.
TISSUE=Neuroblastoma;
PubMed=9620797; DOI=10.1038/30666;
McLatchie L.M., Fraser N.J., Main M.J., Wise A., Brown J.,
Thompson N., Solari R., Lee M.G., Foord S.M.;
"RAMPs regulate the transport and ligand specificity of the
calcitonin-receptor-like receptor.";
Nature 393:333-339(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
Kopatz S.A., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 22-112, SUBUNIT, AND
DISULFIDE BONDS.
PubMed=18725456; DOI=10.1110/ps.036012.108;
Kusano S., Kukimoto-Niino M., Akasaka R., Toyama M., Terada T.,
Shirouzu M., Shindo T., Yokoyama S.;
"Crystal structure of the human receptor activity-modifying protein 1
extracellular domain.";
Protein Sci. 17:1907-1914(2008).
[7]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 26-117 IN COMPLEX WITH CALRL
AND ANTAGONIST, SUBUNIT, AND DISULFIDE BONDS.
PubMed=20826335; DOI=10.1016/j.str.2010.05.014;
ter Haar E., Koth C.M., Abdul-Manan N., Swenson L., Coll J.T.,
Lippke J.A., Lepre C.A., Garcia-Guzman M., Moore J.M.;
"Crystal structure of the ectodomain complex of the CGRP receptor, a
class-B GPCR, reveals the site of drug antagonism.";
Structure 18:1083-1093(2010).
-!- FUNCTION: Transports the calcitonin gene-related peptide type 1
receptor (CALCRL) to the plasma membrane. Acts as a receptor for
calcitonin-gene-related peptide (CGRP) together with CALCRL.
{ECO:0000269|PubMed:9620797}.
-!- SUBUNIT: Heterodimer of CALCRL and RAMP1.
{ECO:0000269|PubMed:18725456, ECO:0000269|PubMed:20826335}.
-!- INTERACTION:
Q16602:CALCRL; NbExp=3; IntAct=EBI-962893, EBI-962878;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Expressed in many tissues including the
uterus, bladder, brain, pancreas and gastro-intestinal tract.
{ECO:0000269|PubMed:9620797}.
-!- SIMILARITY: Belongs to the RAMP family. {ECO:0000305}.
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EMBL; AJ001014; CAA04472.1; -; mRNA.
EMBL; AY265457; AAP23298.1; -; mRNA.
EMBL; CR542032; CAG46829.1; -; mRNA.
EMBL; CR542044; CAG46841.1; -; mRNA.
EMBL; CH471063; EAW71127.1; -; Genomic_DNA.
EMBL; BC000548; AAH00548.1; -; mRNA.
CCDS; CCDS2522.1; -.
RefSeq; NP_005846.1; NM_005855.3.
UniGene; Hs.471783; -.
PDB; 2YX8; X-ray; 2.40 A; A=27-112.
PDB; 3N7P; X-ray; 2.80 A; D/E/F/R=26-117.
PDB; 3N7R; X-ray; 2.90 A; C/D=26-117.
PDB; 3N7S; X-ray; 2.10 A; C/D=26-117.
PDB; 4RWG; X-ray; 2.44 A; A/B/C=24-108.
PDB; 5V6Y; X-ray; 2.80 A; A/B/C/D=24-111.
PDBsum; 2YX8; -.
PDBsum; 3N7P; -.
PDBsum; 3N7R; -.
PDBsum; 3N7S; -.
PDBsum; 4RWG; -.
PDBsum; 5V6Y; -.
ProteinModelPortal; O60894; -.
SMR; O60894; -.
BioGrid; 115558; 22.
CORUM; O60894; -.
DIP; DIP-37675N; -.
IntAct; O60894; 1.
STRING; 9606.ENSP00000254661; -.
BindingDB; O60894; -.
ChEMBL; CHEMBL2107838; -.
DrugBank; DB01278; Pramlintide.
GuidetoPHARMACOLOGY; 51; -.
iPTMnet; O60894; -.
PhosphoSitePlus; O60894; -.
BioMuta; RAMP1; -.
PaxDb; O60894; -.
PeptideAtlas; O60894; -.
PRIDE; O60894; -.
DNASU; 10267; -.
Ensembl; ENST00000254661; ENSP00000254661; ENSG00000132329.
GeneID; 10267; -.
KEGG; hsa:10267; -.
UCSC; uc002vxj.4; human.
CTD; 10267; -.
DisGeNET; 10267; -.
EuPathDB; HostDB:ENSG00000132329.10; -.
GeneCards; RAMP1; -.
HGNC; HGNC:9843; RAMP1.
HPA; HPA057814; -.
MIM; 605153; gene.
neXtProt; NX_O60894; -.
OpenTargets; ENSG00000132329; -.
PharmGKB; PA34202; -.
eggNOG; ENOG410IZHQ; Eukaryota.
eggNOG; ENOG4111NGJ; LUCA.
GeneTree; ENSGT00390000016200; -.
HOGENOM; HOG000253018; -.
HOVERGEN; HBG061268; -.
InParanoid; O60894; -.
KO; K08447; -.
OMA; WRSKRPE; -.
OrthoDB; EOG091G0KY6; -.
PhylomeDB; O60894; -.
TreeFam; TF333286; -.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-419812; Calcitonin-like ligand receptors.
ChiTaRS; RAMP1; human.
EvolutionaryTrace; O60894; -.
GeneWiki; RAMP1; -.
GenomeRNAi; 10267; -.
PRO; PR:O60894; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000132329; -.
CleanEx; HS_RAMP1; -.
ExpressionAtlas; O60894; baseline and differential.
Genevisible; O60894; HS.
GO; GO:1903440; C:amylin receptor complex; IDA:ARUK-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:1990406; C:CGRP receptor complex; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
GO; GO:1990407; F:calcitonin gene-related peptide binding; IPI:UniProtKB.
GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; IPI:UniProtKB.
GO; GO:0015026; F:coreceptor activity; IEA:Ensembl.
GO; GO:0008565; F:protein transporter activity; IDA:UniProtKB.
GO; GO:0004872; F:receptor activity; IDA:UniProtKB.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IPI:UniProtKB.
GO; GO:0097647; P:amylin receptor signaling pathway; IGI:ARUK-UCL.
GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
GO; GO:1990408; P:calcitonin gene-related peptide receptor signaling pathway; IPI:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0030816; P:positive regulation of cAMP metabolic process; IGI:ARUK-UCL.
GO; GO:0060050; P:positive regulation of protein glycosylation; IDA:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IDA:UniProtKB.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IEA:InterPro.
Gene3D; 1.10.150.510; -; 1.
InterPro; IPR006985; RAMP.
InterPro; IPR038126; RAMP_sf.
PANTHER; PTHR14076; PTHR14076; 1.
Pfam; PF04901; RAMP; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Membrane; Receptor;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Transport.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 148 Receptor activity-modifying protein 1.
/FTId=PRO_0000030168.
TOPO_DOM 27 117 Extracellular. {ECO:0000255}.
TRANSMEM 118 138 Helical. {ECO:0000255}.
TOPO_DOM 139 148 Cytoplasmic. {ECO:0000255}.
DISULFID 27 82
DISULFID 40 72
DISULFID 57 104
HELIX 26 28 {ECO:0000244|PDB:4RWG}.
HELIX 29 39 {ECO:0000244|PDB:3N7S}.
HELIX 41 51 {ECO:0000244|PDB:3N7S}.
HELIX 53 55 {ECO:0000244|PDB:3N7S}.
HELIX 59 80 {ECO:0000244|PDB:3N7S}.
HELIX 87 100 {ECO:0000244|PDB:3N7S}.
STRAND 101 103 {ECO:0000244|PDB:2YX8}.
STRAND 111 113 {ECO:0000244|PDB:3N7S}.
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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