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Receptor activity-modifying protein 2 (Calcitonin-receptor-like receptor activity-modifying protein 2) (CRLR activity-modifying protein 2)

 RAMP2_HUMAN             Reviewed;         175 AA.
O60895; A7L9S6; K7EMD3; Q8N1F2;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
10-JAN-2003, sequence version 2.
27-SEP-2017, entry version 152.
RecName: Full=Receptor activity-modifying protein 2;
AltName: Full=Calcitonin-receptor-like receptor activity-modifying protein 2;
Short=CRLR activity-modifying protein 2;
Flags: Precursor;
Name=RAMP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
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 [MRNA] (ISOFORM 2).
Rorabaugh B.R., Witt K.M., Smith D.D., Abel P.W., Scofield M.A.;
"Characterization of adrenomedullin receptors and identification of a
receptor activity modifying protein 2 (RAMP2) variant in SV40LT-SMC
cells.";
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Heart;
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
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 (2.0 ANGSTROMS) OF 48-139, AND DISULFIDE BONDS.
Structural genomics consortium (SGC);
"Structure of the extracellular domain of human RAMP2.";
Submitted (DEC-2010) to the PDB data bank.
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 52-139 IN COMPLEX WITH
CALCRL, FUNCTION, AND DISULFIDE BONDS.
PubMed=22102369; DOI=10.1002/pro.2003;
Kusano S., Kukimoto-Niino M., Hino N., Ohsawa N., Okuda K.,
Sakamoto K., Shirouzu M., Shindo T., Yokoyama S.;
"Structural basis for extracellular interactions between calcitonin
receptor-like receptor and receptor activity-modifying protein 2 for
adrenomedullin-specific binding.";
Protein Sci. 21:199-210(2012).
-!- FUNCTION: Transports the calcitonin gene-related peptide type 1
receptor (CALCRL) to the plasma membrane. Acts as a receptor for
adrenomedullin (AM) together with CALCRL.
{ECO:0000269|PubMed:22102369, ECO:0000269|PubMed:9620797}.
-!- SUBUNIT: Heterodimer of CALCRL and RAMP2. {ECO:0000250}.
-!- INTERACTION:
Q16602:CALCRL; NbExp=6; IntAct=EBI-9009040, EBI-962878;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O60895-1; Sequence=Displayed;
Name=2;
IsoId=O60895-2; Sequence=VSP_055838;
-!- TISSUE SPECIFICITY: Strongly expressed in lung, breast, immune
system and fetal tissues. {ECO:0000269|PubMed:9620797}.
-!- SIMILARITY: Belongs to the RAMP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ001015; CAA04473.1; -; mRNA.
EMBL; EF687002; ABS28868.1; -; mRNA.
EMBL; AY265458; AAP23299.1; -; mRNA.
EMBL; AC100793; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC027975; AAH27975.1; -; mRNA.
CCDS; CCDS11437.1; -. [O60895-1]
RefSeq; NP_005845.2; NM_005854.2. [O60895-1]
UniGene; Hs.514193; -.
PDB; 2XVT; X-ray; 2.05 A; A/B/C/D/E/F=48-139.
PDB; 3AQE; X-ray; 2.00 A; A/B/C/D/E/F=56-139.
PDB; 3AQF; X-ray; 2.60 A; A=56-139.
PDB; 4RWF; X-ray; 1.76 A; A=55-138.
PDBsum; 2XVT; -.
PDBsum; 3AQE; -.
PDBsum; 3AQF; -.
PDBsum; 4RWF; -.
ProteinModelPortal; O60895; -.
SMR; O60895; -.
BioGrid; 115557; 1.
CORUM; O60895; -.
IntAct; O60895; 2.
STRING; 9606.ENSP00000253796; -.
BindingDB; O60895; -.
ChEMBL; CHEMBL2364173; -.
DrugBank; DB01278; Pramlintide.
GuidetoPHARMACOLOGY; 52; -.
PhosphoSitePlus; O60895; -.
BioMuta; RAMP2; -.
PaxDb; O60895; -.
PeptideAtlas; O60895; -.
PRIDE; O60895; -.
DNASU; 10266; -.
Ensembl; ENST00000253796; ENSP00000253796; ENSG00000131477. [O60895-1]
Ensembl; ENST00000587142; ENSP00000466455; ENSG00000131477. [O60895-2]
GeneID; 10266; -.
KEGG; hsa:10266; -.
UCSC; uc002ibg.5; human. [O60895-1]
CTD; 10266; -.
DisGeNET; 10266; -.
EuPathDB; HostDB:ENSG00000131477.10; -.
GeneCards; RAMP2; -.
HGNC; HGNC:9844; RAMP2.
HPA; HPA052020; -.
MIM; 605154; gene.
neXtProt; NX_O60895; -.
OpenTargets; ENSG00000131477; -.
PharmGKB; PA34203; -.
eggNOG; ENOG410IYPR; Eukaryota.
eggNOG; ENOG4112A9G; LUCA.
GeneTree; ENSGT00390000016200; -.
HOGENOM; HOG000230963; -.
HOVERGEN; HBG067366; -.
InParanoid; O60895; -.
KO; K08448; -.
OMA; DLGFPNP; -.
OrthoDB; EOG091G0RMZ; -.
PhylomeDB; O60895; -.
TreeFam; TF333286; -.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-419812; Calcitonin-like ligand receptors.
ChiTaRS; RAMP2; human.
GeneWiki; RAMP2; -.
GenomeRNAi; 10266; -.
PRO; PR:O60895; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000131477; -.
CleanEx; HS_RAMP2; -.
ExpressionAtlas; O60895; baseline and differential.
Genevisible; O60895; HS.
GO; GO:1903440; C:amylin receptor complex; IDA:ARUK-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; TAS:ProtInc.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005764; C:lysosome; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
GO; GO:0015026; F:coreceptor activity; ISS:UniProtKB.
GO; GO:0008565; F:protein transporter activity; IDA:UniProtKB.
GO; GO:0034333; P:adherens junction assembly; IDA:UniProtKB.
GO; GO:0097647; P:amylin receptor signaling pathway; IGI:ARUK-UCL.
GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
GO; GO:0070831; P:basement membrane assembly; ISS:UniProtKB.
GO; GO:0070830; P:bicellular tight junction assembly; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB.
GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; ISS:UniProtKB.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:UniProtKB.
GO; GO:0043116; P:negative regulation of vascular permeability; IDA:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IGI:UniProtKB.
GO; GO:0030816; P:positive regulation of cAMP metabolic process; IGI:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:2001214; P:positive regulation of vasculogenesis; IEA:Ensembl.
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:0008217; P:regulation of blood pressure; ISS:UniProtKB.
GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IEA:InterPro.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0097084; P:vascular smooth muscle cell development; ISS:UniProtKB.
GO; GO:0001570; P:vasculogenesis; IMP:UniProtKB.
InterPro; IPR006985; RAMP.
PANTHER; PTHR14076; PTHR14076; 1.
Pfam; PF04901; RAMP; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Membrane; Receptor; Reference proteome; Signal;
Transmembrane; Transmembrane helix; Transport.
SIGNAL 1 42 {ECO:0000255}.
CHAIN 43 175 Receptor activity-modifying protein 2.
/FTId=PRO_0000030172.
TOPO_DOM 43 145 Extracellular. {ECO:0000255}.
TRANSMEM 146 166 Helical. {ECO:0000255}.
TOPO_DOM 167 175 Cytoplasmic. {ECO:0000255}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 68 99
DISULFID 84 131
VAR_SEQ 54 54 E -> EASVPT (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_055838.
CONFLICT 13 13 R -> C (in Ref. 2; ABS28868).
{ECO:0000305}.
CONFLICT 25 25 L -> V (in Ref. 1; CAA04473).
{ECO:0000305}.
HELIX 61 76 {ECO:0000244|PDB:4RWF}.
HELIX 77 82 {ECO:0000244|PDB:4RWF}.
HELIX 86 106 {ECO:0000244|PDB:4RWF}.
HELIX 114 126 {ECO:0000244|PDB:4RWF}.
TURN 127 130 {ECO:0000244|PDB:3AQE}.
SEQUENCE 175 AA; 19608 MW; AF69A9A461EFFCA3 CRC64;
MASLRVERAG GPRLPRTRVG RPAALRLLLL LGAVLNPHEA LAQPLPTTGT PGSEGGTVKN
YETAVQFCWN HYKDQMDPIE KDWCDWAMIS RPYSTLRDCL EHFAELFDLG FPNPLAERII
FETHQIHFAN CSLVQPTFSD PPEDVLLAMI IAPICLIPFL ITLVVWRSKD SEAQA


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