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Advanced glycosylation end product-specific receptor (Receptor for advanced glycosylation end products)

 RAGE_RAT                Reviewed;         402 AA.
Q63495;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
20-JUN-2018, entry version 128.
RecName: Full=Advanced glycosylation end product-specific receptor;
AltName: Full=Receptor for advanced glycosylation end products;
Flags: Precursor;
Name=Ager; Synonyms=Rage;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Lung;
PubMed=9224812;
Renard C., Chappey O., Wautier M.P., Nagashima M., Lundh E.,
Morser J., Zhao L., Schmidt A.M., Scherrmann J.M., Wautier J.-L.;
"Recombinant advanced glycation end product receptor pharmacokinetics
in normal and diabetic rats.";
Mol. Pharmacol. 52:54-62(1997).
[2]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH S100B AND S100A1,
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=19910580; DOI=10.1161/CIRCRESAHA.109.195834;
Tsoporis J.N., Izhar S., Leong-Poi H., Desjardins J.F., Huttunen H.J.,
Parker T.G.;
"S100B interaction with the receptor for advanced glycation end
products (RAGE): a novel receptor-mediated mechanism for myocyte
apoptosis postinfarction.";
Circ. Res. 106:93-101(2010).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376 AND SER-389, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Mediates interactions of advanced glycosylation end
products (AGE). These are nonenzymatically glycosylated proteins
which accumulate in vascular tissue in aging and at an accelerated
rate in diabetes. Acts as a mediator of both acute and chronic
vascular inflammation in conditions such as atherosclerosis and in
particular as a complication of diabetes. AGE/RAGE signaling plays
an important role in regulating the production/expression of TNF-
alpha, oxidative stress, and endothelial dysfunction in type 2
diabetes. Interaction with S100A12 on endothelium, mononuclear
phagocytes, and lymphocytes triggers cellular activation, with
generation of key proinflammatory mediators. Receptor for amyloid
beta peptide. Contributes to the translocation of amyloid-beta
peptide (ABPP) across the cell membrane from the extracellular to
the intracellular space in cortical neurons. ABPP-initiated RAGE
signaling, especially stimulation of p38 mitogen-activated protein
kinase (MAPK), has the capacity to drive a transport system
delivering ABPP as a complex with RAGE to the intraneuronal space.
Can also bind oligonucleotides (By similarity). Interaction with
S100B after myocardial infarction may play a role in myocyte
apoptosis by activating ERK1/2 and p53/TP53 signaling.
{ECO:0000250, ECO:0000269|PubMed:19910580}.
-!- SUBUNIT: Interacts with S100A12, S100A14 and APP. Constitutive
homodimer; disulfide-linked (By similarity). Interacts with S100B
and S100A1. {ECO:0000250, ECO:0000269|PubMed:19910580}.
-!- INTERACTION:
P04631:S100b; NbExp=3; IntAct=EBI-6479195, EBI-2696631;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19910580};
Single-pass type I membrane protein {ECO:0000269|PubMed:19910580}.
-!- TISSUE SPECIFICITY: Endothelial cells and cardiomyocytes.
{ECO:0000269|PubMed:19910580}.
-!- INDUCTION: Up-regulated in periinfarct ventricular myocardium.
{ECO:0000269|PubMed:19910580}.
-----------------------------------------------------------------------
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EMBL; L33413; AAA42027.1; -; mRNA.
UniGene; Rn.9829; -.
ProteinModelPortal; Q63495; -.
SMR; Q63495; -.
IntAct; Q63495; 2.
STRING; 10116.ENSRNOP00000000508; -.
ChEMBL; CHEMBL2176847; -.
iPTMnet; Q63495; -.
PhosphoSitePlus; Q63495; -.
PaxDb; Q63495; -.
PRIDE; Q63495; -.
UCSC; RGD:69258; rat.
RGD; 69258; Ager.
eggNOG; ENOG410IVT2; Eukaryota.
eggNOG; ENOG4111C4I; LUCA.
HOGENOM; HOG000232122; -.
HOVERGEN; HBG004350; -.
InParanoid; Q63495; -.
PhylomeDB; Q63495; -.
PRO; PR:Q63495; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0050785; F:advanced glycation end-product receptor activity; IMP:RGD.
GO; GO:0070379; F:high mobility group box 1 binding; IPI:RGD.
GO; GO:0044548; F:S100 protein binding; IPI:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0055074; P:calcium ion homeostasis; IMP:RGD.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0009100; P:glycoprotein metabolic process; IEP:RGD.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0007259; P:JAK-STAT cascade; IMP:RGD.
GO; GO:0030324; P:lung development; IEP:RGD.
GO; GO:0007162; P:negative regulation of cell adhesion; IMP:RGD.
GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IMP:RGD.
GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:RGD.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:RGD.
GO; GO:0033689; P:negative regulation of osteoblast proliferation; IEP:RGD.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:RGD.
GO; GO:0031175; P:neuron projection development; IMP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0010508; P:positive regulation of autophagy; IMP:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IMP:RGD.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:RGD.
GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:RGD.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:0050729; P:positive regulation of inflammatory response; IMP:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:1901216; P:positive regulation of neuron death; IMP:RGD.
GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IMP:RGD.
GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IMP:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:RGD.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
GO; GO:2000676; P:positive regulation of type B pancreatic cell apoptotic process; IMP:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0009750; P:response to fructose; IEP:RGD.
GO; GO:0033595; P:response to genistein; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0051595; P:response to methylglyoxal; IEP:RGD.
GO; GO:0072714; P:response to selenite ion; IEP:RGD.
GO; GO:0033189; P:response to vitamin A; IEP:RGD.
GO; GO:0060290; P:transdifferentiation; IEP:RGD.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF08205; C2-set_2; 1.
Pfam; PF13895; Ig_2; 1.
SMART; SM00409; IG; 2.
SMART; SM00408; IGc2; 2.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Inflammatory response; Membrane;
Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 402 Advanced glycosylation end product-
specific receptor.
/FTId=PRO_0000014925.
TOPO_DOM 23 341 Extracellular. {ECO:0000255}.
TRANSMEM 342 362 Helical. {ECO:0000255}.
TOPO_DOM 363 402 Cytoplasmic. {ECO:0000255}.
DOMAIN 23 109 Ig-like V-type.
DOMAIN 123 219 Ig-like C2-type 1.
DOMAIN 233 315 Ig-like C2-type 2.
MOD_RES 376 376 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 80 80 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 38 98 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 143 206 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 257 257 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DISULFID 299 299 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
SEQUENCE 402 AA; 42664 MW; 594481BC3A51E94E CRC64;
MPTGTVARAW VLVLALWGAV AGGQNITARI GEPLMLSCKG APKKPTQKLE WKLNTGRTEA
WKVLSPQGDP WDSVARILPN GSLLLPAIGI VDEGTFRCRA TNRLGKEVKS NYRVRVYQIP
GKPEIVNPAS ELTANVPNKV GTCVSEGSYP AGTLSWHLDG KPLIPDGKGT VVKEETRRHP
ETGLFTLRSE LTVTPAQGGT TPTYSCSFSL GLPRRRPLNT APIQPRVREP LPPEGIQLLV
EPEGGTVAPG GTVTLTCAIS AQPPPQIHWI KDGTPLPLAP SPVLLLPEVG HEDEGIYSCV
ATHPSHGPQE SPPVNIRVTE TGDEGQAAGS VDGSGLGTLA LALGILGGLG IAALLIGAIL
WRKRQPRLEE RKAPESQEDE EERAELNQSE EAEMPENGAG GP


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