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

 RAGE_MOUSE              Reviewed;         402 AA.
Q62151; C5H3H4; C5H3H5; C5H3H7; C5H3I0; C5H7W3; C5H7W4; C5H7W5;
C5H7W6; C5H7W7; C5H7W8; C5H7W9; O35444; Q2PGG1; V5R4Y0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
17-FEB-2016, sequence version 2.
07-NOV-2018, entry version 146.
RecName: Full=Advanced glycosylation end product-specific receptor;
AltName: Full=Receptor for advanced glycosylation end products;
Flags: Precursor;
Name=Ager; Synonyms=Rage;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ; 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] {ECO:0000312|EMBL:BAE72665.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2),
SUBCELLULAR LOCATION (ISOFORM 2), AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J {ECO:0000303|PubMed:16503878};
TISSUE=Brain {ECO:0000303|PubMed:16503878};
PubMed=16503878; DOI=10.1042/BJ20051573;
Harashima A., Yamamoto Y., Cheng C., Tsuneyama K., Myint K.M.,
Takeuchi A., Yoshimura K., Li H., Watanabe T., Takasawa S.,
Okamoto H., Yonekura H., Yamamoto H.;
"Identification of mouse orthologue of endogenous secretory receptor
for advanced glycation end-products: structure, function and
expression.";
Biochem. J. 396:109-115(2006).
[3] {ECO:0000312|EMBL:ACD35949.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 11; 12
AND 13), SPLICE ISOFORMS THAT ARE POTENTIAL NMD TARGETS, AND TISSUE
SPECIFICITY.
STRAIN=BALB/cJ {ECO:0000312|EMBL:ACD35949.1};
PubMed=19164451; DOI=10.1096/fj.08-117739;
Kalea A.Z., Reiniger N., Yang H., Arriero M., Schmidt A.M.,
Hudson B.I.;
"Alternative splicing of the murine receptor for advanced glycation
end-products (RAGE) gene.";
FASEB J. 23:1766-1774(2009).
[4] {ECO:0000312|EMBL:AHB30242.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), FUNCTION (ISOFORM 10),
SUBCELLULAR LOCATION (ISOFORM 10), AND TISSUE SPECIFICITY.
TISSUE=Lung {ECO:0000312|EMBL:AHB30242.1};
PubMed=24260107; DOI=10.1371/journal.pone.0078267;
Jules J., Maiguel D., Hudson B.I.;
"Alternative splicing of the RAGE cytoplasmic domain regulates cell
signaling and function.";
PLoS ONE 8:E78267-E78267(2013).
[5] {ECO:0000312|EMBL:AAB82007.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129;
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[6] {ECO:0000312|EMBL:CT009767, ECO:0000312|Ensembl:ENSMUSP00000015596, ECO:0000312|Proteomes:UP000000589}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000015596,
ECO:0000312|Proteomes:UP000000589};
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[7] {ECO:0000312|EMBL:EDL26799.1, ECO:0000312|EMBL:EDL26800.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8] {ECO:0000312|EMBL:AAH61182.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[9]
FUNCTION, AND INTERACTION WITH S100A12.
TISSUE=Lung;
PubMed=10399917; DOI=10.1016/S0092-8674(00)80801-6;
Hofmann M.A., Drury S., Fu C., Qu W., Taguchi A., Lu Y., Avila C.,
Kambham N., Bierhaus A., Nawroth P., Neurath M.F., Slattery T.,
Beach D., McClary J., Nagashima M., Morser J., Stern D., Schmidt A.M.;
"RAGE mediates a novel proinflammatory axis: a central cell surface
receptor for S100/calgranulin polypeptides.";
Cell 97:889-901(1999).
[10]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=18539754; DOI=10.1152/ajpheart.00464.2008;
Gao X., Zhang H., Schmidt A.M., Zhang C.;
"AGE/RAGE produces endothelial dysfunction in coronary arterioles in
type 2 diabetic mice.";
Am. J. Physiol. 295:H491-H498(2008).
[11]
FUNCTION, AND INTERACTION WITH APP.
PubMed=19901339; DOI=10.1073/pnas.0905686106;
Takuma K., Fang F., Zhang W., Yan S., Fukuzaki E., Du H., Sosunov A.,
McKhann G., Funatsu Y., Nakamichi N., Nagai T., Mizoguchi H., Ibi D.,
Hori O., Ogawa S., Stern D.M., Yamada K., Yan S.S.;
"RAGE-mediated signaling contributes to intraneuronal transport of
amyloid-{beta} and neuronal dysfunction.";
Proc. Natl. Acad. Sci. U.S.A. 106:20021-20026(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
FUNCTION.
PubMed=19906677; DOI=10.1096/fj.09-139634;
Fang F., Lue L.-F., Yan S., Xu H., Luddy J.S., Chen D., Walker D.G.,
Stern D.M., Yan S., Schmidt A.M., Chen J.X., Yan S.S.;
"RAGE-dependent signaling in microglia contributes to
neuroinflammation, Abeta accumulation, and impaired learning/memory in
a mouse model of Alzheimer's disease.";
FASEB J. 24:1043-1055(2010).
-!- 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. Interaction with
S100B after myocardial infarction may play a role in myocyte
apoptosis by activating ERK1/2 and p53/TP53 signaling. Can also
bind oligonucleotides. 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.
RAGE-dependent signaling in microglia contributes to
neuroinflammation, amyloid accumulation, and impaired
learning/memory in a mouse model of Alzheimer disease.
{ECO:0000269|PubMed:10399917, ECO:0000269|PubMed:18539754,
ECO:0000269|PubMed:19901339, ECO:0000269|PubMed:19906677}.
-!- FUNCTION: Isoform 2: Is able to advanced glycosylation end product
(AGE)-induce nuclear factor NF-kappa-B activation.
{ECO:0000269|PubMed:16503878}.
-!- FUNCTION: Isoform 10: Down-regulates receptor for advanced
glycosylation end products (RAGE)-ligand induced signaling through
various MAPK pathways including ERK1/2, p38 and SAPK/JNK.
Significantly affects tumor cell properties through decreasing
cell migration, invasion, adhesion and proliferation, and
increasing cellular apoptosis. Exhibits drastic inhibition on
tumorigenesis in vitro. {ECO:0000269|PubMed:24260107}.
-!- SUBUNIT: Interacts with S100B, S100A1 and S100A14. Constitutive
homodimer; disulfide-linked (By similarity). Interacts with
S100A12 and APP. {ECO:0000250, ECO:0000269|PubMed:10399917,
ECO:0000269|PubMed:19901339}.
-!- INTERACTION:
Q02956:Prkcz; NbExp=7; IntAct=EBI-6665091, EBI-642057;
-!- SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted
{ECO:0000269|PubMed:16503878}.
-!- SUBCELLULAR LOCATION: Isoform 10: Cell membrane
{ECO:0000269|PubMed:24260107}; Single-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=13;
Name=1; Synonyms=mRAGE {ECO:0000303|PubMed:19164451};
IsoId=Q62151-1; Sequence=Displayed;
Name=2; Synonyms=mRAGE_v1 {ECO:0000303|PubMed:19164451}, mRAGE_v3
{ECO:0000303|PubMed:19164451}, endogenous secretory receptor for
AGE (esRAGE) {ECO:0000303|PubMed:16503878};
IsoId=Q62151-2; Sequence=VSP_058091, VSP_058092;
Name=3; Synonyms=mRAGE_v4 {ECO:0000303|PubMed:19164451};
IsoId=Q62151-3; Sequence=VSP_058090;
Name=4; Synonyms=mRAGE_v15 {ECO:0000303|PubMed:19164451};
IsoId=Q62151-4; Sequence=VSP_058080, VSP_058090;
Name=5; Synonyms=mRAGE_v14 {ECO:0000303|PubMed:19164451};
IsoId=Q62151-5; Sequence=VSP_058089;
Name=6; Synonyms=mRAGE_v10 {ECO:0000303|PubMed:19164451};
IsoId=Q62151-6; Sequence=VSP_058087, VSP_058088;
Name=7; Synonyms=mRAGE_v7 {ECO:0000303|PubMed:19164451};
IsoId=Q62151-7; Sequence=VSP_058083, VSP_058086;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.
{ECO:0000269|PubMed:19164451};
Name=8; Synonyms=mRAGE_v11 {ECO:0000303|PubMed:19164451};
IsoId=Q62151-8; Sequence=VSP_058084, VSP_058085;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.
{ECO:0000269|PubMed:19164451};
Name=9; Synonyms=mRAGE_v9 {ECO:0000303|PubMed:19164451};
IsoId=Q62151-9; Sequence=VSP_058076, VSP_058082;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.
{ECO:0000269|PubMed:19164451};
Name=10; Synonyms=RAGE deletion of intracellular domain
{ECO:0000303|PubMed:24260107}, RAGEdeltaICD
{ECO:0000303|PubMed:24260107}, mRAGE_v20
{ECO:0000303|PubMed:24260107};
IsoId=Q62151-10; Sequence=VSP_058093, VSP_058094;
Name=11; Synonyms=mRAGE_v2 {ECO:0000303|PubMed:19164451}, mRAGE_v5
{ECO:0000303|PubMed:19164451}, mRAGE_v6
{ECO:0000303|PubMed:19164451}, mRAGE_v8
{ECO:0000303|PubMed:19164451}, mRAGE_v16
{ECO:0000303|PubMed:19164451}, mRAGE_v17
{ECO:0000303|PubMed:19164451};
IsoId=Q62151-11; Sequence=VSP_058075, VSP_058081;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.
{ECO:0000269|PubMed:19164451};
Name=12; Synonyms=mRAGE_v13 {ECO:0000303|PubMed:19164451};
IsoId=Q62151-12; Sequence=VSP_058077, VSP_058079;
Name=13; Synonyms=mRAGE_v12 {ECO:0000303|PubMed:19164451};
IsoId=Q62151-13; Sequence=VSP_058078;
-!- TISSUE SPECIFICITY: Isoform 1: Expressed at higher levels in the
coronary arterioles in type 2 diabetic mice (at protein level).
Endothelial cells (PubMed:18539754). Expressed in lung, kidney,
brain and heart. Most prevalent isoform with the highest level in
heart (PubMed:19164451). Isoform 2: Expressed in brain, lung,
kidney and small intestine with the highest level in lung.
Expressed in brain, lung, kidney and small intestine with the
highest level in small intestine (at protein level). Detected in
neurons of the cerebrum, bronchial epithelium, endothelial cells,
tubular cells of kidney and epithelial cells of small intestine
(at protein level). Expression is increased in the kidney of
diabetic wild-type mice (at protein level), but not in the other
tissues (PubMed:16503878). Expressed only in kidney. Expression is
increased in the kidney of diabetic mice (PubMed:19164451).
Isoform 3: Expressed in lung, kidney and heart. The second most
prevalent isoform with the highest level in lung. Not expressed in
brain (PubMed:19164451). Isoform 4: Expressed at very low level in
lung only (PubMed:19164451). Isoform 5: Expressed at very low
level in lung only (PubMed:19164451). Isoform 6: Expressed at very
low level in lung only (PubMed:19164451). Isoform 7: Expressed at
very low level in heart only (PubMed:19164451). Isoform 8:
Expressed at very low level in lung only (PubMed:19164451).
Isoform 9: Expressed at very low level in heart only
(PubMed:19164451). Isoform 10: Expressed in lung, brain, heart and
kidney with a very high level in kidney (PubMed:24260107). Isoform
11: Expressed in brain, kidney and heart. Not expressed in lung
(PubMed:19164451). Isoform 12: Expressed at very low level in lung
and kidney (PubMed:19164451). Isoform 13: Expressed at very low
level in lung only (PubMed:19164451).
{ECO:0000269|PubMed:16503878, ECO:0000269|PubMed:18539754,
ECO:0000269|PubMed:19164451, ECO:0000269|PubMed:24260107}.
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EMBL; L33412; AAA40040.1; -; mRNA.
EMBL; AB207883; BAE72665.1; -; mRNA.
EMBL; EU520325; ACD35949.1; -; mRNA.
EMBL; EU570240; ACE63492.1; -; mRNA.
EMBL; EU570241; ACE63493.1; -; mRNA.
EMBL; EU570242; ACE63494.1; -; mRNA.
EMBL; EU570243; ACE63495.1; -; mRNA.
EMBL; EU570244; ACE63496.1; -; mRNA.
EMBL; EU570245; ACE63497.1; -; mRNA.
EMBL; EU570246; ACE63498.1; -; mRNA.
EMBL; EU570247; ACE63499.1; -; mRNA.
EMBL; EU906857; ACK28143.1; -; mRNA.
EMBL; EU906858; ACK28144.1; -; mRNA.
EMBL; EU906859; ACK28145.1; -; mRNA.
EMBL; EU906860; ACK28146.1; -; mRNA.
EMBL; EU906861; ACK28147.1; -; mRNA.
EMBL; EU906862; ACK28148.1; -; mRNA.
EMBL; EU906863; ACK28149.1; -; mRNA.
EMBL; EU906864; ACK28150.1; -; mRNA.
EMBL; EU906865; ACK28151.1; -; mRNA.
EMBL; KC692918; AHB30242.1; -; mRNA.
EMBL; AF030001; AAB82007.1; -; Genomic_DNA.
EMBL; CT009767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466666; EDL26799.1; -; Genomic_DNA.
EMBL; CH466666; EDL26800.1; -; Genomic_DNA.
EMBL; BC061182; AAH61182.1; -; mRNA.
CCDS; CCDS28649.1; -. [Q62151-1]
CCDS; CCDS70795.1; -. [Q62151-3]
CCDS; CCDS70796.1; -. [Q62151-4]
PIR; T09062; T09062.
RefSeq; NP_001258351.1; NM_001271422.1. [Q62151-3]
RefSeq; NP_001258352.1; NM_001271423.1. [Q62151-4]
RefSeq; NP_031451.2; NM_007425.3. [Q62151-1]
UniGene; Mm.3383; -.
PDB; 4IM8; X-ray; 3.50 A; A=23-230.
PDBsum; 4IM8; -.
ProteinModelPortal; Q62151; -.
SMR; Q62151; -.
IntAct; Q62151; 8.
MINT; Q62151; -.
STRING; 10090.ENSMUSP00000015596; -.
ChEMBL; CHEMBL2189161; -.
iPTMnet; Q62151; -.
PhosphoSitePlus; Q62151; -.
MaxQB; Q62151; -.
PaxDb; Q62151; -.
PRIDE; Q62151; -.
Ensembl; ENSMUST00000015596; ENSMUSP00000015596; ENSMUSG00000015452. [Q62151-1]
Ensembl; ENSMUST00000173992; ENSMUSP00000134579; ENSMUSG00000015452. [Q62151-4]
Ensembl; ENSMUST00000174069; ENSMUSP00000133391; ENSMUSG00000015452. [Q62151-2]
Ensembl; ENSMUST00000174496; ENSMUSP00000134401; ENSMUSG00000015452. [Q62151-3]
GeneID; 11596; -.
KEGG; mmu:11596; -.
UCSC; uc008ccw.3; mouse.
UCSC; uc008ccx.2; mouse.
UCSC; uc012aqe.2; mouse.
UCSC; uc012aqf.2; mouse.
UCSC; uc012aqg.2; mouse.
UCSC; uc033hcv.1; mouse.
CTD; 177; -.
MGI; MGI:893592; Ager.
eggNOG; ENOG410IVT2; Eukaryota.
eggNOG; ENOG4111C4I; LUCA.
GeneTree; ENSGT00890000139566; -.
HOGENOM; HOG000232122; -.
HOVERGEN; HBG004350; -.
InParanoid; Q62151; -.
KO; K19722; -.
OMA; LHTAPIQ; -.
OrthoDB; EOG091G0BCY; -.
TreeFam; TF337155; -.
Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-MMU-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-MMU-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
PRO; PR:Q62151; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000015452; Expressed in 175 organ(s), highest expression level in lung.
CleanEx; MM_RAGE; -.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0005576; C:extracellular region; IDA:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:1904599; F:advanced glycation end-product binding; IDA:MGI.
GO; GO:0050785; F:advanced glycation end-product receptor activity; ISO:MGI.
GO; GO:0070379; F:high mobility group box 1 binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
GO; GO:0014002; P:astrocyte development; IMP:MGI.
GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
GO; GO:1904646; P:cellular response to amyloid-beta; IMP:ARUK-UCL.
GO; GO:0010255; P:glucose mediated signaling pathway; ISO:MGI.
GO; GO:0050930; P:induction of positive chemotaxis; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IGI:MGI.
GO; GO:0007259; P:JAK-STAT cascade; ISO:MGI.
GO; GO:0007611; P:learning or memory; ISO:MGI.
GO; GO:0090647; P:modulation of age-related behavioral decline; ISO:MGI.
GO; GO:1904604; P:negative regulation of advanced glycation end-product receptor activity; IDA:MGI.
GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
GO; GO:1904597; P:negative regulation of connective tissue replacement involved in inflammatory response wound healing; IMP:MGI.
GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:MGI.
GO; GO:1900453; P:negative regulation of long-term synaptic depression; ISO:MGI.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
GO; GO:0023057; P:negative regulation of signaling; ISO:MGI.
GO; GO:0031175; P:neuron projection development; ISO:MGI.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:MGI.
GO; GO:1904605; P:positive regulation of advanced glycation end-product receptor activity; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0061890; P:positive regulation of astrocyte activation; ISO:MGI.
GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:2001200; P:positive regulation of dendritic cell differentiation; ISO:MGI.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:MGI.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
GO; GO:0032735; P:positive regulation of interleukin-12 production; ISO:MGI.
GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:MGI.
GO; GO:1903980; P:positive regulation of microglial cell activation; ISO:MGI.
GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IGI:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI.
GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISO:MGI.
GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
GO; GO:0023056; P:positive regulation of signaling; ISO:MGI.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:2000676; P:positive regulation of type B pancreatic cell apoptotic process; ISO:MGI.
GO; GO:0072657; P:protein localization to membrane; IMP:MGI.
GO; GO:2000514; P:regulation of CD4-positive, alpha-beta T cell activation; ISO:MGI.
GO; GO:0051101; P:regulation of DNA binding; IMP:MGI.
GO; GO:0050727; P:regulation of inflammatory response; IDA:UniProtKB.
GO; GO:1900271; P:regulation of long-term synaptic potentiation; IMP:ARUK-UCL.
GO; GO:1900744; P:regulation of p38MAPK cascade; IGI:ARUK-UCL.
GO; GO:0150003; P:regulation of spontaneous synaptic transmission; ISO:MGI.
GO; GO:0001914; P:regulation of T cell mediated cytotoxicity; ISO:MGI.
GO; GO:1904645; P:response to amyloid-beta; IGI:ARUK-UCL.
GO; GO:0001666; P:response to hypoxia; IMP:MGI.
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.
InterPro; IPR013151; Immunoglobulin.
Pfam; PF08205; C2-set_2; 1.
Pfam; PF00047; ig; 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;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunoglobulin domain;
Inflammatory response; Membrane; Phosphoprotein; Reference proteome;
Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 402 Advanced glycosylation end product-
specific receptor.
/FTId=PRO_0000014924.
TOPO_DOM 23 340 Extracellular. {ECO:0000255}.
TRANSMEM 341 361 Helical. {ECO:0000255}.
TOPO_DOM 362 402 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:21183079}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000250|UniProtKB:Q63495}.
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}.
VAR_SEQ 19 77 AVAGGQNITARIGEPLVLSCKGAPKKPPQQLEWKLNTGRTE
AWKVLSPQGGPWDSVARI -> ETLPAPTLPLSSPAPTPPP
VPPCPLEIPLNLGTTFQRPSPTLSYTRTPQPHLSPSTLPQ
(in isoform 11).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058075.
VAR_SEQ 27 85 TARIGEPLVLSCKGAPKKPPQQLEWKLNTGRTEAWKVLSPQ
GGPWDSVARILPNGSLLL -> PALCCSSLRWGTRMRAPIA
AWPPTLATDLRKALLSASGSQKPAMRGQLKALWVSLGWVR
(in isoform 9).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058076.
VAR_SEQ 30 40 IGEPLVLSCKG -> KARRMRRNVQS (in isoform
12). {ECO:0000269|PubMed:19164451}.
/FTId=VSP_058077.
VAR_SEQ 31 402 Missing (in isoform 13).
/FTId=VSP_058078.
VAR_SEQ 41 402 Missing (in isoform 12).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058079.
VAR_SEQ 54 62 Missing (in isoform 4).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058080.
VAR_SEQ 78 402 Missing (in isoform 11).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058081.
VAR_SEQ 86 402 Missing (in isoform 9).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058082.
VAR_SEQ 118 138 QIPGKPEIVDPASELTASVPN -> RKGPRLSHFAFIKKPS
CTPNP (in isoform 7).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058083.
VAR_SEQ 119 137 IPGKPEIVDPASELTASVP -> KPAMRGQLKALWVSLGWV
R (in isoform 8).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058084.
VAR_SEQ 138 402 Missing (in isoform 8).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058085.
VAR_SEQ 139 402 Missing (in isoform 7).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058086.
VAR_SEQ 153 153 T -> G (in isoform 6).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058087.
VAR_SEQ 154 402 Missing (in isoform 6).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058088.
VAR_SEQ 188 382 Missing (in isoform 5).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058089.
VAR_SEQ 320 328 Missing (in isoform 3 and isoform 4).
{ECO:0000269|PubMed:19164451}.
/FTId=VSP_058090.
VAR_SEQ 330 333 SVGE -> EGLD (in isoform 2).
{ECO:0000269|PubMed:16503878,
ECO:0000269|PubMed:19164451}.
/FTId=VSP_058091.
VAR_SEQ 334 402 Missing (in isoform 2).
{ECO:0000269|PubMed:16503878,
ECO:0000269|PubMed:19164451}.
/FTId=VSP_058092.
VAR_SEQ 372 384 KAPESQEDEEERA -> PRKARRMRRNVQS (in
isoform 10).
{ECO:0000269|PubMed:24260107}.
/FTId=VSP_058093.
VAR_SEQ 385 402 Missing (in isoform 10).
{ECO:0000269|PubMed:24260107}.
/FTId=VSP_058094.
CONFLICT 28 30 ARI -> TQA (in Ref. 3; ACK28146).
{ECO:0000305}.
CONFLICT 76 76 R -> Q (in Ref. 1; AAA40040 and 2;
BAE72665). {ECO:0000305}.
CONFLICT 199 199 G -> GT (in Ref. 1; AAA40040 and 2;
BAE72665). {ECO:0000305}.
CONFLICT 292 292 E -> A (in Ref. 1; AAA40040 and 2;
BAE72665). {ECO:0000305}.
SEQUENCE 402 AA; 42654 MW; DBFDC50A6C8CB902 CRC64;
MPAGTAARAW VLVLALWGAV AGGQNITARI GEPLVLSCKG APKKPPQQLE WKLNTGRTEA
WKVLSPQGGP WDSVARILPN GSLLLPATGI VDEGTFRCRA TNRRGKEVKS NYRVRVYQIP
GKPEIVDPAS ELTASVPNKV GTCVSEGSYP AGTLSWHLDG KLLIPDGKET LVKEETRRHP
ETGLFTLRSE LTVIPTQGGT HPTFSCSFSL GLPRRRPLNT APIQLRVREP GPPEGIQLLV
EPEGGIVAPG GTVTLTCAIS AQPPPQVHWI KDGAPLPLAP SPVLLLPEVG HEDEGTYSCV
ATHPSHGPQE SPPVSIRVTE TGDEGPAEGS VGESGLGTLA LALGILGGLG VVALLVGAIL
WRKRQPRREE RKAPESQEDE EERAELNQSE EAEMPENGAG GP


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