RAGE_MOUSE
ID RAGE_MOUSE Reviewed; 402 AA.
AC Q62151; C5H3H4; C5H3H5; C5H3H7; C5H3I0; C5H7W3; C5H7W4; C5H7W5; C5H7W6;
AC C5H7W7; C5H7W8; C5H7W9; O35444; Q2PGG1; V5R4Y0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Advanced glycosylation end product-specific receptor;
DE AltName: Full=Receptor for advanced glycosylation end products;
DE Flags: Precursor;
GN Name=Ager; Synonyms=Rage;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=9224812; DOI=10.1124/mol.52.1.54;
RA Renard C., Chappey O., Wautier M.P., Nagashima M., Lundh E., Morser J.,
RA Zhao L., Schmidt A.M., Scherrmann J.M., Wautier J.-L.;
RT "Recombinant advanced glycation end product receptor pharmacokinetics in
RT normal and diabetic rats.";
RL Mol. Pharmacol. 52:54-62(1997).
RN [2] {ECO:0000312|EMBL:BAE72665.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORM 2), SUBCELLULAR
RP LOCATION (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J {ECO:0000303|PubMed:16503878};
RC TISSUE=Brain {ECO:0000303|PubMed:16503878};
RX PubMed=16503878; DOI=10.1042/bj20051573;
RA Harashima A., Yamamoto Y., Cheng C., Tsuneyama K., Myint K.M., Takeuchi A.,
RA Yoshimura K., Li H., Watanabe T., Takasawa S., Okamoto H., Yonekura H.,
RA Yamamoto H.;
RT "Identification of mouse orthologue of endogenous secretory receptor for
RT advanced glycation end-products: structure, function and expression.";
RL Biochem. J. 396:109-115(2006).
RN [3] {ECO:0000312|EMBL:ACD35949.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 11; 12 AND
RP 13), SPLICE ISOFORMS THAT ARE POTENTIAL NMD TARGETS, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:ACD35949.1};
RX PubMed=19164451; DOI=10.1096/fj.08-117739;
RA Kalea A.Z., Reiniger N., Yang H., Arriero M., Schmidt A.M., Hudson B.I.;
RT "Alternative splicing of the murine receptor for advanced glycation end-
RT products (RAGE) gene.";
RL FASEB J. 23:1766-1774(2009).
RN [4] {ECO:0000312|EMBL:AHB30242.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), FUNCTION (ISOFORM 10), SUBCELLULAR
RP LOCATION (ISOFORM 10), AND TISSUE SPECIFICITY.
RC TISSUE=Lung {ECO:0000312|EMBL:AHB30242.1};
RX PubMed=24260107; DOI=10.1371/journal.pone.0078267;
RA Jules J., Maiguel D., Hudson B.I.;
RT "Alternative splicing of the RAGE cytoplasmic domain regulates cell
RT signaling and function.";
RL PLoS ONE 8:E78267-E78267(2013).
RN [5] {ECO:0000312|EMBL:AAB82007.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [6] {ECO:0000312|EMBL:CT009767, ECO:0000312|Ensembl:ENSMUSP00000015596, ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Ensembl:ENSMUSP00000015596,
RC ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7] {ECO:0000312|EMBL:EDL26799.1, ECO:0000312|EMBL:EDL26800.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000312|EMBL:AAH61182.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP FUNCTION, AND INTERACTION WITH S100A12.
RC TISSUE=Lung;
RX PubMed=10399917; DOI=10.1016/s0092-8674(00)80801-6;
RA Hofmann M.A., Drury S., Fu C., Qu W., Taguchi A., Lu Y., Avila C.,
RA Kambham N., Bierhaus A., Nawroth P., Neurath M.F., Slattery T., Beach D.,
RA McClary J., Nagashima M., Morser J., Stern D., Schmidt A.M.;
RT "RAGE mediates a novel proinflammatory axis: a central cell surface
RT receptor for S100/calgranulin polypeptides.";
RL Cell 97:889-901(1999).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18539754; DOI=10.1152/ajpheart.00464.2008;
RA Gao X., Zhang H., Schmidt A.M., Zhang C.;
RT "AGE/RAGE produces endothelial dysfunction in coronary arterioles in type 2
RT diabetic mice.";
RL Am. J. Physiol. 295:H491-H498(2008).
RN [11]
RP FUNCTION, AND INTERACTION WITH APP.
RX PubMed=19901339; DOI=10.1073/pnas.0905686106;
RA Takuma K., Fang F., Zhang W., Yan S., Fukuzaki E., Du H., Sosunov A.,
RA McKhann G., Funatsu Y., Nakamichi N., Nagai T., Mizoguchi H., Ibi D.,
RA Hori O., Ogawa S., Stern D.M., Yamada K., Yan S.S.;
RT "RAGE-mediated signaling contributes to intraneuronal transport of
RT amyloid-{beta} and neuronal dysfunction.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20021-20026(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION.
RX PubMed=19906677; DOI=10.1096/fj.09-139634;
RA Fang F., Lue L.-F., Yan S., Xu H., Luddy J.S., Chen D., Walker D.G.,
RA Stern D.M., Yan S., Schmidt A.M., Chen J.X., Yan S.S.;
RT "RAGE-dependent signaling in microglia contributes to neuroinflammation,
RT Abeta accumulation, and impaired learning/memory in a mouse model of
RT Alzheimer's disease.";
RL FASEB J. 24:1043-1055(2010).
CC -!- FUNCTION: Mediates interactions of advanced glycosylation end products
CC (AGE). These are nonenzymatically glycosylated proteins which
CC accumulate in vascular tissue in aging and at an accelerated rate in
CC diabetes. Acts as a mediator of both acute and chronic vascular
CC inflammation in conditions such as atherosclerosis and in particular as
CC a complication of diabetes. AGE/RAGE signaling plays an important role
CC in regulating the production/expression of TNF-alpha, oxidative stress,
CC and endothelial dysfunction in type 2 diabetes. Interaction with
CC S100A12 on endothelium, mononuclear phagocytes, and lymphocytes
CC triggers cellular activation, with generation of key pro-inflammatory
CC mediators. Interaction with S100B after myocardial infarction may play
CC a role in myocyte apoptosis by activating ERK1/2 and p53/TP53
CC signaling. Can also bind oligonucleotides. Receptor for amyloid beta
CC peptide. Contributes to the translocation of amyloid-beta peptide
CC (ABPP) across the cell membrane from the extracellular to the
CC intracellular space in cortical neurons. ABPP-initiated RAGE signaling,
CC especially stimulation of p38 mitogen-activated protein kinase (MAPK),
CC has the capacity to drive a transport system delivering ABPP as a
CC complex with RAGE to the intraneuronal space. RAGE-dependent signaling
CC in microglia contributes to neuroinflammation, amyloid accumulation,
CC and impaired learning/memory in a mouse model of Alzheimer disease.
CC {ECO:0000269|PubMed:10399917, ECO:0000269|PubMed:18539754,
CC ECO:0000269|PubMed:19901339, ECO:0000269|PubMed:19906677}.
CC -!- FUNCTION: [Isoform 2]: Is able to advanced glycosylation end product
CC (AGE)-induce nuclear factor NF-kappa-B activation.
CC {ECO:0000269|PubMed:16503878}.
CC -!- FUNCTION: [Isoform 10]: Down-regulates receptor for advanced
CC glycosylation end products (RAGE)-ligand induced signaling through
CC various MAPK pathways including ERK1/2, p38 and SAPK/JNK. Significantly
CC affects tumor cell properties through decreasing cell migration,
CC invasion, adhesion and proliferation, and increasing cellular
CC apoptosis. Exhibits drastic inhibition on tumorigenesis in vitro.
CC {ECO:0000269|PubMed:24260107}.
CC -!- SUBUNIT: Interacts with S100B, S100A1 and S100A14. Constitutive
CC homodimer; disulfide-linked (By similarity). Interacts with S100A12 and
CC APP. {ECO:0000250, ECO:0000269|PubMed:10399917,
CC ECO:0000269|PubMed:19901339}.
CC -!- INTERACTION:
CC Q62151; Q02956: Prkcz; NbExp=7; IntAct=EBI-6665091, EBI-642057;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass type I
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:16503878}.
CC -!- SUBCELLULAR LOCATION: [Isoform 10]: Cell membrane
CC {ECO:0000269|PubMed:24260107}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=13;
CC Name=1; Synonyms=mRAGE {ECO:0000303|PubMed:19164451};
CC IsoId=Q62151-1; Sequence=Displayed;
CC Name=2; Synonyms=mRAGE_v1 {ECO:0000303|PubMed:19164451}, mRAGE_v3
CC {ECO:0000303|PubMed:19164451}, endogenous secretory receptor for AGE
CC (esRAGE) {ECO:0000303|PubMed:16503878};
CC IsoId=Q62151-2; Sequence=VSP_058091, VSP_058092;
CC Name=3; Synonyms=mRAGE_v4 {ECO:0000303|PubMed:19164451};
CC IsoId=Q62151-3; Sequence=VSP_058090;
CC Name=4; Synonyms=mRAGE_v15 {ECO:0000303|PubMed:19164451};
CC IsoId=Q62151-4; Sequence=VSP_058080, VSP_058090;
CC Name=5; Synonyms=mRAGE_v14 {ECO:0000303|PubMed:19164451};
CC IsoId=Q62151-5; Sequence=VSP_058089;
CC Name=6; Synonyms=mRAGE_v10 {ECO:0000303|PubMed:19164451};
CC IsoId=Q62151-6; Sequence=VSP_058087, VSP_058088;
CC Name=7; Synonyms=mRAGE_v7 {ECO:0000303|PubMed:19164451};
CC IsoId=Q62151-7; Sequence=VSP_058083, VSP_058086;
CC Name=8; Synonyms=mRAGE_v11 {ECO:0000303|PubMed:19164451};
CC IsoId=Q62151-8; Sequence=VSP_058084, VSP_058085;
CC Name=9; Synonyms=mRAGE_v9 {ECO:0000303|PubMed:19164451};
CC IsoId=Q62151-9; Sequence=VSP_058076, VSP_058082;
CC Name=10; Synonyms=RAGE deletion of intracellular domain
CC {ECO:0000303|PubMed:24260107}, RAGEdeltaICD
CC {ECO:0000303|PubMed:24260107}, mRAGE_v20 {ECO:0000303|PubMed:24260107};
CC IsoId=Q62151-10; Sequence=VSP_058093, VSP_058094;
CC Name=11; Synonyms=mRAGE_v2 {ECO:0000303|PubMed:19164451}, mRAGE_v5
CC {ECO:0000303|PubMed:19164451}, mRAGE_v6 {ECO:0000303|PubMed:19164451},
CC mRAGE_v8 {ECO:0000303|PubMed:19164451}, mRAGE_v16
CC {ECO:0000303|PubMed:19164451}, mRAGE_v17 {ECO:0000303|PubMed:19164451};
CC IsoId=Q62151-11; Sequence=VSP_058075, VSP_058081;
CC Name=12; Synonyms=mRAGE_v13 {ECO:0000303|PubMed:19164451};
CC IsoId=Q62151-12; Sequence=VSP_058077, VSP_058079;
CC Name=13; Synonyms=mRAGE_v12 {ECO:0000303|PubMed:19164451};
CC IsoId=Q62151-13; Sequence=VSP_058078;
CC -!- TISSUE SPECIFICITY: Isoform 1: Expressed at higher levels in the
CC coronary arterioles in type 2 diabetic mice (at protein level).
CC Endothelial cells (PubMed:18539754). Expressed in lung, kidney, brain
CC and heart. Most prevalent isoform with the highest level in heart
CC (PubMed:19164451). Isoform 2: Expressed in brain, lung, kidney and
CC small intestine with the highest level in lung. Expressed in brain,
CC lung, kidney and small intestine with the highest level in small
CC intestine (at protein level). Detected in neurons of the cerebrum,
CC bronchial epithelium, endothelial cells, tubular cells of kidney and
CC epithelial cells of small intestine (at protein level). Expression is
CC increased in the kidney of diabetic wild-type mice (at protein level),
CC but not in the other tissues (PubMed:16503878). Expressed only in
CC kidney. Expression is increased in the kidney of diabetic mice
CC (PubMed:19164451). Isoform 3: Expressed in lung, kidney and heart. The
CC second most prevalent isoform with the highest level in lung. Not
CC expressed in brain (PubMed:19164451). Isoform 4: Expressed at very low
CC level in lung only (PubMed:19164451). Isoform 5: Expressed at very low
CC level in lung only (PubMed:19164451). Isoform 6: Expressed at very low
CC level in lung only (PubMed:19164451). Isoform 7: Expressed at very low
CC level in heart only (PubMed:19164451). Isoform 8: Expressed at very low
CC level in lung only (PubMed:19164451). Isoform 9: Expressed at very low
CC level in heart only (PubMed:19164451). Isoform 10: Expressed in lung,
CC brain, heart and kidney with a very high level in kidney
CC (PubMed:24260107). Isoform 11: Expressed in brain, kidney and heart.
CC Not expressed in lung (PubMed:19164451). Isoform 12: Expressed at very
CC low level in lung and kidney (PubMed:19164451). Isoform 13: Expressed
CC at very low level in lung only (PubMed:19164451).
CC {ECO:0000269|PubMed:16503878, ECO:0000269|PubMed:18539754,
CC ECO:0000269|PubMed:19164451, ECO:0000269|PubMed:24260107}.
CC -!- MISCELLANEOUS: [Isoform 7]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000269|PubMed:19164451}.
CC -!- MISCELLANEOUS: [Isoform 8]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000269|PubMed:19164451}.
CC -!- MISCELLANEOUS: [Isoform 9]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000269|PubMed:19164451}.
CC -!- MISCELLANEOUS: [Isoform 11]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000269|PubMed:19164451}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L33412; AAA40040.1; -; mRNA.
DR EMBL; AB207883; BAE72665.1; -; mRNA.
DR EMBL; EU520325; ACD35949.1; -; mRNA.
DR EMBL; EU570240; ACE63492.1; -; mRNA.
DR EMBL; EU570241; ACE63493.1; -; mRNA.
DR EMBL; EU570242; ACE63494.1; -; mRNA.
DR EMBL; EU570243; ACE63495.1; -; mRNA.
DR EMBL; EU570244; ACE63496.1; -; mRNA.
DR EMBL; EU570245; ACE63497.1; -; mRNA.
DR EMBL; EU570246; ACE63498.1; -; mRNA.
DR EMBL; EU570247; ACE63499.1; -; mRNA.
DR EMBL; EU906857; ACK28143.1; -; mRNA.
DR EMBL; EU906858; ACK28144.1; -; mRNA.
DR EMBL; EU906859; ACK28145.1; -; mRNA.
DR EMBL; EU906860; ACK28146.1; -; mRNA.
DR EMBL; EU906861; ACK28147.1; -; mRNA.
DR EMBL; EU906862; ACK28148.1; -; mRNA.
DR EMBL; EU906863; ACK28149.1; -; mRNA.
DR EMBL; EU906864; ACK28150.1; -; mRNA.
DR EMBL; EU906865; ACK28151.1; -; mRNA.
DR EMBL; KC692918; AHB30242.1; -; mRNA.
DR EMBL; AF030001; AAB82007.1; -; Genomic_DNA.
DR EMBL; CT009767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466666; EDL26799.1; -; Genomic_DNA.
DR EMBL; CH466666; EDL26800.1; -; Genomic_DNA.
DR EMBL; BC061182; AAH61182.1; -; mRNA.
DR CCDS; CCDS28649.1; -. [Q62151-1]
DR CCDS; CCDS70795.1; -. [Q62151-3]
DR CCDS; CCDS70796.1; -. [Q62151-4]
DR PIR; T09062; T09062.
DR RefSeq; NP_001258351.1; NM_001271422.1. [Q62151-3]
DR RefSeq; NP_001258352.1; NM_001271423.1. [Q62151-4]
DR RefSeq; NP_031451.2; NM_007425.3. [Q62151-1]
DR PDB; 4IM8; X-ray; 3.50 A; A=23-230.
DR PDBsum; 4IM8; -.
DR AlphaFoldDB; Q62151; -.
DR SMR; Q62151; -.
DR IntAct; Q62151; 7.
DR STRING; 10090.ENSMUSP00000015596; -.
DR ChEMBL; CHEMBL2189161; -.
DR GlyGen; Q62151; 2 sites.
DR iPTMnet; Q62151; -.
DR PhosphoSitePlus; Q62151; -.
DR MaxQB; Q62151; -.
DR PaxDb; Q62151; -.
DR PRIDE; Q62151; -.
DR ProteomicsDB; 255077; -. [Q62151-1]
DR ProteomicsDB; 255078; -. [Q62151-2]
DR ProteomicsDB; 255079; -. [Q62151-3]
DR ProteomicsDB; 255080; -. [Q62151-4]
DR ProteomicsDB; 255081; -. [Q62151-5]
DR ProteomicsDB; 255082; -. [Q62151-6]
DR ProteomicsDB; 255083; -. [Q62151-7]
DR ProteomicsDB; 255084; -. [Q62151-8]
DR ProteomicsDB; 255086; -. [Q62151-10]
DR ABCD; Q62151; 1 sequenced antibody.
DR Antibodypedia; 28483; 846 antibodies from 45 providers.
DR DNASU; 11596; -.
DR Ensembl; ENSMUST00000015596; ENSMUSP00000015596; ENSMUSG00000015452. [Q62151-1]
DR Ensembl; ENSMUST00000173992; ENSMUSP00000134579; ENSMUSG00000015452. [Q62151-4]
DR Ensembl; ENSMUST00000174069; ENSMUSP00000133391; ENSMUSG00000015452. [Q62151-2]
DR Ensembl; ENSMUST00000174496; ENSMUSP00000134401; ENSMUSG00000015452. [Q62151-3]
DR GeneID; 11596; -.
DR KEGG; mmu:11596; -.
DR UCSC; uc008ccw.3; mouse.
DR UCSC; uc008ccx.2; mouse.
DR UCSC; uc012aqe.2; mouse.
DR UCSC; uc012aqf.2; mouse.
DR UCSC; uc012aqg.2; mouse.
DR UCSC; uc033hcv.1; mouse.
DR CTD; 177; -.
DR MGI; MGI:893592; Ager.
DR VEuPathDB; HostDB:ENSMUSG00000015452; -.
DR eggNOG; ENOG502SQ8N; Eukaryota.
DR GeneTree; ENSGT00890000139566; -.
DR InParanoid; Q62151; -.
DR OMA; HWMKDGM; -.
DR OrthoDB; 807961at2759; -.
DR PhylomeDB; Q62151; -.
DR TreeFam; TF337155; -.
DR Reactome; R-MMU-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-MMU-879415; Advanced glycosylation endproduct receptor signaling.
DR Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
DR BioGRID-ORCS; 11596; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Mok; mouse.
DR PRO; PR:Q62151; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q62151; protein.
DR Bgee; ENSMUSG00000015452; Expressed in right lung lobe and 126 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0070379; F:high mobility group box 1 binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
DR GO; GO:0048143; P:astrocyte activation; ISO:MGI.
DR GO; GO:0014002; P:astrocyte development; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IMP:ARUK-UCL.
DR GO; GO:0010255; P:glucose mediated signaling pathway; ISO:MGI.
DR GO; GO:0050930; P:induction of positive chemotaxis; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IGI:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0001774; P:microglial cell activation; IGI:ARUK-UCL.
DR GO; GO:1903523; P:negative regulation of blood circulation; IGI:ARUK-UCL.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; ISO:MGI.
DR GO; GO:1900453; P:negative regulation of long-term synaptic depression; ISO:MGI.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; IGI:ARUK-UCL.
DR GO; GO:2001200; P:positive regulation of dendritic cell differentiation; ISO:MGI.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:1904472; P:positive regulation of endothelin production; IGI:ARUK-UCL.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; ISO:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IGI:ARUK-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; ISO:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IGI:ARUK-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:MGI.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IGI:MGI.
DR GO; GO:2000439; P:positive regulation of monocyte extravasation; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI.
DR GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; ISO:MGI.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IGI:ARUK-UCL.
DR GO; GO:2000676; P:positive regulation of type B pancreatic cell apoptotic process; ISO:MGI.
DR GO; GO:0072657; P:protein localization to membrane; IMP:MGI.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:2000514; P:regulation of CD4-positive, alpha-beta T cell activation; ISO:MGI.
DR GO; GO:0051101; P:regulation of DNA binding; IMP:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IMP:ARUK-UCL.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; IGI:ARUK-UCL.
DR GO; GO:0150003; P:regulation of spontaneous synaptic transmission; ISO:MGI.
DR GO; GO:0001914; P:regulation of T cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:1904645; P:response to amyloid-beta; IGI:ARUK-UCL.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0045056; P:transcytosis; IMP:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Inflammatory response; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..402
FT /note="Advanced glycosylation end product-specific
FT receptor"
FT /id="PRO_0000014924"
FT TOPO_DOM 23..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..109
FT /note="Ig-like V-type"
FT DOMAIN 123..219
FT /note="Ig-like C2-type 1"
FT DOMAIN 233..315
FT /note="Ig-like C2-type 2"
FT REGION 295..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63495"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 143..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 257
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 299
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 19..77
FT /note="AVAGGQNITARIGEPLVLSCKGAPKKPPQQLEWKLNTGRTEAWKVLSPQGGP
FT WDSVARI -> ETLPAPTLPLSSPAPTPPPVPPCPLEIPLNLGTTFQRPSPTLSYTRTP
FT QPHLSPSTLPQ (in isoform 11)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058075"
FT VAR_SEQ 27..85
FT /note="TARIGEPLVLSCKGAPKKPPQQLEWKLNTGRTEAWKVLSPQGGPWDSVARIL
FT PNGSLLL -> PALCCSSLRWGTRMRAPIAAWPPTLATDLRKALLSASGSQKPAMRGQL
FT KALWVSLGWVR (in isoform 9)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058076"
FT VAR_SEQ 30..40
FT /note="IGEPLVLSCKG -> KARRMRRNVQS (in isoform 12)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058077"
FT VAR_SEQ 31..402
FT /note="Missing (in isoform 13)"
FT /id="VSP_058078"
FT VAR_SEQ 41..402
FT /note="Missing (in isoform 12)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058079"
FT VAR_SEQ 54..62
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058080"
FT VAR_SEQ 78..402
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058081"
FT VAR_SEQ 86..402
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058082"
FT VAR_SEQ 118..138
FT /note="QIPGKPEIVDPASELTASVPN -> RKGPRLSHFAFIKKPSCTPNP (in
FT isoform 7)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058083"
FT VAR_SEQ 119..137
FT /note="IPGKPEIVDPASELTASVP -> KPAMRGQLKALWVSLGWVR (in
FT isoform 8)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058084"
FT VAR_SEQ 138..402
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058085"
FT VAR_SEQ 139..402
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058086"
FT VAR_SEQ 153
FT /note="T -> G (in isoform 6)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058087"
FT VAR_SEQ 154..402
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058088"
FT VAR_SEQ 188..382
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058089"
FT VAR_SEQ 320..328
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000269|PubMed:19164451"
FT /id="VSP_058090"
FT VAR_SEQ 330..333
FT /note="SVGE -> EGLD (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:16503878,
FT ECO:0000269|PubMed:19164451"
FT /id="VSP_058091"
FT VAR_SEQ 334..402
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:16503878,
FT ECO:0000269|PubMed:19164451"
FT /id="VSP_058092"
FT VAR_SEQ 372..384
FT /note="KAPESQEDEEERA -> PRKARRMRRNVQS (in isoform 10)"
FT /evidence="ECO:0000269|PubMed:24260107"
FT /id="VSP_058093"
FT VAR_SEQ 385..402
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000269|PubMed:24260107"
FT /id="VSP_058094"
FT CONFLICT 28..30
FT /note="ARI -> TQA (in Ref. 3; ACK28146)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="R -> Q (in Ref. 1; AAA40040 and 2; BAE72665)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="G -> GT (in Ref. 1; AAA40040 and 2; BAE72665)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="E -> A (in Ref. 1; AAA40040 and 2; BAE72665)"
FT /evidence="ECO:0000305"
SQ 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
