ID RAGE_HUMAN Reviewed; 404 AA.
AC Q15109; A2BFI7; A6NKF0; A7Y2U9; B0V176; Q15279; Q3L1R4; Q3L1R5; Q3L1R6;
AC Q3L1R7; Q3L1R8; Q3L1S0; Q86SN1; Q9H2X7; Q9Y3R3; V5R6A3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 227.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=1378843; DOI=10.1016/s0021-9258(18)42138-2;
RA Neeper M., Schmidt A.M., Brett J., Yan S.D., Wang F., Pan Y.C.,
RA Elliston K., Stern D., Shaw A.;
RT "Cloning and expression of a cell surface receptor for advanced
RT glycosylation end products of proteins.";
RL J. Biol. Chem. 267:14998-15004(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=7835890; DOI=10.1006/geno.1994.1517;
RA Sugaya K., Fukagawa T., Matsumoto K., Mita K., Takahashi E., Ando A.,
RA Inoko H., Ikemura T.;
RT "Three genes in the human MHC class III region near the junction with the
RT class II: gene for receptor of advanced glycosylation end products, PBX2
RT homeobox gene and a notch homolog, human counterpart of mouse mammary tumor
RT gene int-3.";
RL Genomics 23:408-419(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-100.
RA Abedin M.J., Yonekura H., Migita H., Karasawa J., Yamamoto Y., Yamamoto H.;
RT "Molecular heterogeneity of the receptor for advanced glycation
RT endproducts.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Malherbe P., Richards J., Gaillard H., Thompson A., Diener C., Schuler A.,
RA Huber G.;
RT "cDNA cloning of a novel secreted isoform of the human receptor for
RT advanced glycation end products (RAGE) and characterization of cells co-
RT expressing cell-surface scavenger receptors and Swedish mutant amyloid
RT precursor protein.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
RC TISSUE=Skin;
RX PubMed=12495433; DOI=10.1042/bj20021371;
RA Yonekura H., Yamamoto Y., Sakurai S., Petrova R.G., Abedin J., Li H.,
RA Yasui K., Takeuchi M., Makita Z., Takasawa S., Okamoto H., Watanabe T.,
RA Yamamoto H.;
RT "Novel splice variants of the receptor for advanced glycation end-products
RT expressed in human vascular endothelial cells and pericytes, and their
RT putative roles in diabetes-induced vascular injury.";
RL Biochem. J. 370:1097-1109(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6; 7; 8 AND 9), AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Aortic smooth muscle, and Lung;
RX PubMed=18089847; DOI=10.1096/fj.07-9909com;
RA Hudson B.I., Carter A.M., Harja E., Kalea A.Z., Arriero M., Yang H.,
RA Grant P.J., Schmidt A.M.;
RT "Identification, classification, and expression of RAGE gene splice
RT variants.";
RL FASEB J. 22:1572-1580(2008).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), AND SUBCELLULAR LOCATION (ISOFORM
RP 10).
RC TISSUE=Lung;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-82.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RX PubMed=11375354; DOI=10.2337/diabetes.50.6.1505;
RA Hudson B.I., Stickland M.H., Futers T.S., Grant P.J.;
RT "Effects of novel polymorphisms in the RAGE gene on transcriptional
RT regulation and their association with diabetic retinopathy.";
RL Diabetes 50:1505-1511(2001).
RN [14]
RP INTERACTION WITH S100A12.
RX PubMed=19386136; DOI=10.1186/1471-2091-10-11;
RA Moroz O.V., Burkitt W., Wittkowski H., He W., Ianoul A., Novitskaya V.,
RA Xie J., Polyakova O., Lednev I.K., Shekhtman A., Derrick P.J., Bjoerk P.,
RA Foell D., Bronstein I.B.;
RT "Both Ca2+ and Zn2+ are essential for S100A12 protein oligomerization and
RT function.";
RL BMC Biochem. 10:11-11(2009).
RN [15]
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).
RN [16]
RP INTERACTION WITH S100A14, AND FUNCTION.
RX PubMed=21559403; DOI=10.1371/journal.pone.0019375;
RA Jin Q., Chen H., Luo A., Ding F., Liu Z.;
RT "S100A14 stimulates cell proliferation and induces cell apoptosis at
RT different concentrations via receptor for advanced glycation end products
RT (RAGE).";
RL PLoS ONE 6:E19375-E19375(2011).
RN [17]
RP FUNCTION, PHOSPHORYLATION AT SER-391, INTERACTION WITH TIRAP, AND
RP MUTAGENESIS OF SER-391.
RX PubMed=21829704; DOI=10.1371/journal.pone.0023132;
RA Sakaguchi M., Murata H., Yamamoto K., Ono T., Sakaguchi Y., Motoyama A.,
RA Hibino T., Kataoka K., Huh N.H.;
RT "TIRAP, an adaptor protein for TLR2/4, transduces a signal from RAGE
RT phosphorylated upon ligand binding.";
RL PLoS ONE 6:e23132-e23132(2011).
RN [18]
RP SUBUNIT, AND INTERCHAIN DISULFIDE BONDS.
RX PubMed=23284645; DOI=10.1371/journal.pone.0050736;
RA Wei W., Lampe L., Park S., Vangara B.S., Waldo G.S., Cabantous S.,
RA Subaran S.S., Yang D., Lakatta E.G., Lin L.;
RT "Disulfide bonds within the C2 domain of RAGE play key roles in its
RT dimerization and biogenesis.";
RL PLoS ONE 7:E50736-E50736(2012).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27572515; DOI=10.1038/srep32180;
RA Shang D., Peng T., Gou S., Li Y., Wu H., Wang C., Yang Z.;
RT "High Mobility Group Box Protein 1 Boosts Endothelial Albumin Transcytosis
RT through the RAGE/Src/Caveolin-1 Pathway.";
RL Sci. Rep. 6:32180-32180(2016).
RN [20]
RP FUNCTION, UBIQUITINATION AT LYS-374, AND MUTAGENESIS OF LYS-374.
RX PubMed=28515150; DOI=10.1096/fj.201700031r;
RA Evankovich J., Lear T., Mckelvey A., Dunn S., Londino J., Liu Y.,
RA Chen B.B., Mallampalli R.K.;
RT "Receptor for advanced glycation end products is targeted by FBXO10 for
RT ubiquitination and degradation.";
RL FASEB J. 31:3894-3903(2017).
RN [21]
RP FUNCTION, AND INTERACTION WITH HMGB1.
RX PubMed=34743181; DOI=10.1038/s41420-021-00729-0;
RA Wang G., Jin S., Huang W., Li Y., Wang J., Ling X., Huang Y., Hu Y., Li C.,
RA Meng Y., Li X.;
RT "LPS-induced macrophage HMGB1-loaded extracellular vesicles trigger
RT hepatocyte pyroptosis by activating the NLRP3 inflammasome.";
RL Cell. Death. Discov. 7:337-337(2021).
RN [22]
RP STRUCTURE BY NMR OF 23-121, STRUCTURE BY NMR OF 235-323, AND DISULFIDE
RP BONDS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the third Ig-like domain from human advanced
RT glycosylation end product-specific receptor.";
RL Submitted (APR-2008) to the PDB data bank.
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 23-231, FUNCTION, DNA-BINDING,
RP INTERACTION WITH S100B, AND DISULFIDE BOND.
RX PubMed=20943659; DOI=10.1074/jbc.m110.169276;
RA Park H., Adsit F.G., Boyington J.C.;
RT "The 1.5 A crystal structure of human receptor for advanced glycation
RT endproducts (RAGE) ectodomains reveals unique features determining ligand
RT binding.";
RL J. Biol. Chem. 285:40762-40770(2010).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 23-240, INTERACTION WITH S100B,
RP AND DISULFIDE BONDS.
RX PubMed=20947022; DOI=10.1016/j.str.2010.05.017;
RA Koch M., Chitayat S., Dattilo B.M., Schiefner A., Diez J., Chazin W.J.,
RA Fritz G.;
RT "Structural basis for ligand recognition and activation of RAGE.";
RL Structure 18:1342-1352(2010).
RN [25]
RP STRUCTURE BY NMR OF 23-125, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=21565706; DOI=10.1016/j.str.2011.02.013;
RA Xue J., Rai V., Singer D., Chabierski S., Xie J., Reverdatto S., Burz D.S.,
RA Schmidt A.M., Hoffmann R., Shekhtman A.;
RT "Advanced glycation end product recognition by the receptor for AGEs.";
RL Structure 19:722-732(2011).
RN [26] {ECO:0007744|PDB:4OI7, ECO:0007744|PDB:4OI8}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 23-237, FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24081950; DOI=10.1084/jem.20120201;
RA Sirois C.M., Jin T., Miller A.L., Bertheloot D., Nakamura H., Horvath G.L.,
RA Mian A., Jiang J., Schrum J., Bossaller L., Pelka K., Garbi N., Brewah Y.,
RA Tian J., Chang C., Chowdhury P.S., Sims G.P., Kolbeck R., Coyle A.J.,
RA Humbles A.A., Xiao T.S., Latz E.;
RT "RAGE is a nucleic acid receptor that promotes inflammatory responses to
RT DNA.";
RL J. Exp. Med. 210:2447-2463(2013).
CC -!- FUNCTION: Cell surface pattern recognition receptor that senses
CC endogenous stress signals with a broad ligand repertoire including
CC advanced glycation end products, S100 proteins, high-mobility group box
CC 1 protein/HMGB1, amyloid beta/APP oligomers, nucleic acids,
CC phospholipids and glycosaminoglycans (PubMed:27572515, PubMed:28515150,
CC PubMed:34743181). Advanced glycosylation end products are
CC nonenzymatically glycosylated proteins which accumulate in vascular
CC tissue in aging and at an accelerated rate in diabetes
CC (PubMed:21565706). These ligands accumulate at inflammatory sites
CC during the pathogenesis of various diseases, including diabetes,
CC vascular complications, neurodegenerative disorders, and cancers and
CC RAGE transduces their binding into pro-inflammatory responses. Upon
CC ligand binding, uses TIRAP and MYD88 as adapters to transduce the
CC signal ultimately leading to the induction or inflammatory cytokines
CC IL6, IL8 and TNFalpha through activation of NF-kappa-B
CC (PubMed:21829704). Interaction with S100A12 on endothelium, mononuclear
CC phagocytes, and lymphocytes triggers cellular activation, with
CC generation of key pro-inflammatory mediators (PubMed:19386136).
CC Interaction with S100B after myocardial infarction may play a role in
CC myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By
CC similarity). 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 (PubMed:19906677). ABPP-
CC initiated RAGE signaling, especially stimulation of p38 mitogen-
CC activated protein kinase (MAPK), has the capacity to drive a transport
CC system delivering ABPP as a complex with RAGE to the intraneuronal
CC space. Participates in endothelial albumin transcytosis together with
CC HMGB1 through the RAGE/SRC/Caveolin-1 pathway, leading to endothelial
CC hyperpermeability (PubMed:27572515). Mediates the loading of HMGB1 in
CC extracellular vesicles (EVs) that shuttle HMGB1 to hepatocytes by
CC transferrin-mediated endocytosis and subsequently promote hepatocyte
CC pyroptosis by activating the NLRP3 inflammasome (PubMed:34743181).
CC Promotes also extracellular hypomethylated DNA (CpG DNA) uptake by
CC cells via the endosomal route to activate inflammatory responses
CC (PubMed:24081950, PubMed:28515150). {ECO:0000250|UniProtKB:Q62151,
CC ECO:0000269|PubMed:19906677, ECO:0000269|PubMed:20943659,
CC ECO:0000269|PubMed:21559403, ECO:0000269|PubMed:21565706,
CC ECO:0000269|PubMed:21829704, ECO:0000269|PubMed:24081950,
CC ECO:0000269|PubMed:27572515, ECO:0000269|PubMed:28515150,
CC ECO:0000269|PubMed:34743181}.
CC -!- SUBUNIT: Constitutive homodimer; disulfide-linked (PubMed:24081950).
CC Forms homooligomers (PubMed:24081950). Interacts with S100A1 and APP
CC (By similarity). Interacts with S100B, S100A12 and S100A14. Interacts
CC with TIRAP (PubMed:21829704). Interacts with HMGB1 (PubMed:34743181).
CC {ECO:0000250|UniProtKB:Q62151, ECO:0000269|PubMed:19386136,
CC ECO:0000269|PubMed:20943659, ECO:0000269|PubMed:20947022,
CC ECO:0000269|PubMed:21559403, ECO:0000269|PubMed:21565706,
CC ECO:0000269|PubMed:21829704, ECO:0000269|PubMed:23284645,
CC ECO:0000269|PubMed:24081950, ECO:0000269|PubMed:34743181}.
CC -!- INTERACTION:
CC Q15109; Q15109: AGER; NbExp=2; IntAct=EBI-1646426, EBI-1646426;
CC Q15109; P05067: APP; NbExp=3; IntAct=EBI-1646426, EBI-77613;
CC Q15109; P23560-2: BDNF; NbExp=3; IntAct=EBI-1646426, EBI-12275524;
CC Q15109; Q8WU43: C2orf15; NbExp=3; IntAct=EBI-1646426, EBI-12904676;
CC Q15109; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-1646426, EBI-2807956;
CC Q15109; O43889-2: CREB3; NbExp=3; IntAct=EBI-1646426, EBI-625022;
CC Q15109; O60610: DIAPH1; NbExp=3; IntAct=EBI-1646426, EBI-3959709;
CC Q15109; P00533: EGFR; NbExp=2; IntAct=EBI-1646426, EBI-297353;
CC Q15109; P62993: GRB2; NbExp=2; IntAct=EBI-1646426, EBI-401755;
CC Q15109; P09429: HMGB1; NbExp=3; IntAct=EBI-1646426, EBI-389432;
CC Q15109; Q8IW41: MAPKAPK5; NbExp=6; IntAct=EBI-1646426, EBI-1201460;
CC Q15109; Q8N108-16: MIER1; NbExp=3; IntAct=EBI-1646426, EBI-25830642;
CC Q15109; P16333: NCK1; NbExp=2; IntAct=EBI-1646426, EBI-389883;
CC Q15109; Q05513: PRKCZ; NbExp=6; IntAct=EBI-1646426, EBI-295351;
CC Q15109; P61586: RHOA; NbExp=2; IntAct=EBI-1646426, EBI-446668;
CC Q15109; P80511: S100A12; NbExp=2; IntAct=EBI-1646426, EBI-2823305;
CC Q15109; P04271: S100B; NbExp=5; IntAct=EBI-1646426, EBI-458391;
CC Q15109; P25815: S100P; NbExp=2; IntAct=EBI-1646426, EBI-743700;
CC Q15109; P58753: TIRAP; NbExp=9; IntAct=EBI-1646426, EBI-528644;
CC Q15109; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-1646426, EBI-10243654;
CC Q15109; P02766: TTR; NbExp=2; IntAct=EBI-1646426, EBI-711909;
CC Q15109; Q01279: Egfr; Xeno; NbExp=2; IntAct=EBI-1646426, EBI-6296235;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:24081950, ECO:0000269|PubMed:27572515}; Single-pass
CC type I membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 10]: Cell membrane
CC {ECO:0000269|PubMed:24260107}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:24260107}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1;
CC IsoId=Q15109-1; Sequence=Displayed;
CC Name=2; Synonyms=RAGESEC;
CC IsoId=Q15109-2; Sequence=VSP_002551, VSP_002552;
CC Name=3;
CC IsoId=Q15109-3; Sequence=VSP_042011;
CC Name=4;
CC IsoId=Q15109-4; Sequence=VSP_043528, VSP_042011;
CC Name=5; Synonyms=del exon3-7;
CC IsoId=Q15109-5; Sequence=VSP_047884, VSP_047885;
CC Name=6;
CC IsoId=Q15109-6; Sequence=VSP_043528;
CC Name=7; Synonyms=del exon3;
CC IsoId=Q15109-7; Sequence=VSP_002551;
CC Name=8;
CC IsoId=Q15109-8; Sequence=VSP_047886, VSP_047888;
CC Name=9; Synonyms=del exon8-9;
CC IsoId=Q15109-9; Sequence=VSP_047887, VSP_047889;
CC Name=10; Synonyms=delta-ICD, variant 20;
CC IsoId=Q15109-10; Sequence=VSP_055321;
CC -!- TISSUE SPECIFICITY: Endothelial cells.
CC -!- PTM: Phosphorylated on its cytoplasmic domain by PKCzeta/PRKCZ upon
CC ligand binding. {ECO:0000269|PubMed:21829704}.
CC -!- PTM: Targeted by the ubiquitin E3 ligase subunit FBXO10 to mediate its
CC ubiquitination and degradation. {ECO:0000269|PubMed:28515150}.
CC -!- MISCELLANEOUS: [Isoform 10]: Detected in lung, brain, heart and kidney.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/594/AGER";
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DR EMBL; M91211; AAA03574.1; -; mRNA.
DR EMBL; D28769; BAA05958.1; -; Genomic_DNA.
DR EMBL; AB036432; BAA89369.1; -; mRNA.
DR EMBL; AJ133822; CAB43108.1; -; mRNA.
DR EMBL; AB061668; BAC65465.1; -; mRNA.
DR EMBL; U89336; AAB47491.1; -; Genomic_DNA.
DR EMBL; AY755619; AAX07272.1; -; mRNA.
DR EMBL; AY755620; AAX07273.1; -; mRNA.
DR EMBL; AY755621; AAX07274.1; -; mRNA.
DR EMBL; AY755622; AAX07275.1; -; mRNA.
DR EMBL; AY755623; AAX07276.1; -; mRNA.
DR EMBL; AY755624; AAX07277.1; -; mRNA.
DR EMBL; AY755625; AAX07278.1; -; mRNA.
DR EMBL; AY755628; AAX07281.1; -; mRNA.
DR EMBL; DQ104252; AAZ32413.1; -; mRNA.
DR EMBL; EU117141; ABV03807.1; -; mRNA.
DR EMBL; KC692917; AHB30241.1; -; mRNA.
DR EMBL; AK313178; BAG35995.1; -; mRNA.
DR EMBL; AL662830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX284686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR812478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR933878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03610.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03611.1; -; Genomic_DNA.
DR EMBL; BC020669; AAH20669.1; -; mRNA.
DR EMBL; AF208289; AAG35728.1; -; Genomic_DNA.
DR CCDS; CCDS4746.1; -. [Q15109-1]
DR CCDS; CCDS4747.1; -. [Q15109-2]
DR CCDS; CCDS56417.1; -. [Q15109-4]
DR CCDS; CCDS56418.1; -. [Q15109-3]
DR CCDS; CCDS75429.1; -. [Q15109-6]
DR PIR; I61596; I61596.
DR RefSeq; NP_001127.1; NM_001136.4. [Q15109-1]
DR RefSeq; NP_001193858.1; NM_001206929.1. [Q15109-6]
DR RefSeq; NP_001193861.1; NM_001206932.1. [Q15109-7]
DR RefSeq; NP_001193863.1; NM_001206934.1. [Q15109-4]
DR RefSeq; NP_001193865.1; NM_001206936.1. [Q15109-9]
DR RefSeq; NP_001193869.1; NM_001206940.1. [Q15109-3]
DR RefSeq; NP_001193883.1; NM_001206954.1. [Q15109-8]
DR RefSeq; NP_001193895.1; NM_001206966.1. [Q15109-3]
DR RefSeq; NP_751947.1; NM_172197.2. [Q15109-2]
DR PDB; 2E5E; NMR; -; A=23-121.
DR PDB; 2ENS; NMR; -; A=235-323.
DR PDB; 2L7U; NMR; -; A=23-125.
DR PDB; 2LE9; NMR; -; A/D=235-327.
DR PDB; 2LMB; NMR; -; A=363-404.
DR PDB; 2M1K; NMR; -; A/C=23-121.
DR PDB; 2MJW; NMR; -; A/C=23-121.
DR PDB; 2MOV; NMR; -; A=23-125.
DR PDB; 3CJJ; X-ray; 1.85 A; A=23-240.
DR PDB; 3O3U; X-ray; 1.50 A; N=23-231.
DR PDB; 4LP4; X-ray; 2.40 A; A/B=23-231.
DR PDB; 4LP5; X-ray; 3.80 A; A/B=23-323.
DR PDB; 4OF5; X-ray; 2.80 A; A/B=23-237.
DR PDB; 4OFV; X-ray; 3.10 A; A/B=23-235.
DR PDB; 4OI7; X-ray; 3.10 A; A/B=23-237.
DR PDB; 4OI8; X-ray; 3.10 A; A/B=23-237.
DR PDB; 4P2Y; X-ray; 2.30 A; A=23-323.
DR PDB; 4XYN; X-ray; 2.55 A; P=54-68.
DR PDB; 4YBH; X-ray; 2.40 A; A=23-323.
DR PDB; 5D7F; X-ray; 1.30 A; P=65-79.
DR PDB; 6VXG; NMR; -; A=362-404.
DR PDB; 6XQ1; X-ray; 1.51 A; A/B=23-231.
DR PDB; 6XQ3; X-ray; 1.71 A; A/B=23-231.
DR PDB; 6XQ5; X-ray; 1.80 A; A/B=23-231.
DR PDB; 6XQ6; X-ray; 1.90 A; A/B=23-231.
DR PDB; 6XQ7; X-ray; 1.80 A; A/B=23-231.
DR PDB; 6XQ8; X-ray; 1.82 A; A/B=23-231.
DR PDB; 6XQ9; X-ray; 2.30 A; A/B=23-231.
DR PDB; 7LML; X-ray; 2.15 A; A/B=23-231.
DR PDB; 7LMW; X-ray; 2.50 A; A/B=23-231.
DR PDBsum; 2E5E; -.
DR PDBsum; 2ENS; -.
DR PDBsum; 2L7U; -.
DR PDBsum; 2LE9; -.
DR PDBsum; 2LMB; -.
DR PDBsum; 2M1K; -.
DR PDBsum; 2MJW; -.
DR PDBsum; 2MOV; -.
DR PDBsum; 3CJJ; -.
DR PDBsum; 3O3U; -.
DR PDBsum; 4LP4; -.
DR PDBsum; 4LP5; -.
DR PDBsum; 4OF5; -.
DR PDBsum; 4OFV; -.
DR PDBsum; 4OI7; -.
DR PDBsum; 4OI8; -.
DR PDBsum; 4P2Y; -.
DR PDBsum; 4XYN; -.
DR PDBsum; 4YBH; -.
DR PDBsum; 5D7F; -.
DR PDBsum; 6VXG; -.
DR PDBsum; 6XQ1; -.
DR PDBsum; 6XQ3; -.
DR PDBsum; 6XQ5; -.
DR PDBsum; 6XQ6; -.
DR PDBsum; 6XQ7; -.
DR PDBsum; 6XQ8; -.
DR PDBsum; 6XQ9; -.
DR PDBsum; 7LML; -.
DR PDBsum; 7LMW; -.
DR AlphaFoldDB; Q15109; -.
DR BMRB; Q15109; -.
DR SMR; Q15109; -.
DR BioGRID; 106685; 19.
DR DIP; DIP-40658N; -.
DR IntAct; Q15109; 30.
DR MINT; Q15109; -.
DR STRING; 9606.ENSP00000364210; -.
DR BindingDB; Q15109; -.
DR ChEMBL; CHEMBL2176846; -.
DR DrugBank; DB00107; Oxytocin.
DR GuidetoPHARMACOLOGY; 2843; -.
DR TCDB; 8.A.23.1.19; the basigin (basigin) family.
DR GlyCosmos; Q15109; 2 sites, No reported glycans.
DR GlyGen; Q15109; 2 sites.
DR iPTMnet; Q15109; -.
DR PhosphoSitePlus; Q15109; -.
DR BioMuta; AGER; -.
DR DMDM; 2497317; -.
DR jPOST; Q15109; -.
DR MassIVE; Q15109; -.
DR PaxDb; 9606-ENSP00000364210; -.
DR PeptideAtlas; Q15109; -.
DR ProteomicsDB; 60436; -. [Q15109-1]
DR ProteomicsDB; 60437; -. [Q15109-2]
DR ProteomicsDB; 60438; -. [Q15109-3]
DR ProteomicsDB; 60439; -. [Q15109-4]
DR ProteomicsDB; 61748; -.
DR Antibodypedia; 28483; 945 antibodies from 45 providers.
DR DNASU; 177; -.
DR Ensembl; ENST00000375055.6; ENSP00000364195.2; ENSG00000204305.16. [Q15109-3]
DR Ensembl; ENST00000375067.7; ENSP00000364208.3; ENSG00000204305.16. [Q15109-2]
DR Ensembl; ENST00000375069.7; ENSP00000364210.4; ENSG00000204305.16. [Q15109-6]
DR Ensembl; ENST00000375076.9; ENSP00000364217.4; ENSG00000204305.16. [Q15109-1]
DR Ensembl; ENST00000383275.6; ENSP00000372762.2; ENSG00000206320.12. [Q15109-3]
DR Ensembl; ENST00000383279.8; ENSP00000372766.4; ENSG00000206320.12. [Q15109-2]
DR Ensembl; ENST00000412470.6; ENSP00000387853.2; ENSG00000229058.10. [Q15109-2]
DR Ensembl; ENST00000426138.6; ENSP00000415144.2; ENSG00000230514.11.
DR Ensembl; ENST00000427822.6; ENSP00000416042.2; ENSG00000231268.9.
DR Ensembl; ENST00000432831.5; ENSP00000413391.1; ENSG00000237405.10. [Q15109-3]
DR Ensembl; ENST00000436456.6; ENSP00000397227.2; ENSG00000234729.9. [Q15109-1]
DR Ensembl; ENST00000438221.6; ENSP00000387887.2; ENSG00000204305.16. [Q15109-4]
DR Ensembl; ENST00000441180.6; ENSP00000388462.2; ENSG00000234729.9. [Q15109-2]
DR Ensembl; ENST00000441804.6; ENSP00000391743.2; ENSG00000237405.10. [Q15109-2]
DR Ensembl; ENST00000447921.6; ENSP00000395812.2; ENSG00000237405.10. [Q15109-1]
DR Ensembl; ENST00000449037.5; ENSP00000400667.1; ENSG00000229058.10. [Q15109-3]
DR Ensembl; ENST00000451115.6; ENSP00000401068.2; ENSG00000206320.12. [Q15109-1]
DR Ensembl; ENST00000453588.5; ENSP00000399686.1; ENSG00000234729.9. [Q15109-3]
DR Ensembl; ENST00000456918.6; ENSP00000409457.2; ENSG00000229058.10. [Q15109-1]
DR Ensembl; ENST00000547328.5; ENSP00000448579.2; ENSG00000206320.12. [Q15109-6]
DR Ensembl; ENST00000547651.2; ENSP00000449708.1; ENSG00000229058.10. [Q15109-4]
DR Ensembl; ENST00000548464.3; ENSP00000450134.2; ENSG00000234729.9. [Q15109-6]
DR Ensembl; ENST00000549758.5; ENSP00000447301.2; ENSG00000229058.10. [Q15109-6]
DR Ensembl; ENST00000550562.5; ENSP00000446835.1; ENSG00000234729.9. [Q15109-4]
DR Ensembl; ENST00000551254.5; ENSP00000449226.1; ENSG00000206320.12. [Q15109-4]
DR Ensembl; ENST00000551381.5; ENSP00000448979.2; ENSG00000237405.10. [Q15109-6]
DR Ensembl; ENST00000551827.4; ENSP00000449042.1; ENSG00000237405.10. [Q15109-4]
DR GeneID; 177; -.
DR KEGG; hsa:177; -.
DR MANE-Select; ENST00000375076.9; ENSP00000364217.4; NM_001136.5; NP_001127.1.
DR UCSC; uc003oal.3; human. [Q15109-1]
DR AGR; HGNC:320; -.
DR CTD; 177; -.
DR DisGeNET; 177; -.
DR GeneCards; AGER; -.
DR HGNC; HGNC:320; AGER.
DR HPA; ENSG00000204305; Tissue enriched (lung).
DR MIM; 600214; gene.
DR neXtProt; NX_Q15109; -.
DR OpenTargets; ENSG00000204305; -.
DR PharmGKB; PA24617; -.
DR VEuPathDB; HostDB:ENSG00000204305; -.
DR eggNOG; ENOG502SQ8N; Eukaryota.
DR GeneTree; ENSGT00890000139566; -.
DR HOGENOM; CLU_051851_0_1_1; -.
DR InParanoid; Q15109; -.
DR OMA; VAMHPSH; -.
DR OrthoDB; 4637563at2759; -.
DR PhylomeDB; Q15109; -.
DR TreeFam; TF337155; -.
DR PathwayCommons; Q15109; -.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
DR Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
DR SignaLink; Q15109; -.
DR SIGNOR; Q15109; -.
DR BioGRID-ORCS; 177; 12 hits in 1153 CRISPR screens.
DR ChiTaRS; AGER; human.
DR EvolutionaryTrace; Q15109; -.
DR GeneWiki; RAGE_(receptor); -.
DR GenomeRNAi; 177; -.
DR Pharos; Q15109; Tchem.
DR PRO; PR:Q15109; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q15109; Protein.
DR Bgee; ENSG00000204305; Expressed in right lung and 95 other cell types or tissues.
DR ExpressionAtlas; Q15109; baseline and differential.
DR Genevisible; Q15109; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0009986; C:cell surface; NAS:ARUK-UCL.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL.
DR GO; GO:0050785; F:advanced glycation end-product receptor activity; NAS:ARUK-UCL.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005055; F:laminin receptor activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL.
DR GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; TAS:ARUK-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IMP:ARUK-UCL.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0048143; P:astrocyte activation; IGI:ARUK-UCL.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISS:ARUK-UCL.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IDA:CAFA.
DR GO; GO:0050930; P:induction of positive chemotaxis; IEA:Ensembl.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL.
DR GO; GO:0001774; P:microglial cell activation; IGI:ARUK-UCL.
DR GO; GO:1903523; P:negative regulation of blood circulation; ISS:ARUK-UCL.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IDA:UniProtKB.
DR GO; GO:1900453; P:negative regulation of long-term synaptic depression; IGI:ARUK-UCL.
DR GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
DR GO; GO:0031175; P:neuron projection development; IGI:UniProtKB.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IMP:UniProtKB.
DR GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IGI:ARUK-UCL.
DR GO; GO:0032722; P:positive regulation of chemokine production; ISS:ARUK-UCL.
DR GO; GO:2001200; P:positive regulation of dendritic cell differentiation; IMP:UniProtKB.
DR GO; GO:1904472; P:positive regulation of endothelin production; ISS:ARUK-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:ARUK-UCL.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IGI:ARUK-UCL.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:ARUK-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:ARUK-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IGI:ARUK-UCL.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
DR GO; GO:2000439; P:positive regulation of monocyte extravasation; IMP:ARUK-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IGI:ARUK-UCL.
DR GO; GO:1900745; P:positive regulation of p38MAPK cascade; IGI:ARUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:ARUK-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:ARUK-UCL.
DR GO; GO:0072657; P:protein localization to membrane; IEA:Ensembl.
DR GO; GO:2000514; P:regulation of CD4-positive, alpha-beta T cell activation; IDA:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; ISS:ARUK-UCL.
DR GO; GO:1901222; P:regulation of non-canonical NF-kappaB signal transduction; NAS:ARUK-UCL.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; ISS:ARUK-UCL.
DR GO; GO:0150003; P:regulation of spontaneous synaptic transmission; IGI:ARUK-UCL.
DR GO; GO:0048167; P:regulation of synaptic plasticity; TAS:ARUK-UCL.
DR GO; GO:0001914; P:regulation of T cell mediated cytotoxicity; IDA:UniProtKB.
DR GO; GO:1904645; P:response to amyloid-beta; ISS:ARUK-UCL.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; TAS:ProtInc.
DR GO; GO:0045056; P:transcytosis; ISS:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; IDA:ARUK-UCL.
DR CDD; cd00096; Ig; 2.
DR DisProt; DP02555; -.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR11973:SF20; ADVANCED GLYCOSYLATION END PRODUCT-SPECIFIC RECEPTOR; 1.
DR PANTHER; PTHR11973; CELL SURFACE GLYCOPROTEIN MUC18-RELATED; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 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; Ubl conjugation.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..404
FT /note="Advanced glycosylation end product-specific
FT receptor"
FT /id="PRO_0000014923"
FT TOPO_DOM 23..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..116
FT /note="Ig-like V-type"
FT DOMAIN 124..221
FT /note="Ig-like C2-type 1"
FT DOMAIN 227..317
FT /note="Ig-like C2-type 2"
FT REGION 367..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 391
FT /note="Phosphoserine; by PKC/PRKCZ"
FT /evidence="ECO:0000269|PubMed:21829704"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..99
FT /evidence="ECO:0000269|PubMed:20943659,
FT ECO:0000269|PubMed:20947022, ECO:0000269|PubMed:21565706,
FT ECO:0000269|Ref.22"
FT DISULFID 144..208
FT /evidence="ECO:0000269|PubMed:20943659,
FT ECO:0000269|PubMed:20947022, ECO:0000269|PubMed:21565706,
FT ECO:0000269|Ref.22"
FT DISULFID 259
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:23284645"
FT DISULFID 301
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:23284645"
FT VAR_SEQ 54..67
FT /note="Missing (in isoform 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:18089847, ECO:0000303|Ref.4"
FT /id="VSP_002551"
FT VAR_SEQ 113..121
FT /note="YRVRVYQIP -> WWWSQKVEQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:18089847"
FT /id="VSP_047884"
FT VAR_SEQ 122..404
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:18089847"
FT /id="VSP_047885"
FT VAR_SEQ 140
FT /note="K -> KVVEESRRSRKRPCEQE (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:18089847"
FT /id="VSP_043528"
FT VAR_SEQ 275..404
FT /note="GVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEE
FT GPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEER
FT AELNQSEEPEAGESSTGGP -> VSDLERGAGRTRRGGANCRLCGRIRAGNSSPGPGDP
FT GRPGDSRPAHWGHLVAKAATPRRGEEGPRKPGGRGGACRTESVGGT (in isoform
FT 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_002552"
FT VAR_SEQ 275..325
FT /note="GVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGE
FT -> NQARRGQLQVRGLIKSGKQKIAPNTCDWGDGQQERNGRPQKTRRKRRSVQN (in
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:18089847"
FT /id="VSP_047886"
FT VAR_SEQ 276..355
FT /note="VPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEG
FT PTAGSVGGSGLGTLALALGILGGLGTAA -> LRTREPTAVWPPIPATGPRKAVLSASA
FT SSNQARRGQLQVRGLIKSGKQKIAPNTCDWGDGQQERNGRPQKTRRKRRSVQN (in
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:18089847"
FT /id="VSP_047887"
FT VAR_SEQ 326..404
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:18089847"
FT /id="VSP_047888"
FT VAR_SEQ 332..404
FT /note="SVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEE
FT ERAELNQSEEPEAGESSTGGP -> EGFDKVREAEDSPQHM (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:12495433,
FT ECO:0000303|PubMed:18089847"
FT /id="VSP_042011"
FT VAR_SEQ 356..404
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:18089847"
FT /id="VSP_047889"
FT VAR_SEQ 374..404
FT /note="KAPENQEEEEERAELNQSEEPEAGESSTGGP -> PQKTRRKRRSVQN (in
FT isoform 10)"
FT /evidence="ECO:0000303|PubMed:24260107"
FT /id="VSP_055321"
FT VARIANT 82
FT /note="G -> S (in dbSNP:rs2070600)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_024500"
FT VARIANT 100
FT /note="Q -> R"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_011338"
FT MUTAGEN 374
FT /note="K->R: Less monoubiquitinated product and resistant
FT to degradation."
FT /evidence="ECO:0000269|PubMed:28515150"
FT MUTAGEN 391
FT /note="S->A: Complete loss of phosphorylation by
FT PKC/PRKCZ."
FT /evidence="ECO:0000269|PubMed:21829704"
FT CONFLICT 1
FT /note="M -> G (in Ref. 1; AAA03574)"
FT /evidence="ECO:0000305"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6XQ1"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3O3U"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:2E5E"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:3O3U"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3O3U"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:4OF5"
FT STRAND 108..119
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 139..151
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6XQ1"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:6XQ9"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:3O3U"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:3O3U"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3CJJ"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6XQ1"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:4P2Y"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4P2Y"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:4P2Y"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:4P2Y"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2LE9"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:4P2Y"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:4P2Y"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:4P2Y"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:4P2Y"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:4P2Y"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:4P2Y"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:2LE9"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:2LMB"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:2LMB"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:6VXG"
SQ SEQUENCE 404 AA; 42803 MW; 0D584C436C30CCE7 CRC64;
MAAGTAVGAW VLVLSLWGAV VGAQNITARI GEPLVLKCKG APKKPPQRLE WKLNTGRTEA
WKVLSPQGGG PWDSVARVLP NGSLFLPAVG IQDEGIFRCQ AMNRNGKETK SNYRVRVYQI
PGKPEIVDSA SELTAGVPNK VGTCVSEGSY PAGTLSWHLD GKPLVPNEKG VSVKEQTRRH
PETGLFTLQS ELMVTPARGG DPRPTFSCSF SPGLPRHRAL RTAPIQPRVW EPVPLEEVQL
VVEPEGGAVA PGGTVTLTCE VPAQPSPQIH WMKDGVPLPL PPSPVLILPE IGPQDQGTYS
CVATHSSHGP QESRAVSISI IEPGEEGPTA GSVGGSGLGT LALALGILGG LGTAALLIGV
ILWQRRQRRG EERKAPENQE EEEERAELNQ SEEPEAGESS TGGP
//
