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

 RAGE_HUMAN              Reviewed;         404 AA.
Q15109; A2BFI7; A6NKF0; A7Y2U9; B0V176; Q15279; Q3L1R4; Q3L1R5;
Q3L1R6; Q3L1R7; Q3L1R8; Q3L1S0; Q86SN1; Q9H2X7; Q9Y3R3; V5R6A3;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
22-NOV-2017, entry version 187.
RecName: Full=Advanced glycosylation end product-specific receptor;
AltName: Full=Receptor for advanced glycosylation end products;
Flags: Precursor;
Name=AGER; Synonyms=RAGE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=1378843;
Neeper M., Schmidt A.M., Brett J., Yan S.D., Wang F., Pan Y.C.,
Elliston K., Stern D., Shaw A.;
"Cloning and expression of a cell surface receptor for advanced
glycosylation end products of proteins.";
J. Biol. Chem. 267:14998-15004(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=7835890; DOI=10.1006/geno.1994.1517;
Sugaya K., Fukagawa T., Matsumoto K., Mita K., Takahashi E., Ando A.,
Inoko H., Ikemura T.;
"Three genes in the human MHC class III region near the junction with
the class II: gene for receptor of advanced glycosylation end
products, PBX2 homeobox gene and a notch homolog, human counterpart of
mouse mammary tumor gene int-3.";
Genomics 23:408-419(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-100.
Abedin M.J., Yonekura H., Migita H., Karasawa J., Yamamoto Y.,
Yamamoto H.;
"Molecular heterogeneity of the receptor for advanced glycation
endproducts.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Malherbe P., Richards J., Gaillard H., Thompson A., Diener C.,
Schuler A., Huber G.;
"cDNA cloning of a novel secreted isoform of the human receptor for
advanced glycation end products (RAGE) and characterization of cells
co-expressing cell-surface scavenger receptors and Swedish mutant
amyloid precursor protein.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
TISSUE=Skin;
PubMed=12495433; DOI=10.1042/BJ20021371;
Yonekura H., Yamamoto Y., Sakurai S., Petrova R.G., Abedin J., Li H.,
Yasui K., Takeuchi M., Makita Z., Takasawa S., Okamoto H.,
Watanabe T., Yamamoto H.;
"Novel splice variants of the receptor for advanced glycation end-
products expressed in human vascular endothelial cells and pericytes,
and their putative roles in diabetes-induced vascular injury.";
Biochem. J. 370:1097-1109(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5; 6; 7; 8 AND 9), AND
ALTERNATIVE SPLICING.
TISSUE=Aortic smooth muscle, and Lung;
PubMed=18089847; DOI=10.1096/fj.07-9909com;
Hudson B.I., Carter A.M., Harja E., Kalea A.Z., Arriero M., Yang H.,
Grant P.J., Schmidt A.M.;
"Identification, classification, and expression of RAGE gene splice
variants.";
FASEB J. 22:1572-1580(2008).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), AND SUBCELLULAR LOCATION
(ISOFORM 10).
TISSUE=Lung;
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-82.
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
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).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
PubMed=11375354; DOI=10.2337/diabetes.50.6.1505;
Hudson B.I., Stickland M.H., Futers T.S., Grant P.J.;
"Effects of novel polymorphisms in the RAGE gene on transcriptional
regulation and their association with diabetic retinopathy.";
Diabetes 50:1505-1511(2001).
[14]
INTERACTION WITH S100A12.
PubMed=19386136; DOI=10.1186/1471-2091-10-11;
Moroz O.V., Burkitt W., Wittkowski H., He W., Ianoul A.,
Novitskaya V., Xie J., Polyakova O., Lednev I.K., Shekhtman A.,
Derrick P.J., Bjoerk P., Foell D., Bronstein I.B.;
"Both Ca2+ and Zn2+ are essential for S100A12 protein oligomerization
and function.";
BMC Biochem. 10:11-11(2009).
[15]
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).
[16]
INTERACTION WITH S100A14, AND FUNCTION.
PubMed=21559403; DOI=10.1371/journal.pone.0019375;
Jin Q., Chen H., Luo A., Ding F., Liu Z.;
"S100A14 stimulates cell proliferation and induces cell apoptosis at
different concentrations via receptor for advanced glycation end
products (RAGE).";
PLoS ONE 6:E19375-E19375(2011).
[17]
SUBUNIT, AND INTERCHAIN DISULFIDE BONDS.
PubMed=23284645; DOI=10.1371/journal.pone.0050736;
Wei W., Lampe L., Park S., Vangara B.S., Waldo G.S., Cabantous S.,
Subaran S.S., Yang D., Lakatta E.G., Lin L.;
"Disulfide bonds within the C2 domain of RAGE play key roles in its
dimerization and biogenesis.";
PLoS ONE 7:E50736-E50736(2012).
[18]
STRUCTURE BY NMR OF 23-121, STRUCTURE BY NMR OF 235-323, AND DISULFIDE
BONDS.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the third Ig-like domain from human advanced
glycosylation end product-specific receptor.";
Submitted (APR-2008) to the PDB data bank.
[19]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 23-231, FUNCTION,
DNA-BINDING, INTERACTION WITH S100B, AND DISULFIDE BOND.
PubMed=20943659; DOI=10.1074/jbc.M110.169276;
Park H., Adsit F.G., Boyington J.C.;
"The 1.5 A crystal structure of human receptor for advanced glycation
endproducts (RAGE) ectodomains reveals unique features determining
ligand binding.";
J. Biol. Chem. 285:40762-40770(2010).
[20]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 23-240, INTERACTION WITH
S100B, AND DISULFIDE BONDS.
PubMed=20947022; DOI=10.1016/j.str.2010.05.017;
Koch M., Chitayat S., Dattilo B.M., Schiefner A., Diez J.,
Chazin W.J., Fritz G.;
"Structural basis for ligand recognition and activation of RAGE.";
Structure 18:1342-1352(2010).
[21]
STRUCTURE BY NMR OF 23-125, FUNCTION, AND DISULFIDE BONDS.
PubMed=21565706; DOI=10.1016/j.str.2011.02.013;
Xue J., Rai V., Singer D., Chabierski S., Xie J., Reverdatto S.,
Burz D.S., Schmidt A.M., Hoffmann R., Shekhtman A.;
"Advanced glycation end product recognition by the receptor for
AGEs.";
Structure 19:722-732(2011).
-!- 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 (By
similarity). Receptor for amyloid beta peptide. Contributes to the
translocation of amyloid-beta peptide (ABPP) across the cell
membrane from the extracellular to the intracellular space in
cortical neurons. ABPP-initiated RAGE signaling, especially
stimulation of p38 mitogen-activated protein kinase (MAPK), has
the capacity to drive a transport system delivering ABPP as a
complex with RAGE to the intraneuronal space. Can also bind
oligonucleotides. {ECO:0000250, ECO:0000269|PubMed:19906677,
ECO:0000269|PubMed:20943659, ECO:0000269|PubMed:21559403,
ECO:0000269|PubMed:21565706}.
-!- SUBUNIT: Interacts with S100A1 and APP (By similarity). Interacts
with S100B, S100A12 and S100A14. Constitutive homodimer;
disulfide-linked. {ECO:0000250, ECO:0000269|PubMed:19386136,
ECO:0000269|PubMed:20943659, ECO:0000269|PubMed:20947022,
ECO:0000269|PubMed:21559403, ECO:0000269|PubMed:21565706,
ECO:0000269|PubMed:23284645}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1646426, EBI-1646426;
O43889-2:CREB3; NbExp=3; IntAct=EBI-1646426, EBI-625022;
O60610:DIAPH1; NbExp=3; IntAct=EBI-1646426, EBI-3959709;
P00533:EGFR; NbExp=2; IntAct=EBI-1646426, EBI-297353;
Q01279:Egfr (xeno); NbExp=2; IntAct=EBI-1646426, EBI-6296235;
P62993:GRB2; NbExp=2; IntAct=EBI-1646426, EBI-401755;
P09429:HMGB1; NbExp=3; IntAct=EBI-1646426, EBI-389432;
P16333:NCK1; NbExp=2; IntAct=EBI-1646426, EBI-389883;
P61586:RHOA; NbExp=2; IntAct=EBI-1646426, EBI-446668;
P04271:S100B; NbExp=5; IntAct=EBI-1646426, EBI-458391;
P25815:S100P; NbExp=2; IntAct=EBI-1646426, EBI-743700;
P02766:TTR; NbExp=2; IntAct=EBI-1646426, EBI-711909;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 10: Cell membrane
{ECO:0000269|PubMed:24260107}; Single-pass type I membrane protein
{ECO:0000269|PubMed:24260107}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=10;
Name=1;
IsoId=Q15109-1; Sequence=Displayed;
Name=2; Synonyms=RAGESEC;
IsoId=Q15109-2; Sequence=VSP_002551, VSP_002552;
Name=3;
IsoId=Q15109-3; Sequence=VSP_042011;
Name=4;
IsoId=Q15109-4; Sequence=VSP_043528, VSP_042011;
Name=5; Synonyms=del exon3-7;
IsoId=Q15109-5; Sequence=VSP_047884, VSP_047885;
Name=6;
IsoId=Q15109-6; Sequence=VSP_043528;
Name=7; Synonyms=del exon3;
IsoId=Q15109-7; Sequence=VSP_002551;
Name=8;
IsoId=Q15109-8; Sequence=VSP_047886, VSP_047888;
Name=9; Synonyms=del exon8-9;
IsoId=Q15109-9; Sequence=VSP_047887, VSP_047889;
Name=10; Synonyms=delta-ICD, variant 20;
IsoId=Q15109-10; Sequence=VSP_055321;
Note=Detected in lung, brain, heart and kidney.;
-!- TISSUE SPECIFICITY: Endothelial cells.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AGERID594ch6p21.html";
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EMBL; M91211; AAA03574.1; -; mRNA.
EMBL; D28769; BAA05958.1; -; Genomic_DNA.
EMBL; AB036432; BAA89369.1; -; mRNA.
EMBL; AJ133822; CAB43108.1; -; mRNA.
EMBL; AB061668; BAC65465.1; -; mRNA.
EMBL; U89336; AAB47491.1; -; Genomic_DNA.
EMBL; AY755619; AAX07272.1; -; mRNA.
EMBL; AY755620; AAX07273.1; -; mRNA.
EMBL; AY755621; AAX07274.1; -; mRNA.
EMBL; AY755622; AAX07275.1; -; mRNA.
EMBL; AY755623; AAX07276.1; -; mRNA.
EMBL; AY755624; AAX07277.1; -; mRNA.
EMBL; AY755625; AAX07278.1; -; mRNA.
EMBL; AY755628; AAX07281.1; -; mRNA.
EMBL; DQ104252; AAZ32413.1; -; mRNA.
EMBL; EU117141; ABV03807.1; -; mRNA.
EMBL; KC692917; AHB30241.1; -; mRNA.
EMBL; AK313178; BAG35995.1; -; mRNA.
EMBL; AL662830; CAI17535.1; -; Genomic_DNA.
EMBL; AL662830; CAI17536.1; -; Genomic_DNA.
EMBL; AL662830; CAM24893.1; -; Genomic_DNA.
EMBL; AL662884; CAI18354.1; -; Genomic_DNA.
EMBL; AL662884; CAI18355.1; -; Genomic_DNA.
EMBL; AL662884; CAM25647.1; -; Genomic_DNA.
EMBL; AL845464; CAI41809.1; -; Genomic_DNA.
EMBL; AL845464; CAI41810.1; -; Genomic_DNA.
EMBL; AL845464; CAM25716.1; -; Genomic_DNA.
EMBL; BX284686; CAM26223.1; -; Genomic_DNA.
EMBL; BX284686; CAM26225.1; -; Genomic_DNA.
EMBL; BX927239; CAQ06596.1; -; Genomic_DNA.
EMBL; BX927239; CAQ06597.1; -; Genomic_DNA.
EMBL; CR933878; CAQ09624.1; -; Genomic_DNA.
EMBL; CR812478; CAQ10699.1; -; Genomic_DNA.
EMBL; CH471081; EAX03610.1; -; Genomic_DNA.
EMBL; CH471081; EAX03611.1; -; Genomic_DNA.
EMBL; BC020669; AAH20669.1; -; mRNA.
EMBL; AF208289; AAG35728.1; -; Genomic_DNA.
CCDS; CCDS4746.1; -. [Q15109-1]
CCDS; CCDS4747.1; -. [Q15109-2]
CCDS; CCDS56417.1; -. [Q15109-4]
CCDS; CCDS56418.1; -. [Q15109-3]
CCDS; CCDS75429.1; -. [Q15109-6]
PIR; I61596; I61596.
RefSeq; NP_001127.1; NM_001136.4. [Q15109-1]
RefSeq; NP_001193858.1; NM_001206929.1. [Q15109-6]
RefSeq; NP_001193861.1; NM_001206932.1. [Q15109-7]
RefSeq; NP_001193863.1; NM_001206934.1. [Q15109-4]
RefSeq; NP_001193865.1; NM_001206936.1. [Q15109-9]
RefSeq; NP_001193869.1; NM_001206940.1. [Q15109-3]
RefSeq; NP_001193883.1; NM_001206954.1. [Q15109-8]
RefSeq; NP_001193895.1; NM_001206966.1. [Q15109-3]
RefSeq; NP_751947.1; NM_172197.2. [Q15109-2]
UniGene; Hs.534342; -.
PDB; 1PWI; Model; -; A=1-404.
PDB; 2BJP; Model; -; A=1-404.
PDB; 2E5E; NMR; -; A=23-121.
PDB; 2ENS; NMR; -; A=235-323.
PDB; 2L7U; NMR; -; A=23-125.
PDB; 2LE9; NMR; -; A/D=235-327.
PDB; 2LMB; NMR; -; A=363-404.
PDB; 2M1K; NMR; -; A/C=23-121.
PDB; 2MJW; NMR; -; A/C=23-121.
PDB; 2MOV; NMR; -; A=23-125.
PDB; 3CJJ; X-ray; 1.85 A; A=23-240.
PDB; 3O3U; X-ray; 1.50 A; N=23-231.
PDB; 4LP4; X-ray; 2.40 A; A/B=23-231.
PDB; 4LP5; X-ray; 3.80 A; A/B=23-323.
PDB; 4OF5; X-ray; 2.80 A; A/B=23-237.
PDB; 4OFV; X-ray; 3.10 A; A/B=23-235.
PDB; 4OI7; X-ray; 3.10 A; A/B=23-237.
PDB; 4OI8; X-ray; 3.10 A; A/B=23-237.
PDB; 4P2Y; X-ray; 2.30 A; A=23-323.
PDB; 4XYN; X-ray; 2.55 A; P=54-68.
PDB; 4YBH; X-ray; 2.40 A; A=23-323.
PDB; 5D7F; X-ray; 1.30 A; P=65-79.
PDBsum; 1PWI; -.
PDBsum; 2BJP; -.
PDBsum; 2E5E; -.
PDBsum; 2ENS; -.
PDBsum; 2L7U; -.
PDBsum; 2LE9; -.
PDBsum; 2LMB; -.
PDBsum; 2M1K; -.
PDBsum; 2MJW; -.
PDBsum; 2MOV; -.
PDBsum; 3CJJ; -.
PDBsum; 3O3U; -.
PDBsum; 4LP4; -.
PDBsum; 4LP5; -.
PDBsum; 4OF5; -.
PDBsum; 4OFV; -.
PDBsum; 4OI7; -.
PDBsum; 4OI8; -.
PDBsum; 4P2Y; -.
PDBsum; 4XYN; -.
PDBsum; 4YBH; -.
PDBsum; 5D7F; -.
ProteinModelPortal; Q15109; -.
SMR; Q15109; -.
BioGrid; 106685; 6.
DIP; DIP-40658N; -.
IntAct; Q15109; 13.
MINT; MINT-2635420; -.
STRING; 9606.ENSP00000364217; -.
BindingDB; Q15109; -.
ChEMBL; CHEMBL2176846; -.
GuidetoPHARMACOLOGY; 2843; -.
iPTMnet; Q15109; -.
PhosphoSitePlus; Q15109; -.
BioMuta; AGER; -.
DMDM; 2497317; -.
PaxDb; Q15109; -.
PeptideAtlas; Q15109; -.
PRIDE; Q15109; -.
DNASU; 177; -.
Ensembl; ENST00000375055; ENSP00000364195; ENSG00000204305. [Q15109-3]
Ensembl; ENST00000375067; ENSP00000364208; ENSG00000204305. [Q15109-2]
Ensembl; ENST00000375069; ENSP00000364210; ENSG00000204305. [Q15109-6]
Ensembl; ENST00000375076; ENSP00000364217; ENSG00000204305. [Q15109-1]
Ensembl; ENST00000383275; ENSP00000372762; ENSG00000206320. [Q15109-3]
Ensembl; ENST00000383279; ENSP00000372766; ENSG00000206320. [Q15109-2]
Ensembl; ENST00000412470; ENSP00000387853; ENSG00000229058. [Q15109-2]
Ensembl; ENST00000426138; ENSP00000415144; ENSG00000230514.
Ensembl; ENST00000427822; ENSP00000416042; ENSG00000231268.
Ensembl; ENST00000432831; ENSP00000413391; ENSG00000237405. [Q15109-3]
Ensembl; ENST00000436456; ENSP00000397227; ENSG00000234729. [Q15109-1]
Ensembl; ENST00000438221; ENSP00000387887; ENSG00000204305. [Q15109-4]
Ensembl; ENST00000441180; ENSP00000388462; ENSG00000234729. [Q15109-2]
Ensembl; ENST00000441804; ENSP00000391743; ENSG00000237405. [Q15109-2]
Ensembl; ENST00000447921; ENSP00000395812; ENSG00000237405. [Q15109-1]
Ensembl; ENST00000449037; ENSP00000400667; ENSG00000229058. [Q15109-3]
Ensembl; ENST00000451115; ENSP00000401068; ENSG00000206320. [Q15109-1]
Ensembl; ENST00000453588; ENSP00000399686; ENSG00000234729. [Q15109-3]
Ensembl; ENST00000456918; ENSP00000409457; ENSG00000229058. [Q15109-1]
Ensembl; ENST00000547328; ENSP00000448579; ENSG00000206320. [Q15109-6]
Ensembl; ENST00000547651; ENSP00000449708; ENSG00000229058. [Q15109-4]
Ensembl; ENST00000548464; ENSP00000450134; ENSG00000234729. [Q15109-6]
Ensembl; ENST00000549758; ENSP00000447301; ENSG00000229058. [Q15109-6]
Ensembl; ENST00000550562; ENSP00000446835; ENSG00000234729. [Q15109-4]
Ensembl; ENST00000551254; ENSP00000449226; ENSG00000206320. [Q15109-4]
Ensembl; ENST00000551381; ENSP00000448979; ENSG00000237405. [Q15109-6]
Ensembl; ENST00000551827; ENSP00000449042; ENSG00000237405. [Q15109-4]
GeneID; 177; -.
KEGG; hsa:177; -.
UCSC; uc003oal.3; human. [Q15109-1]
CTD; 177; -.
DisGeNET; 177; -.
EuPathDB; HostDB:ENSG00000204305.13; -.
GeneCards; AGER; -.
HGNC; HGNC:320; AGER.
HPA; CAB011682; -.
HPA; HPA064436; -.
MIM; 600214; gene.
neXtProt; NX_Q15109; -.
OpenTargets; ENSG00000204305; -.
PharmGKB; PA24617; -.
eggNOG; ENOG410IVT2; Eukaryota.
eggNOG; ENOG4111C4I; LUCA.
GeneTree; ENSGT00890000139566; -.
HOGENOM; HOG000232122; -.
HOVERGEN; HBG004350; -.
InParanoid; Q15109; -.
KO; K19722; -.
OMA; PNKVGTC; -.
OrthoDB; EOG091G0BCY; -.
PhylomeDB; Q15109; -.
TreeFam; TF337155; -.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
SIGNOR; Q15109; -.
ChiTaRS; AGER; human.
EvolutionaryTrace; Q15109; -.
GeneWiki; RAGE_(receptor); -.
GenomeRNAi; 177; -.
PRO; PR:Q15109; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204305; -.
CleanEx; HS_AGER; -.
CleanEx; HS_RAGE; -.
ExpressionAtlas; Q15109; baseline and differential.
Genevisible; Q15109; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0009986; C:cell surface; NAS:ARUK-UCL.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL.
GO; GO:1904599; F:advanced glycation end-product binding; IEA:Ensembl.
GO; GO:0050785; F:advanced glycation end-product receptor activity; NAS:ARUK-UCL.
GO; GO:0001540; F:amyloid-beta binding; TAS:ARUK-UCL.
GO; GO:0008201; F:heparin binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
GO; GO:0005044; F:scavenger receptor activity; TAS:ARUK-UCL.
GO; GO:0038023; F:signaling receptor activity; IMP:ARUK-UCL.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0010255; P:glucose mediated signaling pathway; IDA:CAFA.
GO; GO:0050930; P:induction of positive chemotaxis; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; TAS:Reactome.
GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL.
GO; GO:0090647; P:modulation of age-related behavioral decline; IGI:ARUK-UCL.
GO; GO:1904604; P:negative regulation of advanced glycation end-product receptor activity; IEA:Ensembl.
GO; GO:1904597; P:negative regulation of connective tissue replacement involved in inflammatory response wound healing; IEA:Ensembl.
GO; GO:0032693; P:negative regulation of interleukin-10 production; IDA:UniProtKB.
GO; GO:1900453; P:negative regulation of long term synaptic depression; IGI:ARUK-UCL.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IGI:ARUK-UCL.
GO; GO:0031175; P:neuron projection development; IGI:UniProtKB.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IMP:UniProtKB.
GO; GO:0061890; P:positive regulation of astrocyte activation; IGI:ARUK-UCL.
GO; GO:2001200; P:positive regulation of dendritic cell differentiation; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:ARUK-UCL.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IGI:ARUK-UCL.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IEA:Ensembl.
GO; GO:1903980; P:positive regulation of microglial cell activation; IGI:ARUK-UCL.
GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IGI:ARUK-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IGI:ARUK-UCL.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; IGI:ARUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:ARUK-UCL.
GO; GO:0072657; P:protein localization to membrane; IEA:Ensembl.
GO; GO:2000514; P:regulation of CD4-positive, alpha-beta T cell activation; IDA:UniProtKB.
GO; GO:0051101; P:regulation of DNA binding; IEA:Ensembl.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; NAS:ARUK-UCL.
GO; GO:1900744; P:regulation of p38MAPK cascade; ISS:ARUK-UCL.
GO; GO:0048167; P:regulation of synaptic plasticity; TAS:ARUK-UCL.
GO; GO:0001914; P:regulation of T cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:1904645; P:response to amyloid-beta; ISS:ARUK-UCL.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0009611; P:response to wounding; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 4.
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; Polymorphism;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 404 Advanced glycosylation end product-
specific receptor.
/FTId=PRO_0000014923.
TOPO_DOM 23 342 Extracellular. {ECO:0000255}.
TRANSMEM 343 363 Helical. {ECO:0000255}.
TOPO_DOM 364 404 Cytoplasmic. {ECO:0000255}.
DOMAIN 23 116 Ig-like V-type.
DOMAIN 124 221 Ig-like C2-type 1.
DOMAIN 227 317 Ig-like C2-type 2.
COMPBIAS 380 384 Poly-Glu.
MOD_RES 391 391 Phosphoserine.
{ECO:0000250|UniProtKB:Q63495}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 38 99 {ECO:0000269|PubMed:20943659,
ECO:0000269|PubMed:20947022,
ECO:0000269|PubMed:21565706,
ECO:0000269|Ref.18}.
DISULFID 144 208 {ECO:0000269|PubMed:20943659,
ECO:0000269|PubMed:20947022,
ECO:0000269|PubMed:21565706,
ECO:0000269|Ref.18}.
DISULFID 259 259 Interchain.
{ECO:0000269|PubMed:23284645}.
DISULFID 301 301 Interchain.
{ECO:0000269|PubMed:23284645}.
VAR_SEQ 54 67 Missing (in isoform 2 and isoform 7).
{ECO:0000303|PubMed:18089847,
ECO:0000303|Ref.4}.
/FTId=VSP_002551.
VAR_SEQ 113 121 YRVRVYQIP -> WWWSQKVEQ (in isoform 5).
{ECO:0000303|PubMed:18089847}.
/FTId=VSP_047884.
VAR_SEQ 122 404 Missing (in isoform 5).
{ECO:0000303|PubMed:18089847}.
/FTId=VSP_047885.
VAR_SEQ 140 140 K -> KVVEESRRSRKRPCEQE (in isoform 4 and
isoform 6).
{ECO:0000303|PubMed:18089847}.
/FTId=VSP_043528.
VAR_SEQ 275 404 GVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRA
VSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAAL
LIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAG
ESSTGGP -> VSDLERGAGRTRRGGANCRLCGRIRAGNSS
PGPGDPGRPGDSRPAHWGHLVAKAATPRRGEEGPRKPGGRG
GACRTESVGGT (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_002552.
VAR_SEQ 275 325 GVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRA
VSISIIEPGE -> NQARRGQLQVRGLIKSGKQKIAPNTCD
WGDGQQERNGRPQKTRRKRRSVQN (in isoform 8).
{ECO:0000303|PubMed:18089847}.
/FTId=VSP_047886.
VAR_SEQ 276 355 VPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAV
SISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAA
-> LRTREPTAVWPPIPATGPRKAVLSASASSNQARRGQLQ
VRGLIKSGKQKIAPNTCDWGDGQQERNGRPQKTRRKRRSVQ
N (in isoform 9).
{ECO:0000303|PubMed:18089847}.
/FTId=VSP_047887.
VAR_SEQ 326 404 Missing (in isoform 8).
{ECO:0000303|PubMed:18089847}.
/FTId=VSP_047888.
VAR_SEQ 332 404 SVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEE
RKAPENQEEEEERAELNQSEEPEAGESSTGGP -> EGFDK
VREAEDSPQHM (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:12495433,
ECO:0000303|PubMed:18089847}.
/FTId=VSP_042011.
VAR_SEQ 356 404 Missing (in isoform 9).
{ECO:0000303|PubMed:18089847}.
/FTId=VSP_047889.
VAR_SEQ 374 404 KAPENQEEEEERAELNQSEEPEAGESSTGGP -> PQKTRR
KRRSVQN (in isoform 10).
{ECO:0000303|PubMed:24260107}.
/FTId=VSP_055321.
VARIANT 82 82 G -> S (in dbSNP:rs2070600).
{ECO:0000269|PubMed:14574404}.
/FTId=VAR_024500.
VARIANT 100 100 Q -> R. {ECO:0000269|Ref.3}.
/FTId=VAR_011338.
CONFLICT 1 1 M -> G (in Ref. 1; AAA03574).
{ECO:0000305}.
STRAND 24 29 {ECO:0000244|PDB:3CJJ}.
STRAND 34 36 {ECO:0000244|PDB:3CJJ}.
STRAND 43 46 {ECO:0000244|PDB:3CJJ}.
STRAND 49 55 {ECO:0000244|PDB:3CJJ}.
TURN 56 58 {ECO:0000244|PDB:4P2Y}.
STRAND 62 64 {ECO:0000244|PDB:3CJJ}.
TURN 71 75 {ECO:0000244|PDB:4P2Y}.
STRAND 76 79 {ECO:0000244|PDB:2MJW}.
TURN 80 82 {ECO:0000244|PDB:2E5E}.
STRAND 84 88 {ECO:0000244|PDB:3CJJ}.
HELIX 91 93 {ECO:0000244|PDB:3CJJ}.
STRAND 95 102 {ECO:0000244|PDB:3CJJ}.
STRAND 104 119 {ECO:0000244|PDB:3CJJ}.
STRAND 125 128 {ECO:0000244|PDB:3CJJ}.
STRAND 131 134 {ECO:0000244|PDB:3CJJ}.
STRAND 139 151 {ECO:0000244|PDB:3CJJ}.
STRAND 154 159 {ECO:0000244|PDB:3CJJ}.
STRAND 162 164 {ECO:0000244|PDB:4P2Y}.
STRAND 171 179 {ECO:0000244|PDB:3CJJ}.
TURN 181 183 {ECO:0000244|PDB:3CJJ}.
STRAND 186 194 {ECO:0000244|PDB:3CJJ}.
STRAND 206 211 {ECO:0000244|PDB:3CJJ}.
STRAND 213 216 {ECO:0000244|PDB:3CJJ}.
STRAND 228 230 {ECO:0000244|PDB:3CJJ}.
STRAND 237 244 {ECO:0000244|PDB:4P2Y}.
STRAND 247 249 {ECO:0000244|PDB:4P2Y}.
STRAND 251 253 {ECO:0000244|PDB:4P2Y}.
STRAND 255 260 {ECO:0000244|PDB:4P2Y}.
STRAND 262 264 {ECO:0000244|PDB:2LE9}.
STRAND 268 273 {ECO:0000244|PDB:4P2Y}.
STRAND 284 288 {ECO:0000244|PDB:4P2Y}.
HELIX 293 295 {ECO:0000244|PDB:4P2Y}.
STRAND 297 305 {ECO:0000244|PDB:4P2Y}.
STRAND 308 312 {ECO:0000244|PDB:4P2Y}.
STRAND 316 320 {ECO:0000244|PDB:4P2Y}.
STRAND 322 324 {ECO:0000244|PDB:2LE9}.
STRAND 364 366 {ECO:0000244|PDB:2LMB}.
TURN 367 369 {ECO:0000244|PDB:2LMB}.
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


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