RAGE_BOVIN
ID RAGE_BOVIN Reviewed; 416 AA.
AC Q28173;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 120.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 63-70; 140-159;
RP 162-168; 182-196 AND 228-231.
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 PROTEIN SEQUENCE OF 23-54.
RX PubMed=1321822; DOI=10.1016/s0021-9258(18)42137-0;
RA Schmidt A.M., Vianna M., Gerlach M., Brett J., Ryan J., Kao J.,
RA Esposito C., Hegarty H., Hurley W., Clauss M.;
RT "Isolation and characterization of two binding proteins for advanced
RT glycosylation end products from bovine lung which are present on the
RT endothelial cell surface.";
RL J. Biol. Chem. 267:14987-14997(1992).
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. Receptor for amyloid beta peptide. Contributes to the
CC translocation of amyloid-beta peptide (ABPP) across the cell membrane
CC from the extracellular to the intracellular space in cortical neurons.
CC ABPP-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. Can also bind oligonucleotides (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with S100B, S100A1, S100A12, S100A14 and APP.
CC Constitutive homodimer; disulfide-linked (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Endothelial cells.
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; M91212; AAA03575.1; -; mRNA.
DR PIR; A42879; A42879.
DR RefSeq; NP_776407.1; NM_173982.3.
DR AlphaFoldDB; Q28173; -.
DR SMR; Q28173; -.
DR STRING; 9913.ENSBTAP00000019179; -.
DR PaxDb; Q28173; -.
DR PRIDE; Q28173; -.
DR GeneID; 280986; -.
DR KEGG; bta:280986; -.
DR CTD; 177; -.
DR eggNOG; ENOG502SQ8N; Eukaryota.
DR InParanoid; Q28173; -.
DR OrthoDB; 807961at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
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 Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Inflammatory response; Membrane; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:1321822"
FT CHAIN 23..416
FT /note="Advanced glycosylation end product-specific
FT receptor"
FT /id="PRO_0000014922"
FT TOPO_DOM 23..352
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..115
FT /note="Ig-like V-type"
FT DOMAIN 123..220
FT /note="Ig-like C2-type 1"
FT DOMAIN 238..327
FT /note="Ig-like C2-type 2"
FT REGION 377..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 269
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 311
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 416 AA; 44182 MW; B703815573E767AE CRC64;
MAAGAVVGAW MLVLSLGGTV TGDQNITARI GKPLVLNCKG APKKPPQQLE WKLNTGRTEA
WKVLSPQGDP WDSVARVLPN GSLLLPAVGI QDEGTFRCRA TSRSGKETKS NYRVRVYQIP
GKPEIVDPAS ELMAGVPNKV GTCVSEGGYP AGTLNWLLDG KTLIPDGKGV SVKEETKRHP
KTGLFTLHSE LMVTPARGGA LHPTFSCSFT PGLPRRRALH TAPIQLRVWS EHRGGEGPNV
DAVPLKEVQL VVEPEGGAVA PGGTVTLTCE APAQPPPQIH WIKDGRPLPL PPGPMLLLPE
VGPEDQGTYS CVATHPSHGP QESRAVSVTI IETGEEGTTA GSVEGPGLET LALTLGILGG
LGTVALLIGV IVWHRRRQRK GQERKVPENQ EEEEEERAEL NQPEEPEAAE SSTGGP
