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Database: UniProt/SWISS-PROT
Entry: RAGE_BOVIN
LinkDB: RAGE_BOVIN
Original site: 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   08-MAY-2019, entry version 114.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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;
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;
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
CC       products (AGE). These are nonenzymatically glycosylated proteins
CC       which accumulate in vascular tissue in aging and at an accelerated
CC       rate in diabetes. Acts as a mediator of both acute and chronic
CC       vascular inflammation in conditions such as atherosclerosis and in
CC       particular as a complication of diabetes. AGE/RAGE signaling plays
CC       an important role in regulating the production/expression of TNF-
CC       alpha, oxidative stress, and endothelial dysfunction in type 2
CC       diabetes. Interaction with S100A12 on endothelium, mononuclear
CC       phagocytes, and lymphocytes triggers cellular activation, with
CC       generation of key proinflammatory mediators. Interaction with
CC       S100B after myocardial infarction may play a role in myocyte
CC       apoptosis by activating ERK1/2 and p53/TP53 signaling. Receptor
CC       for amyloid beta peptide. Contributes to the translocation of
CC       amyloid-beta peptide (ABPP) across the cell membrane from the
CC       extracellular to the intracellular space in cortical neurons.
CC       ABPP-initiated RAGE signaling, especially stimulation of p38
CC       mitogen-activated protein kinase (MAPK), has the capacity to drive
CC       a transport system delivering ABPP as a complex with RAGE to the
CC       intraneuronal space. Can also bind oligonucleotides (By
CC       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
CC       protein.
CC   -!- TISSUE SPECIFICITY: Endothelial cells.
DR   EMBL; M91212; AAA03575.1; -; mRNA.
DR   PIR; A42879; A42879.
DR   RefSeq; NP_776407.1; NM_173982.3.
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; ENOG410IVT2; Eukaryota.
DR   eggNOG; ENOG4111C4I; LUCA.
DR   HOGENOM; HOG000232122; -.
DR   InParanoid; Q28173; -.
DR   KO; K19722; -.
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   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Inflammatory response; Membrane;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22       {ECO:0000269|PubMed:1321822}.
FT   CHAIN        23    416       Advanced glycosylation end product-
FT                                specific receptor.
FT                                /FTId=PRO_0000014922.
FT   TOPO_DOM     23    352       Extracellular. {ECO:0000255}.
FT   TRANSMEM    353    373       Helical. {ECO:0000255}.
FT   TOPO_DOM    374    416       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       23    115       Ig-like V-type.
FT   DOMAIN      123    220       Ig-like C2-type 1.
FT   DOMAIN      238    327       Ig-like C2-type 2.
FT   COMPBIAS    391    396       Poly-Glu.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     80     80       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     38     98       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    143    207       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    269    269       Interchain. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00114}.
FT   DISULFID    311    311       Interchain. {ECO:0000255|PROSITE-
FT                                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
//
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