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Database: UniProt
Entry: F7IAJ5_CALJA
LinkDB: F7IAJ5_CALJA
Original site: F7IAJ5_CALJA 
ID   F7IAJ5_CALJA            Unreviewed;       418 AA.
AC   F7IAJ5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 71.
DE   SubName: Full=Advanced glycosylation end-product specific receptor {ECO:0000313|Ensembl:ENSCJAP00000046914.3};
GN   Name=AGER {ECO:0000313|Ensembl:ENSCJAP00000046914.3};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000046914.3, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000046914.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000046914.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; F7IAJ5; -.
DR   STRING; 9483.ENSCJAP00000046914; -.
DR   Ensembl; ENSCJAT00000059374.3; ENSCJAP00000046914.3; ENSCJAG00000001904.5.
DR   GeneTree; ENSGT00890000139566; -.
DR   InParanoid; F7IAJ5; -.
DR   OMA; VAMHPSH; -.
DR   Proteomes; UP000008225; Chromosome 4.
DR   Bgee; ENSCJAG00000001904; Expressed in testis and 6 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0044548; F:S100 protein binding; IEA:Ensembl.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:Ensembl.
DR   GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR   GO; GO:0048143; P:astrocyte activation; IEA:Ensembl.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
DR   GO; GO:0010255; P:glucose mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0050930; P:induction of positive chemotaxis; IEA:Ensembl.
DR   GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR   GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
DR   GO; GO:1903523; P:negative regulation of blood circulation; IEA:Ensembl.
DR   GO; GO:0032693; P:negative regulation of interleukin-10 production; IEA:Ensembl.
DR   GO; GO:1900453; P:negative regulation of long-term synaptic depression; IEA:Ensembl.
DR   GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0042104; P:positive regulation of activated T cell proliferation; IEA:Ensembl.
DR   GO; GO:2001200; P:positive regulation of dendritic cell differentiation; IEA:Ensembl.
DR   GO; GO:1904472; P:positive regulation of endothelin production; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
DR   GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:1900745; P:positive regulation of p38MAPK cascade; IEA:Ensembl.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0150003; P:regulation of spontaneous synaptic transmission; IEA:Ensembl.
DR   GO; GO:0001914; P:regulation of T cell mediated cytotoxicity; IEA:Ensembl.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0045056; P:transcytosis; IEA:Ensembl.
DR   GO; GO:0150104; P:transport across blood-brain barrier; IEA:Ensembl.
DR   CDD; cd00096; Ig; 2.
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   4: Predicted;
KW   Immunity {ECO:0000256|ARBA:ARBA00022451};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   MHC I {ECO:0000256|ARBA:ARBA00022451};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..418
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5035273685"
FT   TRANSMEM        354..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..114
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          122..234
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          248..330
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          381..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..395
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  44739 MW;  9787B383C21A776D CRC64;
     MAAGAAVGAW VLVLSLWGAV VGAQNITARI GEPLVLKCKG VPKKPPQQLE WKLNTGRTEA
     WKVLSPQGGP WDSVARVPNG SLFLPAVGIQ DEGIFRCRAM NRNGKETKSN YRVRVYQIPG
     KPEIIDPASE LTAGVPNKVA EESRSKNQSC EQEVGTCVSE GSYPAGTLSW HLDGKPLVPN
     EKGVSVKEQT RRHPETGLFT LHSELMVTPA WGGAAHLTFS CSFSPGLPRR RALHTAPIQP
     RVWEPVPPEE TQLVVEPEGG AVAPGGTVTL TCDVPAQTSP QIQWMKDGVP LSLPSSPVLI
     LPEIGPQDQG TYRCVATHPS HPPQESRAVS ISIIEPGEEG PTAGSVRGSG LGTLALVLGI
     LGGLATAALL IGVILWQRRR RRRGEERKAP ENQEEEEEHA ELNQSEEHEA SESGTGGP
//
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