Protein: Advanced glycosylation end product-specific receptor (Receptor for advanced glycosylation end products) (Q15109)
Organism: Homo sapiens (Human)
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 pro-inflammatory 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.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22509345}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, phagocytic cup {ECO:0000269|PubMed:35974093}. Early endosome {ECO:0000269|PubMed:22509345}. Nucleus {ECO:0000269|PubMed:33918759, ECO:0000269|PubMed:36807739}. Note=Detected on the surface of CD11c+ peripheral blood mononuclear cells under basal conditions and after activation (PubMed:22509345). No surface expression is observed on resting T cells (PubMed:22509345). Localizes intracellularly in early endosomes in activated T cells of healthy controls and in resting T cells of patients with type I diabetes (PubMed:22509345). Nuclear translocation is enhanced by irradiation, hypoxia and reperfusion injury to brain or kidney (By similarity). Nuclear localization is enhanced by DNA damage in trophoblasts and increases in pre-term labor and preeclampsia placentas compared to control placentas (PubMed:33918759). {ECO:0000250|UniProtKB:Q62151, ECO:0000269|PubMed:22509345, ECO:0000269|PubMed:33918759}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:24081950, ECO:0000269|PubMed:27572515, ECO:0000269|PubMed:33436632}; Single-pass type I membrane protein {ECO:0000255}.; 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}.
Interaction partners:
- Protein S100-B
- High mobility group protein B1
- Protein S100-A12
- Protein S100-A4
- Protein S100-A6
- Protein diaphanous homolog 1
- Protein S100-P
- Protein S100-A11
- Protein S100-A13
- GTPase KRas
Sequence:
MAAGTAVGAWVLVLSLWGAVVGAQNITARIGEPLVLKCKGAPKKPPQRLEWKLNTGRTEAWKVLSPQGGGPWDSVARVLPNGSLFLPAVGIQDEGIFRCQAMNRNGKETKSNYRVRVYQIPGKPEIVDSASELTAGVPNKVGTCVSEGSYPAGTLSWHLDGKPLVPNEKGVSVKEQTRRHPETGLFTLQSELMVTPARGGDPRPTFSCSFSPGLPRHRALRTAPIQPRVWEPVPLEEVQLVVEPEGGAVAPGGTVTLTCEVPAQPSPQIHWMKDGVPLPLPPSPVLILPEIGPQDQGTYSCVATHSSHGPQESRAVSISIIEPGEEGPTAGSVGGSGLGTLALALGILGGLGTAALLIGVILWQRRQRRGEERKAPENQEEEEERAELNQSEEPEAGESSTGGP