Primary Information |
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BoMiProt ID | Bomi322 |
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Protein Name | CD47 molecule |
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Organism | Bos taurus |
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Uniprot ID | Q08DW0 |
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Milk Fraction | MFGM, Exosome |
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Ref Sequence ID | NP_777133.2 |
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Aminoacid Length | 303 |
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Molecular Weight | 33311 |
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FASTA Sequence |
Download |
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Gene Name | CD47 |
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Gene ID | 282661 |
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Protein Existence Status | Unreviewed: Experimental evidence at transcript level |
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Secondary Information |
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Presence in other biological fluids/tissue/cells | virtually all
cells in the body |
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Protein Function | integral membrane protein that serves as the counter-receptor for the inhibitory phagocyte receptor signal-regulatory protein-α (SIRPα) and as a signaling receptor for the secreted matricellular protein thrombospondin-1; important pathophysiological functions of CD47 in cardiovascular homeostasis, immune regulation, resistance of cells and tissues to stress, and chronic diseases of aging including cancer; can regulate many important physiological cellular
mechanisms by interacting with integrins, TSP-1, or SIRPα |
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Biochemical Properties | lacks a substantial cytoplasmic signaling domain, but several cytoplasmic binding partners have been identified; N-terminal extracellular IgV domain derived from the immunoglobulin superfamily followed by a presenilin domain containing five membrane-spanning segments and ending in a short variably spliced cytoplasmic sequence; disulfide bond links Cys33 in the IgV domain to Cys263 in the last extracellular loop in the transmembrane domain and is essential for some signaling functions of CD47 |
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Significance in milk | negatively regulate phagocytosis of apoptotic mammary epithelial cells by
bystander epithelial cells during mammary gland involution |
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PTMs | Glycosylated: homotrimeric glycoprotein;IgV domain is N-glycosylated and modified with an O-linked glycosaminoglycan |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Significance of PTMs | is required for thrombospondin-1 (TSP1) signaling through CD47 |
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Bibliography | 1. Rebres, R. A. et al. (2001) ‘Membrane Raft Association of CD47 Is Necessary for Actin Polymerization and Protein Kinase C θ Translocation in Its Synergistic Activation of T Cells’, Journal of Biological Chemistry, 276(10), pp. 7672–7680. doi: 10.1074/jbc.M008858200. 2. Kaur, S. et al. (2011) ‘Heparan Sulfate Modification of the Transmembrane Receptor CD47 Is Necessary for Inhibition of T Cell Receptor Signaling by Thrombospondin-1’, Journal of Biological Chemistry, 286(17), pp. 14991–15002. doi: 10.1074/jbc.M110.179663. |