S100A8

S100 calcium-binding protein A8 (S100A8) is a protein that in humans is encoded by the S100A8 gene.[5] It is also known as calgranulin A.

S100A8
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1MR8, 1XK4, 4GGF, 4XJK, 5HLO, 5HLV
Identifiers
Aliases	S100A8, 60B8AG, CAGA, CFAG, CGLA, CP-10, L1Ag, MA387, MIF, MRP8, NIF, P8, S100 calcium binding protein A8
External IDs	OMIM: 123885 MGI: 88244 HomoloGene: 2225 GeneCards: S100A8
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q21.3 Start 153,390,032 bp[1] End 153,391,073 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3 F1|3 39.9 cM Start 90,668,978 bp[2] End 90,670,035 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • Toll-like receptor 4 binding • RAGE receptor binding • microtubule binding • GO:0001948 protein binding • calcium ion binding • arachidonic acid binding • zinc ion binding • metal ion binding Cellular component • cell nucleus • cytoskeleton • cytosol • extracellular exosome • membrane • cell membrane • cytoplasm • extracellular • secretory granule lumen • intermediate filament cytoskeleton • extracellular region • collagen-containing extracellular matrix Biological process • regulation of inflammatory response • activation of cysteine-type endopeptidase activity involved in apoptotic process • immune system process • positive regulation of inflammatory response • neutrophil chemotaxis • positive regulation of intrinsic apoptotic signaling pathway • defense response to fungus • response to ethanol • chemokine production • response to zinc ion • acute inflammatory response • defense response to bacterium • leukocyte migration involved in inflammatory response • peptidyl-cysteine S-nitrosylation • sequestering of zinc ion • neutrophil aggregation • response to lipopolysaccharide • chemotaxis • positive regulation of peptide secretion • chronic inflammation • astrocyte development • wound healing • apoptotic process • positive regulation of cell growth • autophagy • inflammatory response • regulation of cytoskeleton organization • cytokine production • positive regulation of NF-kappaB transcription factor activity • innate immune system • toll-like receptor signaling pathway • antimicrobial humoral response • neutrophil degranulation • autocrine signaling Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6279	20201
Ensembl	ENSG00000143546	ENSMUSG00000056054
UniProt	P05109	P27005
RefSeq (mRNA)	NM_002964 NM_001319196 NM_001319197 NM_001319198 NM_001319201	NM_013650
RefSeq (protein)	NP_001306125 NP_001306126 NP_001306127 NP_001306130 NP_002955	NP_038678
Location (UCSC)	Chr 1: 153.39 – 153.39 Mb	Chr 3: 90.67 – 90.67 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The proteins S100A8 and S100A9 form a heterodimer called calprotectin.

The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells, and involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100 genes include at least 13 members which are located as a cluster on chromosome 1q21. This protein may function in the inhibition of casein kinase and as a cytokine. Altered expression of this protein is associated with the disease cystic fibrosis.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000143546 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000056054 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: S100A8 S100 calcium binding protein A8".

Further reading

• Schäfer BW, Heizmann CW (1996). "The S100 family of EF-hand calcium-binding proteins: functions and pathology". Trends Biochem. Sci. 21 (4): 134–40. doi:10.1016/S0968-0004(96)80167-8. PMID 8701470.
• Kerkhoff C, Klempt M, Sorg C (1999). "Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9)". Biochim. Biophys. Acta. 1448 (2): 200–11. doi:10.1016/S0167-4889(98)00144-X. PMID 9920411.
• Nacken W, Roth J, Sorg C, Kerkhoff C (2003). "S100A9/S100A8: Myeloid representatives of the S100 protein family as prominent players in innate immunity". Microsc. Res. Tech. 60 (6): 569–80. doi:10.1002/jemt.10299. PMID 12645005.
• Roth J, Vogl T, Sorg C, Sunderkötter C (2004). "Phagocyte-specific S100 proteins: a novel group of proinflammatory molecules". Trends Immunol. 24 (4): 155–8. doi:10.1016/S1471-4906(03)00062-0. PMID 12697438.
• Rasmussen HH, van Damme J, Puype M, et al. (1993). "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes". Electrophoresis. 13 (12): 960–9. doi:10.1002/elps.11501301199. PMID 1286667.
• Lemarchand P, Vaglio M, Mauël J, Markert M (1992). "Translocation of a small cytosolic calcium-binding protein (MRP-8) to plasma membrane correlates with human neutrophil activation". J. Biol. Chem. 267 (27): 19379–82. PMID 1326551.
• Schäfer T, Sachse GE, Gassen HG (1991). "The calcium-binding protein MRP-8 is produced by human pulmonary tumor cells". Biol. Chem. Hoppe-Seyler. 372 (1): 1–4. doi:10.1515/bchm3.1991.372.1.1. PMID 2039599.
• Dorin JR, Emslie E, van Heyningen V (1991). "Related calcium-binding proteins map to the same subregion of chromosome 1q and to an extended region of synteny on mouse chromosome 3". Genomics. 8 (3): 420–6. doi:10.1016/0888-7543(90)90027-R. PMID 2149559.
• Wilkinson MM, Busuttil A, Hayward C, et al. (1989). "Expression pattern of two related cystic fibrosis-associated calcium-binding proteins in normal and abnormal tissues". J. Cell Sci. 91 (2): 221–30. PMID 3267695.
• Odink K, Cerletti N, Brüggen J, et al. (1987). "Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis". Nature. 330 (6143): 80–2. doi:10.1038/330080a0. PMID 3313057.
• Lagasse E, Clerc RG (1988). "Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation". Mol. Cell. Biol. 8 (6): 2402–10. PMC 363438. PMID 3405210.
• Dorin JR, Novak M, Hill RE, et al. (1987). "A clue to the basic defect in cystic fibrosis from cloning the CF antigen gene". Nature. 326 (6113): 614–7. doi:10.1038/326614a0. PMID 3561500.
• Schäfer BW, Wicki R, Engelkamp D, et al. (1995). "Isolation of a YAC clone covering a cluster of nine S100 genes on human chromosome 1q21: rationale for a new nomenclature of the S100 calcium-binding protein family". Genomics. 25 (3): 638–43. doi:10.1016/0888-7543(95)80005-7. PMID 7759097.
• Umekawa T, Kurita T (1995). "Calprotectin-like protein is related to soluble organic matrix in calcium oxalate urinary stone". Biochem. Mol. Biol. Int. 34 (2): 309–13. PMID 7849642.
• Engelkamp D, Schäfer BW, Mattei MG, et al. (1993). "Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E". Proc. Natl. Acad. Sci. U.S.A. 90 (14): 6547–51. doi:10.1073/pnas.90.14.6547. PMC 46969. PMID 8341667.
• Roth J, Burwinkel F, van den Bos C, et al. (1993). "MRP8 and MRP14, S-100-like proteins associated with myeloid differentiation, are translocated to plasma membrane and intermediate filaments in a calcium-dependent manner". Blood. 82 (6): 1875–83. PMID 8400238.
• Miyasaki KT, Bodeau AL, Murthy AR, Lehrer RI (1993). "In vitro antimicrobial activity of the human neutrophil cytosolic S-100 protein complex, calprotectin, against Capnocytophaga sputigena". J. Dent. Res. 72 (2): 517–23. doi:10.1177/00220345930720020801. PMID 8423249.
• Marti T, Erttmann KD, Gallin MY (1996). "Host-parasite interaction in human onchocerciasis: identification and sequence analysis of a novel human calgranulin". Biochem. Biophys. Res. Commun. 221 (2): 454–8. doi:10.1006/bbrc.1996.0616. PMID 8619876.