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Protein S100-A8 (Calgranulin-A) (Calprotectin L1L subunit) (Cystic fibrosis antigen) (CFAG) (Leukocyte L1 complex light chain) (Migration inhibitory factor-related protein 8) (MRP-8) (p8) (S100 calcium-binding protein A8) (Urinary stone protein band A)

 S10A8_HUMAN             Reviewed;          93 AA.
P05109; A8K5L3; D3DV37; Q5SY70; Q9UC84; Q9UC92; Q9UCJ0; Q9UCM6;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
27-SEP-2017, entry version 190.
RecName: Full=Protein S100-A8;
AltName: Full=Calgranulin-A;
AltName: Full=Calprotectin L1L subunit;
AltName: Full=Cystic fibrosis antigen;
Short=CFAG;
AltName: Full=Leukocyte L1 complex light chain;
AltName: Full=Migration inhibitory factor-related protein 8;
Short=MRP-8;
Short=p8;
AltName: Full=S100 calcium-binding protein A8;
AltName: Full=Urinary stone protein band A;
Name=S100A8; Synonyms=CAGA, CFAG, MRP8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3561500; DOI=10.1038/326614a0;
Dorin J.R., Novak M., Hill R.E., Brock D.J.H., Secher D.S.,
van Heyningen V.;
"A clue to the basic defect in cystic fibrosis from cloning the CF
antigen gene.";
Nature 326:614-617(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3313057; DOI=10.1038/330080a0;
Odink K., Cerletti N., Bruggen J., Clerc R.G., Tarcsay L., Zwaldo G.,
Gerhards G., Schlegel R., Sorg C.;
"Two calcium-binding proteins in infiltrate macrophages of rheumatoid
arthritis.";
Nature 330:80-82(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3405210; DOI=10.1128/MCB.8.6.2402;
Lagasse E., Clerc R.G.;
"Cloning and expression of two human genes encoding calcium-binding
proteins that are regulated during myeloid differentiation.";
Mol. Cell. Biol. 8:2402-2410(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-30.
PubMed=2039599; DOI=10.1515/bchm3.1991.372.1.1;
Schaefer T., Sachse G.E., Gassen H.G.;
"The calcium-binding protein MRP-8 is produced by human pulmonary
tumor cells.";
Biol. Chem. Hoppe-Seyler 372:1-4(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PROTEIN SEQUENCE OF 1-19; 24-35 AND 63-89.
PubMed=8619876; DOI=10.1006/bbrc.1996.0616;
Marti T., Erttmann K.D., Gallin M.Y.;
"Host-parasite interaction in human onchocerciasis: identification and
sequence analysis of a novel human calgranulin.";
Biochem. Biophys. Res. Commun. 221:454-458(1996).
[12]
PROTEIN SEQUENCE OF 1-27.
PubMed=8423249; DOI=10.1177/00220345930720020801;
Miyasaki K.T., Bodeau A.L., Murthy A.R., Lehrer R.I.;
"In vitro antimicrobial activity of the human neutrophil cytosolic S-
100 protein complex, calprotectin, against Capnocytophaga sputigena.";
J. Dent. Res. 72:517-523(1993).
[13]
PROTEIN SEQUENCE OF 1-25.
TISSUE=Neutrophil;
PubMed=1326551;
Lemarchand P., Vaglio M., Mauel J., Markert M.;
"Translocation of a small cytosolic calcium-binding protein (MRP-8) to
plasma membrane correlates with human neutrophil activation.";
J. Biol. Chem. 267:19379-19382(1992).
[14]
PROTEIN SEQUENCE OF 1-20.
PubMed=7849642;
Umekawa T., Kurita T.;
"Calprotectin-like protein is related to soluble organic matrix in
calcium oxalate urinary stone.";
Biochem. Mol. Biol. Int. 34:309-313(1994).
[15]
PROTEIN SEQUENCE OF 1-20.
TISSUE=Ascites;
PubMed=7695842;
Nakai M., Ishikawa M., Hamada Y., Sugano S.;
"Isolation of an ascitic oncodevelopmental protein exhibiting high
sequence homology with calcium-binding protein MRP8.";
Biol. Chem. Hoppe-Seyler 375:789-792(1994).
[16]
PROTEIN SEQUENCE OF 38-47 AND 50-56.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[17]
SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=9083090; DOI=10.1074/jbc.272.14.9496;
Rammes A., Roth J., Goebeler M., Klempt M., Hartmann M., Sorg C.;
"Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins
of the S100 family, are secreted by activated monocytes via a novel,
tubulin-dependent pathway.";
J. Biol. Chem. 272:9496-9502(1997).
[18]
INTERACTION WITH CEACAM3.
PubMed=11708798; DOI=10.1006/bbrc.2001.5955;
Streichert T., Ebrahimnejad A., Ganzer S., Flayeh R., Wagener C.,
Bruemmer J.;
"The microbial receptor CEACAM3 is linked to the calprotectin complex
in granulocytes.";
Biochem. Biophys. Res. Commun. 289:191-197(2001).
[19]
FUNCTION.
PubMed=12626582; DOI=10.4049/jimmunol.170.6.3233;
Ryckman C., Vandal K., Rouleau P., Talbot M., Tessier P.A.;
"Proinflammatory activities of S100: proteins S100A8, S100A9, and
S100A8/A9 induce neutrophil chemotaxis and adhesion.";
J. Immunol. 170:3233-3242(2003).
[20]
FUNCTION, AND INTERACTION WITH TUBULIN.
PubMed=15331440; DOI=10.1182/blood-2004-02-0446;
Vogl T., Ludwig S., Goebeler M., Strey A., Thorey I.S., Reichelt R.,
Foell D., Gerke V., Manitz M.P., Nacken W., Werner S., Sorg C.,
Roth J.;
"MRP8 and MRP14 control microtubule reorganization during
transendothelial migration of phagocytes.";
Blood 104:4260-4268(2004).
[21]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
PubMed=15598812; DOI=10.1182/blood-2004-07-2520;
Viemann D., Strey A., Janning A., Jurk K., Klimmek K., Vogl T.,
Hirono K., Ichida F., Foell D., Kehrel B., Gerke V., Sorg C., Roth J.;
"Myeloid-related proteins 8 and 14 induce a specific inflammatory
response in human microvascular endothelial cells.";
Blood 105:2955-2962(2005).
[22]
FUNCTION, AND INTERACTION WITH NCF2/P67PHOX; RAC1 AND RAC2.
PubMed=15642721; DOI=10.1096/fj.04-2377fje;
Kerkhoff C., Nacken W., Benedyk M., Dagher M.C., Sopalla C.,
Doussiere J.;
"The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase
activation by interaction with p67phox and Rac-2.";
FASEB J. 19:467-469(2005).
[23]
FUNCTION, INHIBITION BY ZINC IONS, AND SUBUNIT.
PubMed=16258195; DOI=10.1155/MI.2005.280;
Nakatani Y., Yamazaki M., Chazin W.J., Yui S.;
"Regulation of S100A8/A9 (calprotectin) binding to tumor cells by zinc
ion and its implication for apoptosis-inducing activity.";
Mediators Inflamm. 2005:280-292(2005).
[24]
SUBCELLULAR LOCATION, AND INTERACTION WITH ANXA6.
PubMed=18786929; DOI=10.1074/jbc.M803908200;
Bode G., Lueken A., Kerkhoff C., Roth J., Ludwig S., Nacken W.;
"Interaction between S100A8/A9 and annexin A6 is involved in the
calcium-induced cell surface exposition of S100A8/A9.";
J. Biol. Chem. 283:31776-31784(2008).
[25]
S-NITROSYLATION AT CYS-42.
PubMed=18832721; DOI=10.4049/jimmunol.181.8.5627;
Lim S.Y., Raftery M., Cai H., Hsu K., Yan W.X., Hseih H.L.,
Watts R.N., Richardson D., Thomas S., Perry M., Geczy C.L.;
"S-nitrosylated S100A8: novel anti-inflammatory properties.";
J. Immunol. 181:5627-5636(2008).
[26]
REVIEW.
PubMed=20523765; DOI=10.2174/187152309789838975;
Hsu K., Champaiboon C., Guenther B.D., Sorenson B.S., Khammanivong A.,
Ross K.F., Geczy C.L., Herzberg M.C.;
"Anti-infective protective properties of S100 calgranulins.";
Antiinflamm. Antiallergy Agents Med. Chem. 8:290-305(2009).
[27]
REVIEW.
PubMed=19835859; DOI=10.1016/j.ejphar.2009.08.044;
Ghavami S., Chitayat S., Hashemi M., Eshraghi M., Chazin W.J.,
Halayko A.J., Kerkhoff C.;
"S100A8/A9: a Janus-faced molecule in cancer therapy and
tumorgenesis.";
Eur. J. Pharmacol. 625:73-83(2009).
[28]
FUNCTION, AND MUTAGENESIS OF CYS-42.
PubMed=19087201; DOI=10.1111/j.1574-695X.2008.00498.x;
Sroussi H.Y., Koehler G.A., Agabian N., Villines D., Palefsky J.M.;
"Substitution of methionine 63 or 83 in S100A9 and cysteine 42 in
S100A8 abrogate the antifungal activities of S100A8/A9: potential role
for oxidative regulation.";
FEMS Immunol. Med. Microbiol. 55:55-61(2009).
[29]
FUNCTION, AND SUBUNIT.
PubMed=19122197; DOI=10.1074/jbc.M806605200;
Champaiboon C., Sappington K.J., Guenther B.D., Ross K.F.,
Herzberg M.C.;
"Calprotectin S100A9 calcium-binding loops I and II are essential for
keratinocyte resistance to bacterial invasion.";
J. Biol. Chem. 284:7078-7090(2009).
[30]
REVIEW.
PubMed=19451397; DOI=10.1189/jlb.1008647;
Ehrchen J.M., Sunderkoetter C., Foell D., Vogl T., Roth J.;
"The endogenous Toll-like receptor 4 agonist S100A8/S100A9
(calprotectin) as innate amplifier of infection, autoimmunity, and
cancer.";
J. Leukoc. Biol. 86:557-566(2009).
[31]
FUNCTION.
PubMed=19935772; DOI=10.1038/cr.2009.129;
Ghavami S., Eshragi M., Ande S.R., Chazin W.J., Klonisch T.,
Halayko A.J., McNeill K.D., Hashemi M., Kerkhoff C., Los M.;
"S100A8/A9 induces autophagy and apoptosis via ROS-mediated cross-talk
between mitochondria and lysosomes that involves BNIP3.";
Cell Res. 20:314-331(2010).
[32]
REVIEW.
PubMed=19935766; DOI=10.1038/icb.2009.88;
Perera C., McNeil H.P., Geczy C.L.;
"S100 Calgranulins in inflammatory arthritis.";
Immunol. Cell Biol. 88:41-49(2010).
[33]
REVIEW.
PubMed=20213444; DOI=10.1007/s00726-010-0528-0;
Goyette J., Geczy C.L.;
"Inflammation-associated S100 proteins: new mechanisms that regulate
function.";
Amino Acids 41:821-842(2011).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[35]
REVIEW.
PubMed=22095980; DOI=10.1161/ATVBAHA.111.236927;
Averill M.M., Kerkhoff C., Bornfeldt K.E.;
"S100A8 and S100A9 in cardiovascular biology and disease.";
Arterioscler. Thromb. Vasc. Biol. 32:223-229(2012).
[36]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21487906; DOI=10.1007/s10753-011-9330-8;
Koike A., Arai S., Yamada S., Nagae A., Saita N., Itoh H., Uemoto S.,
Totani M., Ikemoto M.;
"Dynamic mobility of immunological cells expressing S100A8 and S100A9
in vivo: a variety of functional roles of the two proteins as
regulators in acute inflammatory reaction.";
Inflammation 35:409-419(2012).
[37]
REVIEW.
PubMed=22489132; DOI=10.3390/ijms13032893;
Vogl T., Gharibyan A.L., Morozova-Roche L.A.;
"Pro-inflammatory S100A8 and S100A9 proteins: self-assembly into
multifunctional native and amyloid complexes.";
Int. J. Mol. Sci. 13:2893-2917(2012).
[38]
REVIEW.
PubMed=21912088; DOI=10.1159/000330095;
Srikrishna G.;
"S100A8 and S100A9: new insights into their roles in malignancy.";
J. Innate Immun. 4:31-40(2012).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[40]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CYBA AND CYBB.
PubMed=22808130; DOI=10.1371/journal.pone.0040277;
Berthier S., Nguyen M.V., Baillet A., Hograindleur M.A., Paclet M.H.,
Polack B., Morel F.;
"Molecular interface of S100A8 with cytochrome b and NADPH oxidase
activation.";
PLoS ONE 7:E40277-E40277(2012).
[41]
FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22363402; DOI=10.1371/journal.pone.0029333;
Atallah M., Krispin A., Trahtemberg U., Ben-Hamron S., Grau A.,
Verbovetski I., Mevorach D.;
"Constitutive neutrophil apoptosis: regulation by cell concentration
via S100 A8/9 and the MEK-ERK pathway.";
PLoS ONE 7:E29333-E29333(2012).
[42]
FUNCTION, INTERACTION WITH GAPDH, AND ASSEMBLY IN THE INOS-S100A8/A9
COMPLEX.
PubMed=25417112; DOI=10.1016/j.cell.2014.09.032;
Jia J., Arif A., Terenzi F., Willard B., Plow E.F., Hazen S.L.,
Fox P.L.;
"Target-selective protein S-nitrosylation by sequence motif
recognition.";
Cell 159:623-634(2014).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[44]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=10771424; DOI=10.1107/S0907444900002833;
Ishikawa K., Nakagawa A., Tanaka I., Suzuki M., Nishihira J.;
"The structure of human MRP8, a member of the S100 calcium-binding
protein family, by MAD phasing at 1.9 A resolution.";
Acta Crystallogr. D 56:559-566(2000).
[45]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH S100A9, SUBUNIT,
AND ZINC-BINDING.
PubMed=17553524; DOI=10.1016/j.jmb.2007.04.065;
Korndoerfer I.P., Brueckner F., Skerra A.;
"The crystal structure of the human (S100A8/S100A9)2 heterotetramer,
calprotectin, illustrates how conformational changes of interacting
alpha-helices can determine specific association of two EF-hand
proteins.";
J. Mol. Biol. 370:887-898(2007).
-!- FUNCTION: S100A8 is a calcium- and zinc-binding protein which
plays a prominent role in the regulation of inflammatory processes
and immune response. It can induce neutrophil chemotaxis and
adhesion. Predominantly found as calprotectin (S100A8/A9) which
has a wide plethora of intra- and extracellular functions. The
intracellular functions include: facilitating leukocyte
arachidonic acid trafficking and metabolism, modulation of the
tubulin-dependent cytoskeleton during migration of phagocytes and
activation of the neutrophilic NADPH-oxidase. Activates NADPH-
oxidase by facilitating the enzyme complex assembly at the cell
membrane, transferring arachidonic acid, an essential cofactor, to
the enzyme complex and S100A8 contributes to the enzyme assembly
by directly binding to NCF2/P67PHOX. The extracellular functions
involve proinfammatory, antimicrobial, oxidant-scavenging and
apoptosis-inducing activities. Its proinflammatory activity
includes recruitment of leukocytes, promotion of cytokine and
chemokine production, and regulation of leukocyte adhesion and
migration. Acts as an alarmin or a danger associated molecular
pattern (DAMP) molecule and stimulates innate immune cells via
binding to pattern recognition receptors such as Toll-like
receptor 4 (TLR4) and receptor for advanced glycation endproducts
(AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-
kappa-B signaling pathways resulting in the amplification of the
proinflammatory cascade. Has antimicrobial activity towards
bacteria and fungi and exerts its antimicrobial activity probably
via chelation of Zn(2+) which is essential for microbial growth.
Can induce cell death via autophagy and apoptosis and this occurs
through the cross-talk of mitochondria and lysosomes via reactive
oxygen species (ROS) and the process involves BNIP3. Can regulate
neutrophil number and apoptosis by an anti-apoptotic effect;
regulates cell survival via ITGAM/ITGB and TLR4 and a signaling
mechanism involving MEK-ERK. Its role as an oxidant scavenger has
a protective role in preventing exaggerated tissue damage by
scavenging oxidants. Can act as a potent amplifier of inflammation
in autoimmunity as well as in cancer development and tumor spread.
The iNOS-S100A8/A9 transnitrosylase complex directs selective
inflammatory stimulus-dependent S-nitrosylation of GAPDH and
probably multiple targets such as ANXA5, EZR, MSN and VIM by
recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute
to S-nitrosylation site selectivity. {ECO:0000269|PubMed:12626582,
ECO:0000269|PubMed:15331440, ECO:0000269|PubMed:15598812,
ECO:0000269|PubMed:15642721, ECO:0000269|PubMed:16258195,
ECO:0000269|PubMed:19087201, ECO:0000269|PubMed:19122197,
ECO:0000269|PubMed:19935772, ECO:0000269|PubMed:21487906,
ECO:0000269|PubMed:22363402, ECO:0000269|PubMed:22808130,
ECO:0000269|PubMed:25417112}.
-!- SUBUNIT: Homodimer. Preferentially exists as a heterodimer or
heterotetramer with S100A9 known as calprotectin (S100A8/A9).
S100A8 interacts with AGER, ATP2A2 and with the heterodimeric
complex formed by TLR4 and LY96 (By similarity). Interacts with
GAPDH. Calprotectin (S100A8/9) interacts with CEACAM3 and tubulin
filaments in a calcium-dependent manner. Heterotetrameric
calprotectin (S100A8/A9) interacts with ANXA6 and associates with
tubulin filaments in activated monocytes. S100A8 and calprotectin
(S100A8/9) interact with NCF2/P67PHOX, RAC1 and RAC2. Calprotectin
(S100A8/9) interacts with CYBA and CYBB. Calprotectin (S100A8/9)
interacts with NOS2 to form the iNOS-S100A8/A9 transnitrosylase
complex; induced by LDL(ox) (PubMed:25417112). {ECO:0000250,
ECO:0000269|PubMed:11708798, ECO:0000269|PubMed:15331440,
ECO:0000269|PubMed:15642721, ECO:0000269|PubMed:16258195,
ECO:0000269|PubMed:17553524, ECO:0000269|PubMed:18786929,
ECO:0000269|PubMed:19122197, ECO:0000269|PubMed:22808130,
ECO:0000269|PubMed:25417112, ECO:0000269|PubMed:9083090}.
-!- INTERACTION:
P04406:GAPDH; NbExp=6; IntAct=EBI-355281, EBI-354056;
P06702:S100A9; NbExp=7; IntAct=EBI-355281, EBI-1055001;
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm,
cytoskeleton. Cell membrane; Peripheral membrane protein.
Note=Predominantly localized in the cytoplasm. Upon elevation of
the intracellular calcium level, translocated from the cytoplasm
to the cytoskeleton and the cell membrane. Upon neutrophil
activation or endothelial adhesion of monocytes, is secreted via a
microtubule-mediated, alternative pathway.
-!- TISSUE SPECIFICITY: Calprotectin (S100A8/9) is predominantly
expressed in myeloid cells. Except for inflammatory conditions,
the expression is restricted to a specific stage of myeloid
differentiation since both proteins are expressed in circulating
neutrophils and monocytes but are absent in normal tissue
macrophages and lymphocytes. Under chronic inflammatory
conditions, such as psoriasis and malignant disorders, also
expressed in the epidermis. Found in high concentrations at local
sites of inflammation or in the serum of patients with
inflammatory diseases such as rheumatoid, cystic fibrosis,
inflammatory bowel disease, Crohn's disease, giant cell arteritis,
cystic fibrosis, Sjogren's syndrome, systemic lupus erythematosus,
and progressive systemic sclerosis. Involved in the formation and
deposition of amyloids in the aging prostate known as corpora
amylacea inclusions. Strongly up-regulated in many tumors,
including gastric, esophageal, colon, pancreatic, bladder,
ovarian, thyroid, breast and skin cancers.
{ECO:0000269|PubMed:15598812, ECO:0000269|PubMed:9083090}.
-!- MISCELLANEOUS: Binds two calcium ions per molecule with an
affinity similar to that of the S100 proteins.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/S100A8ID46446ch1q21.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y00278; CAA68390.1; -; mRNA.
EMBL; X06234; CAA29580.1; -; mRNA.
EMBL; M21005; AAA36327.1; -; Genomic_DNA.
EMBL; AK291328; BAF84017.1; -; mRNA.
EMBL; CR407674; CAG28602.1; -; mRNA.
EMBL; BT007378; AAP36042.1; -; mRNA.
EMBL; AL591704; CAI19497.1; -; Genomic_DNA.
EMBL; CH471121; EAW53330.1; -; Genomic_DNA.
EMBL; CH471121; EAW53331.1; -; Genomic_DNA.
EMBL; BC005928; AAH05928.1; -; mRNA.
CCDS; CCDS1038.1; -.
PIR; A31848; BCHUCF.
RefSeq; NP_001306126.1; NM_001319197.1.
RefSeq; NP_001306127.1; NM_001319198.1.
RefSeq; NP_001306130.1; NM_001319201.1.
RefSeq; NP_002955.2; NM_002964.4.
UniGene; Hs.416073; -.
PDB; 1MR8; X-ray; 1.90 A; A/B=1-93.
PDB; 1XK4; X-ray; 1.80 A; A/B/E/F/I/J=1-93.
PDB; 4GGF; X-ray; 1.60 A; A/K/S/U=1-93.
PDB; 4XJK; X-ray; 1.76 A; A/C/E/G/I=1-93.
PDB; 5HLO; X-ray; 2.10 A; A/B/C/D=2-93.
PDB; 5HLV; X-ray; 2.20 A; A/B/C/D/E/F/G/H=2-93.
PDB; 5W1F; X-ray; 2.60 A; A/C/E/G=1-93.
PDBsum; 1MR8; -.
PDBsum; 1XK4; -.
PDBsum; 4GGF; -.
PDBsum; 4XJK; -.
PDBsum; 5HLO; -.
PDBsum; 5HLV; -.
PDBsum; 5W1F; -.
ProteinModelPortal; P05109; -.
SMR; P05109; -.
BioGrid; 112187; 56.
CORUM; P05109; -.
DIP; DIP-1165N; -.
IntAct; P05109; 44.
MINT; MINT-1151603; -.
STRING; 9606.ENSP00000357721; -.
iPTMnet; P05109; -.
PhosphoSitePlus; P05109; -.
BioMuta; S100A8; -.
DMDM; 115442; -.
SWISS-2DPAGE; P05109; -.
EPD; P05109; -.
MaxQB; P05109; -.
PaxDb; P05109; -.
PeptideAtlas; P05109; -.
PRIDE; P05109; -.
TopDownProteomics; P05109; -.
DNASU; 6279; -.
Ensembl; ENST00000368732; ENSP00000357721; ENSG00000143546.
Ensembl; ENST00000368733; ENSP00000357722; ENSG00000143546.
GeneID; 6279; -.
KEGG; hsa:6279; -.
UCSC; uc001fbs.3; human.
CTD; 6279; -.
DisGeNET; 6279; -.
EuPathDB; HostDB:ENSG00000143546.9; -.
GeneCards; S100A8; -.
HGNC; HGNC:10498; S100A8.
HPA; CAB002791; -.
HPA; HPA024372; -.
MIM; 123885; gene.
neXtProt; NX_P05109; -.
OpenTargets; ENSG00000143546; -.
PharmGKB; PA34910; -.
eggNOG; ENOG410J2UM; Eukaryota.
eggNOG; ENOG4111CN5; LUCA.
GeneTree; ENSGT00760000119034; -.
HOVERGEN; HBG001479; -.
InParanoid; P05109; -.
KO; K21127; -.
OMA; IKGNYHA; -.
OrthoDB; EOG091G13NB; -.
PhylomeDB; P05109; -.
TreeFam; TF332727; -.
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6799990; Metal sequestration by antimicrobial proteins.
ChiTaRS; S100A8; human.
EvolutionaryTrace; P05109; -.
GeneWiki; S100_calcium_binding_protein_A8; -.
GenomeRNAi; 6279; -.
PRO; PR:P05109; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143546; -.
CleanEx; HS_S100A8; -.
Genevisible; P05109; HS.
GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0050544; F:arachidonic acid binding; TAS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
GO; GO:0008017; F:microtubule binding; TAS:UniProtKB.
GO; GO:0050786; F:RAGE receptor binding; TAS:UniProtKB.
GO; GO:0035662; F:Toll-like receptor 4 binding; TAS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
GO; GO:0006914; P:autophagy; IDA:UniProtKB.
GO; GO:0032602; P:chemokine production; TAS:UniProtKB.
GO; GO:0002544; P:chronic inflammatory response; IEA:Ensembl.
GO; GO:0001816; P:cytokine production; TAS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; TAS:UniProtKB.
GO; GO:0050832; P:defense response to fungus; TAS:UniProtKB.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IDA:UniProtKB.
GO; GO:0070488; P:neutrophil aggregation; IDA:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IMP:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; TAS:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; IDA:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:UniProtKB.
GO; GO:0002793; P:positive regulation of peptide secretion; IEA:Ensembl.
GO; GO:0051493; P:regulation of cytoskeleton organization; TAS:UniProtKB.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
GO; GO:0032119; P:sequestering of zinc ion; TAS:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
InterPro; IPR028474; S100A8.
PANTHER; PTHR11639:SF111; PTHR11639:SF111; 1.
Pfam; PF01023; S_100; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 1.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
3D-structure; Antimicrobial; Apoptosis; Autophagy; Calcium;
Cell membrane; Chemotaxis; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Immunity; Inflammatory response;
Innate immunity; Membrane; Metal-binding; Reference proteome; Repeat;
S-nitrosylation; Secreted; Zinc.
CHAIN 1 93 Protein S100-A8.
/FTId=PRO_0000143993.
DOMAIN 12 47 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 46 81 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 20 33 1; low affinity.
CA_BIND 59 70 2; high affinity.
METAL 17 17 Zinc. {ECO:0000305}.
METAL 27 27 Zinc. {ECO:0000305}.
METAL 83 83 Zinc. {ECO:0000305}.
METAL 87 87 Zinc. {ECO:0000305}.
MOD_RES 42 42 S-nitrosocysteine.
{ECO:0000269|PubMed:18832721}.
MUTAGEN 42 42 C->A: Loss of antifungal activity.
{ECO:0000269|PubMed:19087201}.
CONFLICT 80 93 VAAHKKSHEESHKE -> WQPTKKAMKKATKSS (in
Ref. 1; CAA68390). {ECO:0000305}.
HELIX 4 20 {ECO:0000244|PDB:4GGF}.
STRAND 22 25 {ECO:0000244|PDB:4GGF}.
HELIX 31 41 {ECO:0000244|PDB:4GGF}.
HELIX 44 47 {ECO:0000244|PDB:4GGF}.
HELIX 51 58 {ECO:0000244|PDB:4GGF}.
STRAND 63 66 {ECO:0000244|PDB:4GGF}.
HELIX 68 86 {ECO:0000244|PDB:4GGF}.
SEQUENCE 93 AA; 10835 MW; 78F589140B9CE166 CRC64;
MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI
NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE


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