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Protein S100-A9 (Calgranulin-B) (Calprotectin L1H subunit) (Leukocyte L1 complex heavy chain) (Migration inhibitory factor-related protein 14) (MRP-14) (p14) (S100 calcium-binding protein A9)

 S10A9_HUMAN             Reviewed;         114 AA.
P06702; D3DV36; Q6FGA1; Q9NYM0; Q9UCJ1;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
25-OCT-2017, entry version 200.
RecName: Full=Protein S100-A9;
AltName: Full=Calgranulin-B;
AltName: Full=Calprotectin L1H subunit;
AltName: Full=Leukocyte L1 complex heavy chain;
AltName: Full=Migration inhibitory factor-related protein 14;
Short=MRP-14;
Short=p14;
AltName: Full=S100 calcium-binding protein A9;
Name=S100A9; Synonyms=CAGB, CFAG, MRP14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND BLOCKAGE OF N-TERMINUS.
PubMed=2656677;
Murao S., Collart F.R., Huberman E.;
"A protein containing the cystic fibrosis antigen is an inhibitor of
protein kinases.";
J. Biol. Chem. 264:8356-8360(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-20.
Wang M., Xu X., Cai Y., Xu H., Han Y., Xu Z., Wu M.;
"Human gene for migration inhibitory factor-related protein 14
(MRP14), variant allele.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
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).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[9]
PROTEIN SEQUENCE OF 84-114, AND PHOSPHORYLATION AT THR-113.
PubMed=2478889; DOI=10.1038/342189a0;
Edgeworth J., Freemont P., Hogg N.;
"Ionomycin-regulated phosphorylation of the myeloid calcium-binding
protein p14.";
Nature 342:189-192(1989).
[10]
PROTEIN SEQUENCE, AND BLOCKAGE OF N-TERMINUS.
PubMed=2776242; DOI=10.1248/cpb.37.1576;
Tobe T., Murakami K., Tomita M., Nozawa R.;
"Amino acid sequences of 60B8 antigens induced in HL-60 cells by 1,25-
dihydroxyvitamin D3. The antigens are identical with macrophage-
related protein-14 and -8.";
Chem. Pharm. Bull. 37:1576-1580(1989).
[11]
PROTEIN SEQUENCE OF 11-19; 26-37 AND 94-107.
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).
[12]
PROTEIN SEQUENCE OF 5-34, SUBCELLULAR LOCATION, IDENTIFICATION IN THE
CALPROTECTIN COMPLEX, FUNCTION, AND TISSUE SPECIFICITY.
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]
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).
[14]
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).
[15]
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).
[16]
FUNCTION, INTERACTION WITH TUBULIN, AND PHOSPHORYLATION AT THR-113.
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).
[17]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION
BY MASS SPECTROMETRY.
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).
[18]
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).
[19]
PHOSPHORYLATION AT THR-113.
PubMed=15905572; DOI=10.4049/jimmunol.174.11.7257;
Lominadze G., Rane M.J., Merchant M., Cai J., Ward R.A., McLeish K.R.;
"Myeloid-related protein-14 is a p38 MAPK substrate in human
neutrophils.";
J. Immunol. 174:7257-7267(2005).
[20]
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).
[21]
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[24]
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).
[25]
FUNCTION.
PubMed=19534726; DOI=10.1042/BJ20090465;
Li C., Chen H., Ding F., Zhang Y., Luo A., Wang M., Liu Z.;
"A novel p53 target gene, S100A9, induces p53-dependent cellular
apoptosis and mediates the p53 apoptosis pathway.";
Biochem. J. 422:363-372(2009).
[26]
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).
[27]
FUNCTION, SUBUNIT, MUTAGENESIS OF MET-63; MET-81 AND MET-83, AND
INHIBITION BY ZINC IONS.
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).
[28]
FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-36 AND GLU-78.
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).
[29]
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).
[30]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TLR4; LY96
AND AGER, AND QUINOLINE-3-CARBOXAMIDE BINDING.
PubMed=19402754; DOI=10.1371/journal.pbio.1000097;
Bjoerk P., Bjoerk A., Vogl T., Stenstroem M., Liberg D., Olsson A.,
Roth J., Ivars F., Leanderson T.;
"Identification of human S100A9 as a novel target for treatment of
autoimmune disease via binding to quinoline-3-carboxamides.";
PLoS Biol. 7:E97-E97(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]
FUNCTION.
PubMed=20103766; DOI=10.1189/jlb.1009676;
Simard J.C., Girard D., Tessier P.A.;
"Induction of neutrophil degranulation by S100A9 via a MAPK-dependent
mechanism.";
J. Leukoc. Biol. 87:905-914(2010).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[35]
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).
[36]
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).
[37]
FUNCTION.
PubMed=21325622; DOI=10.4049/jimmunol.1002956;
Simard J.C., Simon M.M., Tessier P.A., Girard D.;
"Damage-associated molecular pattern S100A9 increases bactericidal
activity of human neutrophils by enhancing phagocytosis.";
J. Immunol. 186:3622-3631(2011).
[38]
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).
[39]
FUNCTION.
PubMed=22804476; DOI=10.1111/j.1365-2567.2012.03619.x;
Riva M., Kaellberg E., Bjoerk P., Hancz D., Vogl T., Roth J.,
Ivars F., Leanderson T.;
"Induction of nuclear factor-kappaB responses by the S100A9 protein is
Toll-like receptor-4-dependent.";
Immunology 137:172-182(2012).
[40]
FUNCTION.
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).
[41]
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).
[42]
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).
[43]
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).
[44]
INTERACTION WITH APP.
PubMed=22457725; DOI=10.1371/journal.pone.0032953;
Zhang C., Liu Y., Gilthorpe J., van der Maarel J.R.;
"MRP14 (S100A9) protein interacts with Alzheimer beta-amyloid peptide
and induces its fibrillization.";
PLoS ONE 7:E32953-E32953(2012).
[45]
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).
[46]
FUNCTION, ASSEMBLY IN THE INOS-S100A8/A9 COMPLEX, MUTAGENESIS OF
CYS-3, AND S-NITROSYLATION AT CYS-3.
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).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113, AND 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).
[48]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
MASS SPECTROMETRY, AND SUBUNIT.
PubMed=11851337; DOI=10.1006/jmbi.2001.5340;
Itou H., Yao M., Fujita I., Watanabe N., Suzuki M., Nishihira J.,
Tanaka I.;
"The crystal structure of human MRP14 (S100A9), a Ca(2+)-dependent
regulator protein in inflammatory process.";
J. Mol. Biol. 316:265-276(2002).
[49]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-114 IN COMPLEX WITH S100A8,
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: S100A9 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,
adhesion, can increase the bactericidal activity of neutrophils by
promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2
and can induce degranulation of neutrophils by a MAPK-dependent
mechanism. 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.
Has transnitrosylase activity; in oxidatively-modified low-
densitity lipoprotein (LDL(ox))-induced S-nitrosylation of GAPDH
on 'Cys-247' proposed to transfer the NO moiety from NOS2/iNOS to
GAPDH via its own S-nitrosylated Cys-3. The iNOS-S100A8/A9
transnitrosylase complex is proposed to also direct selective
inflammatory stimulus-dependent S-nitrosylation of multiple
targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-
x-x-[DE] motif. {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:19402754, ECO:0000269|PubMed:19534726,
ECO:0000269|PubMed:19935772, ECO:0000269|PubMed:20103766,
ECO:0000269|PubMed:21325622, ECO:0000269|PubMed:21487906,
ECO:0000269|PubMed:22363402, ECO:0000269|PubMed:22804476,
ECO:0000269|PubMed:22808130, ECO:0000269|PubMed:25417112,
ECO:0000269|PubMed:8423249}.
-!- SUBUNIT: Homodimer. Preferentially exists as a heterodimer or
heterotetramer with S100A8 known as calprotectin (S100A8/A9).
S100A9 interacts with ATP2A2 (By similarity). S100A9 interacts
with AGER, and with the heterodimeric complex formed by TLR4 and
LY96 in the presence of calcium and/or zinc ions. S100A9 binds
quinoline-3-carboxamides in the presence of calcium and/or zinc
ions. S100A9 interacts with amyloid-beta protein 40. 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. Calprotectin (S100A8/9)
interacts with NCF2/P67PHOX, RAC1, RAC2, 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:11851337, ECO:0000269|PubMed:15331440,
ECO:0000269|PubMed:15642721, ECO:0000269|PubMed:16258195,
ECO:0000269|PubMed:17553524, ECO:0000269|PubMed:18786929,
ECO:0000269|PubMed:19087201, ECO:0000269|PubMed:19122197,
ECO:0000269|PubMed:19402754, ECO:0000269|PubMed:22457725,
ECO:0000269|PubMed:22808130, ECO:0000269|PubMed:25417112,
ECO:0000269|PubMed:8423249, ECO:0000269|PubMed:9083090,
ECO:0000305|PubMed:25417112}.
-!- INTERACTION:
P49407:ARRB1; NbExp=2; IntAct=EBI-1055001, EBI-743313;
P32121:ARRB2; NbExp=2; IntAct=EBI-1055001, EBI-714559;
P05109:S100A8; NbExp=7; IntAct=EBI-1055001, EBI-355281;
-!- 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:3313057,
ECO:0000269|PubMed:3405210, ECO:0000269|PubMed:8423249,
ECO:0000269|PubMed:9083090}.
-!- PTM: Phosphorylated. Phosphorylation inhibits activation of
tubulin polymerization. {ECO:0000269|PubMed:15331440,
ECO:0000269|PubMed:15905572, ECO:0000269|PubMed:2478889}.
-!- PTM: S-nitrosylation of Cys-3 is implicated in LDL(ox)-induced S-
nitrosylation of GAPDH at 'Cys-247' through a transnitrosylase
mechanism involving a iNOS-S100A8/9 complex (PubMed:25417112).
{ECO:0000305|PubMed:25417112}.
-!- MASS SPECTROMETRY: Mass=13115; Method=MALDI; Range=2-114;
Evidence={ECO:0000269|PubMed:11851337};
-!- 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/S100A9ID45569ch1q21.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X06233; CAA29579.1; -; mRNA.
EMBL; M21064; AAA36326.1; -; Genomic_DNA.
EMBL; M26311; AAA68480.1; -; mRNA.
EMBL; AF237581; AAF62536.1; -; Genomic_DNA.
EMBL; AF237582; AAF62537.1; -; Genomic_DNA.
EMBL; CR542207; CAG47003.1; -; mRNA.
EMBL; CR542224; CAG47020.1; -; mRNA.
EMBL; AL591704; CAI19494.1; -; Genomic_DNA.
EMBL; CH471121; EAW53333.1; -; Genomic_DNA.
EMBL; CH471121; EAW53334.1; -; Genomic_DNA.
EMBL; BC047681; AAH47681.1; -; mRNA.
CCDS; CCDS1036.1; -.
PIR; B31848; B31848.
RefSeq; NP_002956.1; NM_002965.3.
UniGene; Hs.112405; -.
PDB; 1IRJ; X-ray; 2.10 A; A/B/C/D/E/F/G/H=2-114.
PDB; 1XK4; X-ray; 1.80 A; C/D/G/H/K/L=2-114.
PDB; 4GGF; X-ray; 1.60 A; C/L/T/V=1-114.
PDB; 4XJK; X-ray; 1.76 A; B/D/F/H/J=1-114.
PDB; 5I8N; NMR; -; A/B=1-114.
PDB; 5W1F; X-ray; 2.60 A; B/D/F/H=1-114.
PDBsum; 1IRJ; -.
PDBsum; 1XK4; -.
PDBsum; 4GGF; -.
PDBsum; 4XJK; -.
PDBsum; 5I8N; -.
PDBsum; 5W1F; -.
ProteinModelPortal; P06702; -.
SMR; P06702; -.
BioGrid; 112188; 114.
CORUM; P06702; -.
DIP; DIP-1166N; -.
IntAct; P06702; 27.
MINT; MINT-5002390; -.
STRING; 9606.ENSP00000357727; -.
iPTMnet; P06702; -.
PhosphoSitePlus; P06702; -.
SwissPalm; P06702; -.
BioMuta; S100A9; -.
DMDM; 115444; -.
OGP; P06702; -.
SWISS-2DPAGE; P06702; -.
UCD-2DPAGE; P06702; -.
EPD; P06702; -.
MaxQB; P06702; -.
PaxDb; P06702; -.
PeptideAtlas; P06702; -.
PRIDE; P06702; -.
TopDownProteomics; P06702; -.
Ensembl; ENST00000368738; ENSP00000357727; ENSG00000163220.
GeneID; 6280; -.
KEGG; hsa:6280; -.
UCSC; uc001fbq.3; human.
CTD; 6280; -.
DisGeNET; 6280; -.
EuPathDB; HostDB:ENSG00000163220.10; -.
GeneCards; S100A9; -.
HGNC; HGNC:10499; S100A9.
HPA; CAB009441; -.
HPA; HPA004193; -.
MIM; 123886; gene.
neXtProt; NX_P06702; -.
OpenTargets; ENSG00000163220; -.
PharmGKB; PA34911; -.
eggNOG; ENOG410J1XC; Eukaryota.
eggNOG; ENOG4111C30; LUCA.
GeneTree; ENSGT00900000141006; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P06702; -.
KO; K21128; -.
OMA; DHIMEDL; -.
OrthoDB; EOG091G12NB; -.
PhylomeDB; P06702; -.
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.
SIGNOR; P06702; -.
ChiTaRS; S100A9; human.
EvolutionaryTrace; P06702; -.
GeneWiki; S100A9; -.
GenomeRNAi; 6280; -.
PRO; PR:P06702; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000163220; -.
CleanEx; HS_S100A9; -.
Genevisible; P06702; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; 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:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
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:0004871; F:signal transducer activity; TAS:ProtInc.
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:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006914; P:autophagy; IDA:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0032602; P:chemokine production; TAS:UniProtKB.
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:0035821; P:modification of morphology or physiology of other organism; 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:0035606; P:peptidyl-cysteine S-trans-nitrosylation; IDA: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:0051493; P:regulation of cytoskeleton organization; TAS:UniProtKB.
GO; GO:0032119; P:sequestering of zinc ion; TAS:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR028475; S100-A9.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
PANTHER; PTHR11639:SF79; PTHR11639:SF79; 1.
Pfam; PF01023; S_100; 1.
SMART; SM00054; EFh; 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; Antioxidant; Apoptosis; Autophagy;
Calcium; Cell membrane; Chemotaxis; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Immunity;
Inflammatory response; Innate immunity; Membrane; Metal-binding;
Methylation; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
S-nitrosylation; Secreted; Zinc.
CHAIN 1 114 Protein S100-A9.
/FTId=PRO_0000143997.
DOMAIN 12 47 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 54 89 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 23 36 1; low affinity.
CA_BIND 67 78 2; high affinity. {ECO:0000305}.
METAL 20 20 Zinc. {ECO:0000305}.
METAL 30 30 Zinc. {ECO:0000305}.
METAL 91 91 Zinc. {ECO:0000305}.
METAL 95 95 Zinc. {ECO:0000305}.
MOD_RES 2 2 Blocked amino end (Thr).
MOD_RES 3 3 S-nitrosocysteine; transient.
{ECO:0000305|PubMed:25417112}.
MOD_RES 105 105 Pros-methylhistidine.
{ECO:0000250|UniProtKB:P50116}.
MOD_RES 113 113 Phosphothreonine; by MAPK14.
{ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:15331440,
ECO:0000269|PubMed:15905572,
ECO:0000269|PubMed:2478889}.
VARIANT 20 20 H -> R. {ECO:0000269|Ref.4}.
/FTId=VAR_013008.
MUTAGEN 3 3 C->A: Disrupts interaction with NOS2 and
inhibits LDL(ox)-induced GAPDH S-
nitrosylation; no effect on interaction
with S100A8.
{ECO:0000269|PubMed:25417112}.
MUTAGEN 36 36 E->Q: Loss of resistance to bacterial
invasion; when associated with Q-78.
{ECO:0000269|PubMed:19122197}.
MUTAGEN 63 63 M->A: Loss of antifungal activity.
{ECO:0000269|PubMed:19087201}.
MUTAGEN 78 78 E->Q: Loss of resistance to bacterial
invasion; when associated with Q-36.
{ECO:0000269|PubMed:19122197}.
MUTAGEN 81 81 M->A: No effect on antifungal activity.
{ECO:0000269|PubMed:19087201}.
MUTAGEN 83 83 M->A: Loss of antifungal activity.
{ECO:0000269|PubMed:19087201}.
CONFLICT 6 6 S -> H (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 25 25 K -> F (in Ref. 12; AA sequence).
{ECO:0000305}.
CONFLICT 28 28 H -> L (in Ref. 12; AA sequence).
{ECO:0000305}.
HELIX 7 23 {ECO:0000244|PDB:4GGF}.
STRAND 25 28 {ECO:0000244|PDB:4GGF}.
HELIX 34 44 {ECO:0000244|PDB:4GGF}.
TURN 45 49 {ECO:0000244|PDB:4GGF}.
HELIX 50 53 {ECO:0000244|PDB:4GGF}.
HELIX 56 66 {ECO:0000244|PDB:4GGF}.
STRAND 71 74 {ECO:0000244|PDB:4GGF}.
HELIX 76 94 {ECO:0000244|PDB:4GGF}.
TURN 95 97 {ECO:0000244|PDB:4GGF}.
TURN 108 110 {ECO:0000244|PDB:5I8N}.
SEQUENCE 114 AA; 13242 MW; C3BE19729E14C078 CRC64;
MTCKMSQLER NIETIINTFH QYSVKLGHPD TLNQGEFKEL VRKDLQNFLK KENKNEKVIE
HIMEDLDTNA DKQLSFEEFI MLMARLTWAS HEKMHEGDEG PGHHHKPGLG EGTP


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