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

 S10A9_MOUSE             Reviewed;         113 AA.
P31725;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-FEB-2018, entry version 163.
RecName: Full=Protein S100-A9;
AltName: Full=Calgranulin-B;
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, Mrp14;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=1373330;
Lagasse E., Weissman I.L.;
"Mouse MRP8 and MRP14, two intracellular calcium-binding proteins
associated with the development of the myeloid lineage.";
Blood 79:1907-1915(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=11169745;
DOI=10.1002/1097-4644(20010315)80:4<606::AID-JCB1015>3.0.CO;2-K;
Nacken W.K.F., Lekstrom-Himes J.A., Sorg C., Manitz M.;
"Molecular analysis of the mouse S100A9 gene and evidence that the
myeloid specific transcription factor C/EBPepsilon is not required for
the regulation of the S100A9/A8 gene expression in neutrophils.";
J. Cell. Biochem. 80:606-616(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Mammary gland;
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).
[4]
PROTEIN SEQUENCE OF 2-10; 76-93 AND 95-109, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
PubMed=8645219; DOI=10.1042/bj3160285;
Raftery M.J., Harrison C.A., Alewood P.F., Jones A., Geczy C.L.;
"Isolation of the murine S100 protein MRP14 (14 kDa migration-
inhibitory-factor-related protein) from activated spleen cells:
characterization of post-translational modifications and zinc
binding.";
Biochem. J. 316:285-293(1996).
[5]
DISRUPTION PHENOTYPE.
PubMed=12529407; DOI=10.1128/MCB.23.3.1034-1043.2003;
Manitz M.-P., Horst B., Seeliger S., Strey A., Skryabin B.V.,
Gunzer M., Frings W., Schoenlau F., Roth J., Sorg C., Nacken W.;
"Loss of S100A9 (MRP14) results in reduced interleukin-8-induced CD11b
surface expression, a polarized microfilament system, and diminished
responsiveness to chemoattractants in vitro.";
Mol. Cell. Biol. 23:1034-1043(2003).
[6]
FUNCTION, INTERACTION WITH TUBULIN, AND PHOSPHORYLATION.
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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[8]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND
INTERACTION WITH TLR4 AND LY96.
PubMed=17767165; DOI=10.1038/nm1638;
Vogl T., Tenbrock K., Ludwig S., Leukert N., Ehrhardt C.,
van Zoelen M.A.D., Nacken W., Foell D., van der Poll T., Sorg C.,
Roth J.;
"Mrp8 and Mrp14 are endogenous activators of Toll-like receptor 4,
promoting lethal, endotoxin-induced shock.";
Nat. Med. 13:1042-1049(2007).
[9]
FUNCTION, AND INTERACTION WITH ATP2A2 AND AGER.
PubMed=18403730; DOI=10.1161/CIRCRESAHA.107.167544;
Boyd J.H., Kan B., Roberts H., Wang Y., Walley K.R.;
"S100A8 and S100A9 mediate endotoxin-induced cardiomyocyte dysfunction
via the receptor for advanced glycation end products.";
Circ. Res. 102:1239-1246(2008).
[10]
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).
[11]
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).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[13]
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).
[14]
FUNCTION.
PubMed=21382888; DOI=10.1161/CIRCULATIONAHA.110.985523;
Averill M.M., Barnhart S., Becker L., Li X., Heinecke J.W.,
Leboeuf R.C., Hamerman J.A., Sorg C., Kerkhoff C., Bornfeldt K.E.;
"S100A9 differentially modifies phenotypic states of neutrophils,
macrophages, and dendritic cells: implications for atherosclerosis and
adipose tissue inflammation.";
Circulation 123:1216-1226(2011).
[15]
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).
-!- 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 proinflammatory, 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. The iNOS-S100A8/A9 transnitrosylase complex
is proposed to direct selective inflammatory stimulus-dependent S-
nitrosylation of multiple targets such as GAPDH, NXA5, EZR, MSN
and VIM by recognizing a [IL]-x-C-x-x-[DE] motif (By similarity).
{ECO:0000250|UniProtKB:P06702, ECO:0000269|PubMed:15331440,
ECO:0000269|PubMed:17767165, ECO:0000269|PubMed:18403730,
ECO:0000269|PubMed:19402754, ECO:0000269|PubMed:21382888,
ECO:0000269|PubMed:22804476}.
-!- SUBUNIT: Homodimer. Preferentially exists as a heterodimer or
heterotetramer with S100A8 known as calprotectin (S100A8/A9).
S100A9 interacts with beta-APP40 (amyloid-beta protein 40) peptide
of APP (By similarity). S100A9 interacts with AGER and 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
ATP2A2. Calprotectin (S100A8/9) interacts with NCF2/P67PHOX, RAC1,
RAC2, CYBA and CYBB (By similarity). Heterotetrameric calprotectin
(S100A8/A9) interacts with ANXA6 and associates with tubulin
filaments in activated monocytes (By similarity). Calprotectin
(S100A8/9) interacts with CEACAM3 and tubulin filaments in a
calcium-dependent manner. Calprotectin (S100A8/9) interacts with
NOS2 to form the iNOS-S100A8/A9 transnitrosylase complex (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P06702,
ECO:0000269|PubMed:15331440, ECO:0000269|PubMed:17767165,
ECO:0000269|PubMed:18403730, ECO:0000269|PubMed:19402754}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm.
Cytoplasm, cytoskeleton. Cell membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}. 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.
-!- PTM: Phosphorylated. Phosphorylation inhibits activation of
tubulin polymerization (By similarity). {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=12972; Mass_error=2; Method=Electrospray;
Range=2-113; Evidence={ECO:0000269|PubMed:8645219};
-!- DISRUPTION PHENOTYPE: No visible phenotype. Alters response of
phagocytes to stimulation with bacterial lipopolysaccharide (LPS).
{ECO:0000269|PubMed:12529407, ECO:0000269|PubMed:17767165}.
-!- MISCELLANEOUS: Has been shown to bind calcium.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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EMBL; M83219; AAB07228.1; -; mRNA.
EMBL; AJ250496; CAC14292.1; -; Genomic_DNA.
EMBL; BC027635; AAH27635.1; -; mRNA.
CCDS; CCDS17543.1; -.
PIR; S68242; S68242.
RefSeq; NP_001268781.1; NM_001281852.1.
RefSeq; NP_033140.1; NM_009114.3.
UniGene; Mm.2128; -.
ProteinModelPortal; P31725; -.
SMR; P31725; -.
IntAct; P31725; 2.
MINT; P31725; -.
STRING; 10090.ENSMUSP00000070842; -.
iPTMnet; P31725; -.
PhosphoSitePlus; P31725; -.
PaxDb; P31725; -.
PeptideAtlas; P31725; -.
PRIDE; P31725; -.
Ensembl; ENSMUST00000069960; ENSMUSP00000070842; ENSMUSG00000056071.
Ensembl; ENSMUST00000117167; ENSMUSP00000112843; ENSMUSG00000056071.
GeneID; 20202; -.
KEGG; mmu:20202; -.
UCSC; uc008qde.2; mouse.
CTD; 6280; -.
MGI; MGI:1338947; S100a9.
eggNOG; ENOG410J1XC; Eukaryota.
eggNOG; ENOG4111C30; LUCA.
GeneTree; ENSGT00910000144230; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P31725; -.
KO; K21128; -.
OMA; DHIMEDL; -.
OrthoDB; EOG091G12NB; -.
PhylomeDB; P31725; -.
TreeFam; TF332727; -.
Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6799990; Metal sequestration by antimicrobial proteins.
ChiTaRS; S100a9; mouse.
PRO; PR:P31725; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000056071; -.
CleanEx; MM_S100A9; -.
ExpressionAtlas; P31725; baseline and differential.
Genevisible; P31725; MM.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005576; C:extracellular region; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
GO; GO:0050544; F:arachidonic acid binding; IEA:InterPro.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008017; F:microtubule binding; IEA:InterPro.
GO; GO:0050786; F:RAGE receptor binding; IEA:InterPro.
GO; GO:0035662; F:Toll-like receptor 4 binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0014002; P:astrocyte development; IGI:MGI.
GO; GO:0006914; P:autophagy; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0030595; P:leukocyte chemotaxis; IMP:MGI.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
GO; GO:0035821; P:modification of morphology or physiology of other organism; ISO:MGI.
GO; GO:0070488; P:neutrophil aggregation; ISS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IMP:UniProtKB.
GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISO:MGI.
GO; GO:0030194; P:positive regulation of blood coagulation; IMP:CACAO.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0002793; P:positive regulation of peptide secretion; IDA:MGI.
GO; GO:0045113; P:regulation of integrin biosynthetic process; IMP:MGI.
GO; GO:0006417; P:regulation of translation; IMP:UniProtKB.
InterPro; IPR011992; EF-hand-dom_pair.
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; PS50222; EF_HAND_2; 2.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
Acetylation; 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; Reference proteome; Repeat; Secreted;
Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8645219}.
CHAIN 2 113 Protein S100-A9.
/FTId=PRO_0000143998.
DOMAIN 13 48 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 55 90 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 24 37 1; low affinity. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 68 79 2; high affinity. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
METAL 21 21 Zinc. {ECO:0000250}.
METAL 31 31 Zinc. {ECO:0000250}.
METAL 92 92 Zinc. {ECO:0000250}.
METAL 96 96 Zinc. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:8645219}.
MOD_RES 107 107 Pros-methylhistidine.
{ECO:0000250|UniProtKB:P50116}.
SEQUENCE 113 AA; 13049 MW; F4DCFBD1A181F812 CRC64;
MANKAPSQME RSITTIIDTF HQYSRKEGHP DTLSKKEFRQ MVEAQLATFM KKEKRNEALI
NDIMEDLDTN QDNQLSFEEC MMLMAKLIFA CHEKLHENNP RGHGHSHGKG CGK


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GENTAUR France SARL
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Tel 01 43 25 01 50

Fax 01 43 25 01 60
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BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
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Support Karolina Elandt
Tel: 0035929830070
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San Jose, CA 95123
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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