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Protein S100-A9 (Calgranulin-B) (Migration inhibitory factor-related protein 14) (MRP-14) (p14) (Myeloid-related protein 14) (S100 calcium-binding protein A9)

 S10A9_RAT               Reviewed;         113 AA.
P50116; Q761U7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 140.
RecName: Full=Protein S100-A9;
AltName: Full=Calgranulin-B;
AltName: Full=Migration inhibitory factor-related protein 14;
Short=MRP-14;
Short=p14;
AltName: Full=Myeloid-related protein 14;
AltName: Full=S100 calcium-binding protein A9;
Name=S100a9; Synonyms=Mrp14;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Lewis/N; TISSUE=Peritoneal cavity;
PubMed=8343166; DOI=10.1006/bbrc.1993.1895;
Imamichi T., Uchida I., Wahl S.M., McCartney-Francis N.;
"Expression and cloning of migration inhibitory factor-related protein
(MRP)8 and MRP14 in arthritis-susceptible rats.";
Biochem. Biophys. Res. Commun. 194:819-825(1993).
[2]
PROTEIN SEQUENCE OF 2-57; 62-65 AND 72-113, MASS SPECTROMETRY,
ACETYLATION AT ALA-2, AND METHYLATION AT HIS-107.
TISSUE=Spleen;
PubMed=9570842; DOI=10.1006/abio.1997.2601;
Raftery M.J., Geczy C.L.;
"Identification of posttranslational modifications and cDNA sequencing
errors in the rat S100 proteins MRP8 and 14 using electrospray
ionization mass spectrometry.";
Anal. Biochem. 258:285-292(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-113, PROTEIN SEQUENCE OF 11-25; 38-67;
81-90 AND 94-112, FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
STRAIN=Wistar; TISSUE=Macrophage, and Peritoneal cavity;
PubMed=15153104; DOI=10.1111/j.1432-1033.2004.04129.x;
Shibata F., Miyama K., Shinoda F., Mizumoto J., Takano K.,
Nakagawa H.;
"Fibroblast growth-stimulating activity of S100A9 (MRP-14).";
Eur. J. Biochem. 271:2137-2143(2004).
[4]
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).
-!- 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. 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:15153104,
ECO:0000269|PubMed:21487906}.
-!- SUBUNIT: Homodimer. Preferentially exists as a heterodimer or
heterotetramer with S100A8 known as calprotectin (S100A8/A9).
S100A9 interacts with ATP2A2. 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
beta-APP40 (amyloid-beta protein 40) peptide of APP. 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 (By
similarity). Calprotectin (S100A8/9) interacts with NOS2 to form
the iNOS-S100A8/A9 transnitrosylase complex (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P06702}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm
{ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell
membrane {ECO:0000269|PubMed:21487906}; Peripheral membrane
protein {ECO:0000269|PubMed:21487906}. 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 (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed at sites of inflammation.
{ECO:0000269|PubMed:15153104, ECO:0000269|PubMed:8343166}.
-!- PTM: Phosphorylated. Phosphorylation inhibits activation of
tubulin polymerization (By similarity). {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=13069; Mass_error=2; Method=Electrospray;
Range=2-113; Evidence={ECO:0000269|PubMed:9570842};
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L18948; AAA18214.1; -; mRNA.
EMBL; AB118215; BAC82423.1; -; mRNA.
PIR; JN0686; JN0686.
RefSeq; NP_446039.1; NM_053587.1.
UniGene; Rn.6703; -.
ProteinModelPortal; P50116; -.
SMR; P50116; -.
STRING; 10116.ENSRNOP00000015351; -.
iPTMnet; P50116; -.
PhosphoSitePlus; P50116; -.
PaxDb; P50116; -.
PRIDE; P50116; -.
GeneID; 94195; -.
KEGG; rno:94195; -.
UCSC; RGD:620267; rat.
CTD; 6280; -.
RGD; 620267; S100a9.
eggNOG; ENOG410J1XC; Eukaryota.
eggNOG; ENOG4111C30; LUCA.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P50116; -.
KO; K21128; -.
OrthoDB; EOG091G12NB; -.
PhylomeDB; P50116; -.
TreeFam; TF332727; -.
PRO; PR:P50116; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P50116; RN.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0031012; C:extracellular matrix; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
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; ISO:RGD.
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:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0014002; P:astrocyte development; ISO:RGD.
GO; GO:0006914; P:autophagy; ISS:UniProtKB.
GO; GO:0002544; P:chronic inflammatory response; IEP:RGD.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0030595; P:leukocyte chemotaxis; ISO:RGD.
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:RGD.
GO; GO:0070488; P:neutrophil aggregation; ISS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; ISO:RGD.
GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISO:RGD.
GO; GO:0030194; P:positive regulation of blood coagulation; ISO:RGD.
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:0010976; P:positive regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
GO; GO:0002793; P:positive regulation of peptide secretion; ISO:RGD.
GO; GO:0045113; P:regulation of integrin biosynthetic process; ISO:RGD.
GO; GO:0006417; P:regulation of translation; ISO:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0010043; P:response to zinc ion; IEP:RGD.
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; 1.
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:9570842}.
CHAIN 2 113 Protein S100-A9.
/FTId=PRO_0000143999.
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:9570842}.
MOD_RES 107 107 Pros-methylhistidine.
{ECO:0000269|PubMed:9570842}.
CONFLICT 17 17 I -> Q (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 24 24 S -> C (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 106 106 S -> R (in Ref. 1; AAA18214).
{ECO:0000305}.
SEQUENCE 113 AA; 13145 MW; 6C3A0044A7AEC4FA CRC64;
MAAKTGSQLE RSISTIINVF HQYSRKYGHP DTLNKAEFKE MVNKDLPNFL KREKRNENLL
RDIMEDLDTN QDNQLSFEEC MMLMGKLIFA CHEKLHENNP RGHDHSHGKG CGK


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