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Protein S100-A8 (Calgranulin-A) (Migration inhibitory factor-related protein 8) (MRP-8) (p8) (S100 calcium-binding protein A8)

 S10A8_RAT               Reviewed;          89 AA.
P50115;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 140.
RecName: Full=Protein S100-A8;
AltName: Full=Calgranulin-A;
AltName: Full=Migration inhibitory factor-related protein 8;
Short=MRP-8;
Short=p8;
AltName: Full=S100 calcium-binding protein A8;
Name=S100a8; Synonyms=Mrp8;
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].
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 2-89, MASS SPECTROMETRY, AND ACETYLATION AT ALA-2.
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]
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: 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 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, ANXA5, EZR, MSN
and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to
contribute to S-nitrosylation site selectivity (By similarity).
{ECO:0000250|UniProtKB:P05109, ECO:0000269|PubMed:21487906}.
-!- 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. 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 (By
similarity). Calprotectin (S100A8/9) interacts with NOS2 to form
the iNOS-S100A8/A9 transnitrosylase complex (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P05109}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm
{ECO:0000269|PubMed:21487906}. Cytoplasm, cytoskeleton
{ECO:0000250}. 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 (By similarity). {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=10149; Mass_error=2; Method=Electrospray;
Range=2-89; Evidence={ECO:0000269|PubMed:9570842};
-!- MISCELLANEOUS: Binds two calcium ions per molecule with an
affinity similar to that of the S100 proteins. {ECO:0000250}.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; L18891; AAA41637.1; -; mRNA.
PIR; JN0685; JN0685.
RefSeq; NP_446274.2; NM_053822.2.
RefSeq; XP_006232627.1; XM_006232565.3.
UniGene; Rn.31839; -.
ProteinModelPortal; P50115; -.
SMR; P50115; -.
STRING; 10116.ENSRNOP00000015473; -.
iPTMnet; P50115; -.
PaxDb; P50115; -.
PRIDE; P50115; -.
Ensembl; ENSRNOT00000015473; ENSRNOP00000015473; ENSRNOG00000011557.
GeneID; 116547; -.
KEGG; rno:116547; -.
CTD; 6279; -.
RGD; 620265; S100a8.
eggNOG; ENOG410J2UM; Eukaryota.
eggNOG; ENOG4111CN5; LUCA.
GeneTree; ENSGT00910000144329; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P50115; -.
KO; K21127; -.
OMA; IKGNYHA; -.
OrthoDB; EOG091G13NB; -.
PhylomeDB; P50115; -.
TreeFam; TF332727; -.
Reactome; R-RNO-6798695; Neutrophil degranulation.
Reactome; R-RNO-6799990; Metal sequestration by antimicrobial proteins.
PRO; PR:P50115; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000011557; -.
Genevisible; P50115; RN.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
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:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0002526; P:acute inflammatory response; IEP:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006914; P:autophagy; ISS:UniProtKB.
GO; GO:0002544; P:chronic inflammatory response; IEP:RGD.
GO; GO:0006954; P:inflammatory response; NAS:RGD.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
GO; GO:0070488; P:neutrophil aggregation; ISS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IEA:Ensembl.
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: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.
GO; GO:0042060; P:wound healing; IEP:RGD.
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:SF5; PTHR11639:SF5; 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;
Acetylation; Antimicrobial; Antioxidant; 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.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9570842}.
CHAIN 2 89 Protein S100-A8.
/FTId=PRO_0000143995.
DOMAIN 13 48 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. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 59 70 2; high affinity. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
METAL 17 17 Zinc. {ECO:0000250}.
METAL 27 27 Zinc. {ECO:0000250}.
METAL 83 83 Zinc. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:9570842}.
MOD_RES 42 42 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P05109}.
CONFLICT 73 73 V -> A (in Ref. 1; AAA41637).
{ECO:0000305}.
SEQUENCE 89 AA; 10239 MW; 6AC1AFAF3429B01E CRC64;
MATELEKALS NVIEVYHNYS GIKGNHHALY RDDFRKMVTT ECPQFVQNKN TESLFKELDV
NSDNAINFEE FLVLVIRVGV AAHKDSHKE


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