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S10A8_BOVIN
ID   S10A8_BOVIN             Reviewed;          89 AA.
AC   P28782; Q2NKR8;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Protein S100-A8;
DE   AltName: Full=BEE11;
DE   AltName: Full=Calgranulin-A;
DE   AltName: Full=Neutrophil cytosolic 7 kDa protein;
DE            Short=P7;
DE   AltName: Full=S100 calcium-binding protein A8;
GN   Name=S100A8;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 1-41.
RC   TISSUE=Neutrophil;
RX   PubMed=1610833; DOI=10.1021/bi00140a028;
RA   Dianoux A.-C., Stasia M.-J., Garin J., Gagnon J., Vignais P.V.;
RT   "The 23-kilodalton protein, a substrate of protein kinase C, in bovine
RT   neutrophil cytosol is a member of the S100 family.";
RL   Biochemistry 31:5898-5905(1992).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-29.
RC   TISSUE=Esophageal epithelium;
RX   PubMed=8505358; DOI=10.1242/jcs.104.2.237;
RA   Tang T.K., Hong T.-M., Lin C.-Y., Lai M.-L., Liu C.H.L., Lo H.-J.,
RA   Wang M.-E., Chen L.B., Chen W.-T., Ip W., Lin D.C., Lin J.J.-C., Lin S.,
RA   Sun T.-T., Wang E., Wang J.L., Wu R., Wu C.-W., Chien S.;
RT   "Nuclear proteins of the bovine esophageal epithelium. I. Monoclonal
RT   antibody W2 specifically reacts with condensed nuclei of differentiated
RT   superficial cells.";
RL   J. Cell Sci. 104:237-247(1993).
CC   -!- FUNCTION: S100A8 is a calcium- and zinc-binding protein which plays a
CC       prominent role in the regulation of inflammatory processes and immune
CC       response. It can induce neutrophil chemotaxis and adhesion.
CC       Predominantly found as calprotectin (S100A8/A9) which has a wide
CC       plethora of intra- and extracellular functions. The intracellular
CC       functions include: facilitating leukocyte arachidonic acid trafficking
CC       and metabolism, modulation of the tubulin-dependent cytoskeleton during
CC       migration of phagocytes and activation of the neutrophilic NADPH-
CC       oxidase. Activates NADPH-oxidase by facilitating the enzyme complex
CC       assembly at the cell membrane, transferring arachidonic acid, an
CC       essential cofactor, to the enzyme complex and S100A8 contributes to the
CC       enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular
CC       functions involve pro-inflammatory, antimicrobial, oxidant-scavenging
CC       and apoptosis-inducing activities. Its pro-inflammatory activity
CC       includes recruitment of leukocytes, promotion of cytokine and chemokine
CC       production, and regulation of leukocyte adhesion and migration. Acts as
CC       an alarmin or a danger associated molecular pattern (DAMP) molecule and
CC       stimulates innate immune cells via binding to pattern recognition
CC       receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced
CC       glycation endproducts (AGER). Binding to TLR4 and AGER activates the
CC       MAP-kinase and NF-kappa-B signaling pathways resulting in the
CC       amplification of the pro-inflammatory cascade. Has antimicrobial
CC       activity towards bacteria and fungi and exerts its antimicrobial
CC       activity probably via chelation of Zn(2+) which is essential for
CC       microbial growth. Can induce cell death via autophagy and apoptosis and
CC       this occurs through the cross-talk of mitochondria and lysosomes via
CC       reactive oxygen species (ROS) and the process involves BNIP3. Can
CC       regulate neutrophil number and apoptosis by an anti-apoptotic effect;
CC       regulates cell survival via ITGAM/ITGB and TLR4 and a signaling
CC       mechanism involving MEK-ERK. Its role as an oxidant scavenger has a
CC       protective role in preventing exaggerated tissue damage by scavenging
CC       oxidants (By similarity). The iNOS-S100A8/A9 transnitrosylase complex
CC       is proposed to direct selective inflammatory stimulus-dependent S-
CC       nitrosylation of multiple targets such as GAPDH, ANXA5, EZR, MSN and
CC       VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to
CC       contribute to S-nitrosylation site selectivity (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:P05109}.
CC   -!- SUBUNIT: Homodimer. Preferentially exists as a heterodimer or
CC       heterotetramer with S100A9 known as calprotectin (S100A8/A9). S100A8
CC       interacts with AGER, ATP2A2 and with the heterodimeric complex formed
CC       by TLR4 and LY96. Calprotectin (S100A8/9) interacts with CEACAM3 and
CC       tubulin filaments in a calcium-dependent manner. Heterotetrameric
CC       calprotectin (S100A8/A9) interacts with ANXA6 and associates with
CC       tubulin filaments in activated monocytes. S100A8 and calprotectin
CC       (S100A8/9) interact with NCF2/P67PHOX, RAC1 and RAC2. Calprotectin
CC       (S100A8/9) interacts with CYBA and CYBB (By similarity). Calprotectin
CC       (S100A8/9) interacts with NOS2 to form the iNOS-S100A8/A9
CC       transnitrosylase complex (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:P05109}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Note=Predominantly localized
CC       in the cytoplasm. Upon elevation of the intracellular calcium level,
CC       translocated from the cytoplasm to the cytoskeleton and the cell
CC       membrane. Upon neutrophil activation or endothelial adhesion of
CC       monocytes, is secreted via a microtubule-mediated, alternative pathway
CC       (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Found essentially in phagocytic cells.
CC   -!- MISCELLANEOUS: Binds two calcium ions per molecule with an affinity
CC       similar to that of the S100 proteins. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR   EMBL; BC111678; AAI11679.1; -; mRNA.
DR   PIR; B42628; B42628.
DR   RefSeq; NP_001107197.1; NM_001113725.2.
DR   AlphaFoldDB; P28782; -.
DR   SMR; P28782; -.
DR   STRING; 9913.ENSBTAP00000016774; -.
DR   PaxDb; P28782; -.
DR   PeptideAtlas; P28782; -.
DR   PRIDE; P28782; -.
DR   Ensembl; ENSBTAT00000016774; ENSBTAP00000016774; ENSBTAG00000012640.
DR   Ensembl; ENSBTAT00000066555; ENSBTAP00000074498; ENSBTAG00000012640.
DR   GeneID; 616818; -.
DR   KEGG; bta:616818; -.
DR   CTD; 6279; -.
DR   VEuPathDB; HostDB:ENSBTAG00000012640; -.
DR   VGNC; VGNC:34246; S100A8.
DR   eggNOG; ENOG502SA01; Eukaryota.
DR   GeneTree; ENSGT00910000144329; -.
DR   HOGENOM; CLU_138624_6_0_1; -.
DR   InParanoid; P28782; -.
DR   OMA; YHKYSLE; -.
DR   OrthoDB; 1613717at2759; -.
DR   TreeFam; TF332727; -.
DR   Reactome; R-BTA-5668599; RHO GTPases Activate NADPH Oxidases.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000012640; Expressed in anterior segment of eyeball and 92 other tissues.
DR   ExpressionAtlas; P28782; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR   GO; GO:0050544; F:arachidonic acid binding; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0050786; F:RAGE receptor binding; IEA:InterPro.
DR   GO; GO:0035662; F:Toll-like receptor 4 binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR   GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0002523; P:leukocyte migration involved in inflammatory response; ISS:UniProtKB.
DR   GO; GO:0070488; P:neutrophil aggregation; ISS:UniProtKB.
DR   GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR   GO; GO:0002790; P:peptide secretion; IEA:Ensembl.
DR   GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IEA:Ensembl.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR   GO; GO:0002793; P:positive regulation of peptide secretion; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   InterPro; IPR028474; S100A8.
DR   PANTHER; PTHR11639:SF5; PTHR11639:SF5; 1.
DR   Pfam; PF00036; EF-hand_1; 1.
DR   Pfam; PF01023; S_100; 1.
DR   SMART; SM00054; EFh; 1.
DR   SMART; SM01394; S_100; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS00303; S100_CABP; 1.
PE   1: Evidence at protein level;
KW   Antimicrobial; Antioxidant; Apoptosis; Autophagy; Calcium; Cell membrane;
KW   Chemotaxis; Cytoplasm; Cytoskeleton; Direct protein sequencing; Immunity;
KW   Inflammatory response; Innate immunity; Membrane; Metal-binding;
KW   Reference proteome; Repeat; S-nitrosylation; Secreted; Zinc.
FT   CHAIN           1..89
FT                   /note="Protein S100-A8"
FT                   /id="PRO_0000143992"
FT   DOMAIN          12..47
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          46..81
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         33
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="low affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         61
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         70
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /ligand_note="high affinity"
FT                   /evidence="ECO:0000305"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         42
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P05109"
FT   CONFLICT        10
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        11
FT                   /note="S -> I (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   89 AA;  10460 MW;  5A4BB9E2705732F0 CRC64;
     MLTDLECAIN SLIDVYHKYS LKKGNYHAVY RDDLKQLLET ECPKFMKKKD ADTWFKELDI
     NQDGGINFEE FLVLVIKVGL EAHEEIHKE
 
 
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