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Cathepsin G (EC 3.4.21.20) (Vimentin-specific protease) (VSP)

 CATG_MOUSE              Reviewed;         261 AA.
P28293;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
22-NOV-2017, entry version 142.
RecName: Full=Cathepsin G;
EC=3.4.21.20;
AltName: Full=Vimentin-specific protease;
Short=VSP;
Flags: Precursor;
Name=Ctsg;
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 [GENOMIC DNA].
STRAIN=Swiss Webster; TISSUE=Embryonic fibroblast;
PubMed=8453108;
Heusel J.W., Scarpati E.M., Jenkins N.A., Gilbert D.J., Copeland N.G.,
Shapiro S.D., Ley T.J.;
"Molecular cloning, chromosomal location, and tissue-specific
expression of the murine cathepsin G gene.";
Blood 81:1614-1623(1993).
[2]
NUCLEOTIDE SEQUENCE.
Kulmburg P., Baumruker T., Werner F.;
Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE.
STRAIN=Leaden X A1;
Huang R., Aveskogh M., Hellman L.T.;
Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 21-60.
PubMed=1577012; DOI=10.1111/j.1432-1033.1992.tb16861.x;
Nakamura N., Tsuru A., Hirayoshi K., Nagata K.;
"Purification and characterization of a vimentin-specific protease in
mouse myeloid leukemia cells. Regulation during differentiation and
identity with cathepsin G.";
Eur. J. Biochem. 205:947-954(1992).
-!- FUNCTION: This vimentin-specific protease may regulate the
reorganization of vimentin filaments, occurring during cell
differentiation, movement and mitosis.
-!- CATALYTIC ACTIVITY: Specificity similar to chymotrypsin C.
-!- SUBCELLULAR LOCATION: Membrane. Note=Strongly associated with
membranes.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; M96801; AAA37376.1; -; Genomic_DNA.
EMBL; X70057; CAA49661.1; -; Genomic_DNA.
EMBL; X78544; CAA55290.1; -; mRNA.
CCDS; CCDS27142.1; -.
PIR; S40162; S40162.
RefSeq; NP_031826.1; NM_007800.2.
UniGene; Mm.4858; -.
ProteinModelPortal; P28293; -.
SMR; P28293; -.
STRING; 10090.ENSMUSP00000015583; -.
BindingDB; P28293; -.
ChEMBL; CHEMBL5622; -.
MEROPS; S01.133; -.
PhosphoSitePlus; P28293; -.
PaxDb; P28293; -.
PeptideAtlas; P28293; -.
PRIDE; P28293; -.
Ensembl; ENSMUST00000015583; ENSMUSP00000015583; ENSMUSG00000040314.
GeneID; 13035; -.
KEGG; mmu:13035; -.
UCSC; uc007ubn.1; mouse.
CTD; 1511; -.
MGI; MGI:88563; Ctsg.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118895; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P28293; -.
KO; K01319; -.
OMA; ICVGDRR; -.
OrthoDB; EOG091G0G5F; -.
PhylomeDB; P28293; -.
TreeFam; TF333630; -.
Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6803157; Antimicrobial peptides.
PRO; PR:P28293; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000040314; -.
CleanEx; MM_CTSG; -.
ExpressionAtlas; P28293; baseline and differential.
Genevisible; P28293; MM.
GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0030141; C:secretory granule; ISO:MGI.
GO; GO:0008201; F:heparin binding; ISO:MGI.
GO; GO:0008233; F:peptidase activity; ISO:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
GO; GO:0008236; F:serine-type peptidase activity; ISO:MGI.
GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
GO; GO:0050832; P:defense response to fungus; IMP:MGI.
GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:MGI.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IMP:MGI.
GO; GO:0070946; P:neutrophil mediated killing of gram-positive bacterium; IMP:MGI.
GO; GO:0050778; P:positive regulation of immune response; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Intermediate filament; Membrane; Protease;
Reference proteome; Serine protease; Signal; Zymogen.
SIGNAL 1 18 {ECO:0000250}.
PROPEP 19 20 Activation peptide.
{ECO:0000269|PubMed:1577012}.
/FTId=PRO_0000027514.
CHAIN 21 261 Cathepsin G.
/FTId=PRO_0000027515.
DOMAIN 21 243 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 64 64 Charge relay system. {ECO:0000250}.
ACT_SITE 108 108 Charge relay system. {ECO:0000250}.
ACT_SITE 201 201 Charge relay system. {ECO:0000250}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 49 65 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 142 207 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 172 186 {ECO:0000255|PROSITE-ProRule:PRU00274}.
CONFLICT 51 51 G -> S (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 56 56 E -> G (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 60 60 L -> P (in Ref. 4; AA sequence).
{ECO:0000305}.
SEQUENCE 261 AA; 29096 MW; 5EFA1A6E10E1D7FC CRC64;
MQPLLLLLTF ILLQGDEAGK IIGGREARPH SYPYMAFLLI QSPEGLSACG GFLVREDFVL
TAAHCLGSSI NVTLGAHNIQ MRERTQQLIT VLRAIRHPDY NPQNIRNDIM LLQLRRRARR
SGSVKPVALP QASKKLQPGD LCTVAGWGRV SQSRGTNVLQ EVQLRVQMDQ MCANRFQFYN
SQTQICVGNP RERKSAFRGD SGGPLVCSNV AQGIVSYGSN NGNPPAVFTK IQSFMPWIKR
TMRRFAPRYQ RPANSLSQAQ T


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