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Cathepsin G (CG) (EC 3.4.21.20)

 CATG_HUMAN              Reviewed;         255 AA.
P08311; Q6IBJ6; Q9UCA5; Q9UCU6;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 2.
20-JUN-2018, entry version 182.
RecName: Full=Cathepsin G;
Short=CG;
EC=3.4.21.20;
Flags: Precursor;
Name=CTSG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3304423; DOI=10.1021/bi00382a032;
Salvesen G., Farley D., Shuman J., Przybyla A., Reilly C., Travis J.;
"Molecular cloning of human cathepsin G: structural similarity to mast
cell and cytotoxic T lymphocyte proteinases.";
Biochemistry 26:2289-2293(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2569462;
Hohn P.A., Popescu N.C., Hanson R.D., Salvesen G., Ley T.J.;
"Genomic organization and chromosomal localization of the human
cathepsin G gene.";
J. Biol. Chem. 264:13412-13419(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
[6]
PROTEIN SEQUENCE OF 21-52, FUNCTION, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
TISSUE=Monocyte;
PubMed=8194606; DOI=10.1016/0014-5793(94)00410-2;
Avril L.E., Di Martino-Ferrer M., Pignede G., Seman M., Gauthier F.;
"Identification of the U-937 membrane-associated proteinase
interacting with the V3 loop of HIV-1 gp120 as cathepsin G.";
FEBS Lett. 345:81-86(1994).
[7]
PROTEIN SEQUENCE OF 21-45.
PubMed=3799965; DOI=10.1016/0003-2697(86)90612-3;
Heck L.W., Rostand K.S., Hunter F.A., Bhown A.;
"Isolation, characterization, and amino-terminal amino acid sequence
analysis of human neutrophil cathepsin G from normal donors.";
Anal. Biochem. 158:217-227(1986).
[8]
PROTEIN SEQUENCE OF 21-36.
PubMed=2501794; DOI=10.1073/pnas.86.14.5610;
Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C.,
Marra M.N., Seeger M., Nathan C.F.;
"Antibiotic proteins of human polymorphonuclear leukocytes.";
Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
[9]
PROTEIN SEQUENCE OF 21-30, FUNCTION, AND ENZYME REGULATION.
TISSUE=Monocyte;
PubMed=1861080;
Maison C.M., Villiers C.L., Colomb M.G.;
"Proteolysis of C3 on U937 cell plasma membranes. Purification of
cathepsin G.";
J. Immunol. 147:921-926(1991).
[10]
PROTEIN SEQUENCE OF 21-30.
TISSUE=Neutrophil;
PubMed=7897245; DOI=10.1016/0022-1759(94)00295-8;
Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.;
"Use of proteinase 3 purified by reverse phase HPLC to detect
autoantibodies in systemic vasculitis.";
J. Immunol. Methods 180:25-33(1995).
[11]
FUNCTION AS A MICROBICIDE, AND ENZYME REGULATION.
PubMed=1937776;
Wasiluk K.R., Skubitz K.M., Gray B.H.;
"Comparison of granule proteins from human polymorphonuclear
leukocytes which are bactericidal toward Pseudomonas aeruginosa.";
Infect. Immun. 59:4193-4200(1991).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
ENZYME REGULATION (MICROBIAL INFECTION), INTERACTION WITH
M.TUBERCULOSIS RV3364C (MICROBIAL INFECTION), AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=22275911; DOI=10.3389/fmicb.2011.00281;
Danelishvili L., Everman J.L., McNamara M.J., Bermudez L.E.;
"Inhibition of the plasma-membrane-associated serine protease
cathepsin G by Mycobacterium tuberculosis Rv3364c suppresses caspase-1
and pyroptosis in macrophages.";
Front. Microbiol. 2:281-281(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=8896442;
Hof P., Mayr I., Huber R., Korzus E., Potempa J., Travis J.,
Powers J.C., Bode W.;
"The 1.8 A crystal structure of human cathepsin G in complex with Suc-
Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite
specificities.";
EMBO J. 15:5481-5491(1996).
[16]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medrano F.J., Bode W., Banbula A., Potempa J.;
Submitted (SEP-1997) to the PDB data bank.
[17]
VARIANT SER-125.
PubMed=8454293; DOI=10.1007/BF00230230;
Luedecke B., Poller W., Olek K., Bartholome K.;
"Sequence variant of the human cathepsin G gene.";
Hum. Genet. 91:83-84(1993).
-!- FUNCTION: Serine protease with trypsin- and chymotrypsin-like
specificity. Cleaves complement C3. Has antibacterial activity
against the Gram-negative bacterium P.aeruginosa, antibacterial
activity is inhibited by LPS from P.aeruginosa, Z-Gly-Leu-Phe-
CH2Cl and phenylmethylsulfonyl fluoride.
{ECO:0000269|PubMed:1861080, ECO:0000269|PubMed:1937776,
ECO:0000269|PubMed:8194606}.
-!- CATALYTIC ACTIVITY: Specificity similar to chymotrypsin C.
-!- ENZYME REGULATION: Inhibited by soybean trypsin inhibitor,
benzamidine, the synthetic peptide R13K, Z-Gly-Leu-Phe-CH2Cl,
phenylmethylsulfonyl fluoride, 3,4-dichloroisocoumarin, DFP, SBTI
and alpha-1-antitrypsin. Inhibited by LPS from P.aeruginosa but
not by LPS from S.minnesota. Not inhibited by elastinal, CMK, TLCK
and ETDA. {ECO:0000269|PubMed:1861080, ECO:0000269|PubMed:1937776,
ECO:0000269|PubMed:8194606}.
-!- ENZYME REGULATION: (Microbial infection) Serine protease activity
is inhibited by the M.tuberculosis protein Rv3364c, which leads to
the suppression of downstream caspase-1-dependent apoptosis in
macrophages. {ECO:0000269|PubMed:22275911}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.15 mM for Z-Lys-SBzl {ECO:0000269|PubMed:8194606};
KM=0.26 mM for Suc-Ala-Ala-Pro-Phe-SBzl
{ECO:0000269|PubMed:8194606};
-!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis
protein Rv3364c. {ECO:0000269|PubMed:22275911}.
-!- INTERACTION:
Q15323:KRT31; NbExp=3; IntAct=EBI-5462635, EBI-948001;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-5462635, EBI-945833;
-!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:8194606}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; M16117; AAA52126.1; -; mRNA.
EMBL; J04990; AAA51919.1; -; Genomic_DNA.
EMBL; CR456807; CAG33088.1; -; mRNA.
EMBL; CR541704; CAG46505.1; -; mRNA.
EMBL; CH471078; EAW66006.1; -; Genomic_DNA.
EMBL; BC014460; AAH14460.1; -; mRNA.
CCDS; CCDS9631.1; -.
PIR; A32627; A27122.
RefSeq; NP_001902.1; NM_001911.2.
UniGene; Hs.421724; -.
PDB; 1AU8; X-ray; 1.90 A; A=21-244.
PDB; 1CGH; X-ray; 1.80 A; A=21-244.
PDB; 1KYN; X-ray; 3.50 A; A/B=21-255.
PDB; 1T32; X-ray; 1.85 A; A=21-244.
PDBsum; 1AU8; -.
PDBsum; 1CGH; -.
PDBsum; 1KYN; -.
PDBsum; 1T32; -.
ProteinModelPortal; P08311; -.
SMR; P08311; -.
BioGrid; 107891; 17.
CORUM; P08311; -.
IntAct; P08311; 6.
MINT; P08311; -.
STRING; 9606.ENSP00000216336; -.
BindingDB; P08311; -.
ChEMBL; CHEMBL4071; -.
DrugBank; DB04016; 2-[3-({Methyl[1-(2-Naphthoyl)Piperidin-4-Yl]Amino}Carbonyl)-2-Naphthyl]-1-(1-Naphthyl)-2-Oxoethylphosphonic Acid.
DrugBank; DB02360; Bis-Napthyl Beta-Ketophosphonic Acid.
GuidetoPHARMACOLOGY; 2348; -.
MEROPS; S01.133; -.
iPTMnet; P08311; -.
PhosphoSitePlus; P08311; -.
BioMuta; CTSG; -.
DMDM; 115725; -.
EPD; P08311; -.
MaxQB; P08311; -.
PaxDb; P08311; -.
PeptideAtlas; P08311; -.
PRIDE; P08311; -.
ProteomicsDB; 12623; -.
ProteomicsDB; 52105; -.
TopDownProteomics; P08311; -.
DNASU; 1511; -.
Ensembl; ENST00000216336; ENSP00000216336; ENSG00000100448.
GeneID; 1511; -.
KEGG; hsa:1511; -.
UCSC; uc001wpq.4; human.
CTD; 1511; -.
DisGeNET; 1511; -.
EuPathDB; HostDB:ENSG00000100448.3; -.
GeneCards; CTSG; -.
HGNC; HGNC:2532; CTSG.
HPA; CAB000110; -.
HPA; HPA047737; -.
MIM; 116830; gene.
neXtProt; NX_P08311; -.
OpenTargets; ENSG00000100448; -.
PharmGKB; PA27032; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118895; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; P08311; -.
KO; K01319; -.
OMA; ICVGDRR; -.
OrthoDB; EOG091G0G5F; -.
PhylomeDB; P08311; -.
TreeFam; TF333630; -.
BRENDA; 3.4.21.20; 2681.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6803157; Antimicrobial peptides.
SABIO-RK; P08311; -.
EvolutionaryTrace; P08311; -.
GeneWiki; Cathepsin_G; -.
GenomeRNAi; 1511; -.
PMAP-CutDB; P08311; -.
PRO; PR:P08311; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100448; -.
CleanEx; HS_CTSG; -.
Genevisible; P08311; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030141; C:secretory granule; IDA:MGI.
GO; GO:0008201; F:heparin binding; IDA:MGI.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008236; F:serine-type peptidase activity; IMP:UniProtKB.
GO; GO:0002003; P:angiotensin maturation; TAS:Reactome.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0050832; P:defense response to fungus; IBA:GO_Central.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0070946; P:neutrophil mediated killing of gram-positive bacterium; IBA:GO_Central.
GO; GO:0050778; P:positive regulation of immune response; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IDA:CACAO.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
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;
3D-structure; Antibiotic; Antimicrobial; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Polymorphism; Protease; Reference proteome; Serine protease; Signal;
Zymogen.
SIGNAL 1 18
PROPEP 19 20 Activation peptide.
{ECO:0000269|PubMed:1861080,
ECO:0000269|PubMed:2501794,
ECO:0000269|PubMed:3799965,
ECO:0000269|PubMed:7897245,
ECO:0000269|PubMed:8194606}.
/FTId=PRO_0000027512.
CHAIN 21 255 Cathepsin G.
/FTId=PRO_0000027513.
DOMAIN 21 243 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 64 64 Charge relay system.
ACT_SITE 108 108 Charge relay system.
ACT_SITE 201 201 Charge relay system.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
DISULFID 49 65
DISULFID 142 207
DISULFID 172 186
VARIANT 125 125 N -> S (in dbSNP:rs45567233).
{ECO:0000269|PubMed:8454293}.
/FTId=VAR_006491.
STRAND 35 41 {ECO:0000244|PDB:1CGH}.
TURN 42 45 {ECO:0000244|PDB:1CGH}.
STRAND 48 55 {ECO:0000244|PDB:1CGH}.
STRAND 58 61 {ECO:0000244|PDB:1CGH}.
HELIX 63 65 {ECO:0000244|PDB:1CGH}.
STRAND 68 75 {ECO:0000244|PDB:1CGH}.
STRAND 87 96 {ECO:0000244|PDB:1CGH}.
TURN 102 105 {ECO:0000244|PDB:1CGH}.
STRAND 110 116 {ECO:0000244|PDB:1CGH}.
STRAND 141 147 {ECO:0000244|PDB:1CGH}.
STRAND 150 153 {ECO:0000244|PDB:1CGH}.
STRAND 160 166 {ECO:0000244|PDB:1CGH}.
HELIX 169 175 {ECO:0000244|PDB:1CGH}.
TURN 181 183 {ECO:0000244|PDB:1CGH}.
STRAND 184 187 {ECO:0000244|PDB:1CGH}.
STRAND 204 207 {ECO:0000244|PDB:1CGH}.
STRAND 210 217 {ECO:0000244|PDB:1CGH}.
STRAND 226 230 {ECO:0000244|PDB:1CGH}.
HELIX 231 234 {ECO:0000244|PDB:1CGH}.
HELIX 235 243 {ECO:0000244|PDB:1CGH}.
SEQUENCE 255 AA; 28837 MW; 6228E741E6A43889 CRC64;
MQPLLLLLAF LLPTGAEAGE IIGGRESRPH SRPYMAYLQI QSPAGQSRCG GFLVREDFVL
TAAHCWGSNI NVTLGAHNIQ RRENTQQHIT ARRAIRHPQY NQRTIQNDIM LLQLSRRVRR
NRNVNPVALP RAQEGLRPGT LCTVAGWGRV SMRRGTDTLR EVQLRVQRDR QCLRIFGSYD
PRRQICVGDR RERKAAFKGD SGGPLLCNNV AHGIVSYGKS SGVPPEVFTR VSSFLPWIRT
TMRSFKLLDQ METPL


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