CTSG
entrez
1511
canonical
uniprot
P08311
canonical
ensembl
ENSG00000100448
resolver
ensp
ENSP00000216336
resolver
ensp
ENSP00000541593
resolver
enst
ENST00000216336
resolver
genesymbol
CTSG
resolver
hgnc
HGNC:2532
resolver
uniprot
Q6IBJ6
resolver
uniprot
Q9UCA5
resolver
uniprot
Q9UCU6
resolver
uniprot_entry
CATG_HUMAN
resolver
uniprot_sec
Q6IBJ6
resolver
uniprot_sec
Q9UCA5
resolver
uniprot_sec
Q9UCU6
resolver
activity_regulation
ACTIVITY 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, ETDA or leupeptin. {ECO:0000269|PubMed:1861080, ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:3390156, ECO:0000269|PubMed:8194606}.; ACTIVITY REGULATION: (Microbial infection) Activity is induced by the Td92 surface protein of the periodontal pathogen T.denticola. {ECO:0000269|PubMed:29077095}.
uniprot
proteins
amino_acid_sequence
MQPLLLLLAFLLPTGAEAGEIIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNINVTLGAHNIQRRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYDPRRQICVGDRRERKAAFKGDSGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRSFKLLDQMETPL
uniprot
proteins
ec_number
3.4.21.20
uniprot
proteins
function
FUNCTION: Serine protease with trypsin- and chymotrypsin-like specificity (PubMed:29652924, PubMed:8194606). Also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity (PubMed:2116408, PubMed:2117044). Prefers Phe and Tyr residues in the P1 position of substrates but also cleaves efficiently after Trp and Leu (PubMed:29652924). Shows a preference for negatively charged amino acids in the P2' position and for aliphatic amino acids both upstream and downstream of the cleavage site (PubMed:29652924). Required for recruitment and activation of platelets which is mediated by the F2RL3/PAR4 platelet receptor (PubMed:10702240, PubMed:3390156). Binds reversibly to and stimulates B cells and CD4(+) and CD8(+) T cells (PubMed:7842483, PubMed:9000539). Also binds reversibly to natural killer (NK) cells and enhances NK cell cytotoxicity through its protease activity (PubMed:9000539, PubMed:9536127). Cleaves complement C3 (PubMed:1861080). Cleaves vimentin (By similarity). Cleaves thrombin receptor F2R/PAR1 and acts as either an agonist or an inhibitor, depending on the F2R cleavage site (PubMed:10702240, PubMed:7744748). Cleavage of F2R at '41-Arg-|-Ser-42' results in receptor activation while cleavage at '55-Phe-|-Trp-56' results in inhibition of receptor activation (PubMed:7744748). Cleaves the synovial mucin-type protein PRG4/lubricin (PubMed:32144329). Cleaves and activates IL36G which promotes expression of chemokines CXCL1 and CXLC8 in keratinocytes (PubMed:30804664). Cleaves IL33 into mature forms which have greater activity than the unprocessed form (PubMed:22307629). Cleaves coagulation factor F8 to produce a partially activated form (PubMed:18217133). Also cleaves and activates coagulation factor F10 (PubMed:8920993). Cleaves leukocyte cell surface protein SPN/CD43 to release its extracellular domain and trigger its intramembrane proteolysis by gamma-secretase, releasing the CD43 cytoplasmic tail chain (CD43-ct) which translocates to the nucleus (PubMed:18586676). Cleaves CCL5/RANTES to produce RANTES(4-68) lacking the N-terminal three amino acids which exhibits reduced chemotactic and antiviral activities (PubMed:16963625). During apoptosis, cleaves SMARCA2/BRM to produce a 160 kDa cleavage product which localizes to the cytosol (PubMed:11259672). Cleaves myelin basic protein MBP in B cell lysosomes at '224-Phe-|-Lys-225' and '248-Phe-|-Ser-249', degrading the major immunogenic MBP epitope and preventing the activation of MBP-specific autoreactive T cells (PubMed:15100291). Cleaves annexin ANXA1 and antimicrobial peptide CAMP to produce peptides which act on neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). Acts as a ligand for the N-formyl peptide receptor FPR1, enhancing phagocyte chemotaxis (PubMed:15210802). Has antibacterial activity against the Gram-negative bacteria N.gonorrhoeae and P.aeruginosa (PubMed:1937776, PubMed:2116408). Likely to act against N.gonorrhoeae by interacting with N.gonorrhoeae penA/PBP2 (PubMed:2126324). Exhibits potent antimicrobial activity against the Gram-positive bacterium L.monocytogenes (PubMed:2117044). Has antibacterial activity against the Gram-positive bacterium S.aureus and degrades S.aureus biofilms, allowing polymorphonuclear leukocytes to penetrate the biofilm and phagocytose bacteria (PubMed:2117044, PubMed:32995850). Has antibacterial activity against M.tuberculosis (PubMed:15385470). Mediates CASP4 activation induced by the Td92 surface protein of the periodontal pathogen T.denticola, causing production and secretion of IL1A and leading to pyroptosis of gingival fibroblasts (PubMed:29077095). Induces platelet aggregation which is strongly potentiated in the presence of ELANE (PubMed:25211214, PubMed:9111081). {ECO:0000250|UniProtKB:P28293, ECO:0000269|PubMed:10702240, ECO:0000269|PubMed:11259672, ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:15210802, ECO:0000269|PubMed:15385470, ECO:0000269|PubMed:16963625, ECO:0000269|PubMed:18217133, ECO:0000269|PubMed:18586676, ECO:0000269|PubMed:1861080, ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:2116408, ECO:0000269|PubMed:2117044, ECO:0000269|PubMed:2126324, ECO:0000269|PubMed:22307629, ECO:0000269|PubMed:22879591, ECO:0000269|PubMed:25211214, ECO:0000269|PubMed:29077095, ECO:0000269|PubMed:29652924, ECO:0000269|PubMed:30804664, ECO:0000269|PubMed:32144329, ECO:0000269|PubMed:32995850, ECO:0000269|PubMed:3390156, ECO:0000269|PubMed:7744748, ECO:0000269|PubMed:7842483, ECO:0000269|PubMed:8194606, ECO:0000269|PubMed:8920993, ECO:0000269|PubMed:9000539, ECO:0000269|PubMed:9111081, ECO:0000269|PubMed:9536127}.; FUNCTION: (Microbial infection) Inhibited reversibly by S.aureus serine protease inhibitors Eap, EapH1 and EapH2, impairing microbicidal activity in neutrophils. {ECO:0000269|PubMed:25161283, ECO:0000269|PubMed:32303641, ECO:0000269|PubMed:36736422, ECO:0000269|PubMed:37269950, ECO:0000269|PubMed:39098536}.
uniprot
proteins
mass_dalton
28837
uniprot
proteins
mutagenesis
MUTAGEN 71; /note="N->A: No effect on proteolytic processing, enzyme activation or sorting to cytoplasmic granules."; /evidence="ECO:0000269|PubMed:7499346
uniprot
proteins
post_translational_modification
PTM: Two C-terminal truncation variants have been identified, one which ends at Arg-243 and one which ends at Ser-244. {ECO:0000269|PubMed:26274980}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10702240
uniprot
proteins
pubmed
11259672
uniprot
proteins
pubmed
11942800
uniprot
proteins
pubmed
15100291
uniprot
proteins
pubmed
15210802
uniprot
proteins
pubmed
15385470
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15741158
uniprot
proteins
pubmed
16963625
uniprot
proteins
pubmed
18217133
uniprot
proteins
pubmed
18586676
uniprot
proteins
pubmed
1861080
uniprot
proteins
pubmed
1937776
uniprot
proteins
pubmed
2116408
uniprot
proteins
pubmed
2117044
uniprot
proteins
pubmed
2126324
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22275911
uniprot
proteins
pubmed
22307629
uniprot
proteins
pubmed
22879591
uniprot
proteins
pubmed
2383548
uniprot
proteins
pubmed
2501794
uniprot
proteins
pubmed
25161283
uniprot
proteins
pubmed
25211214
uniprot
proteins
pubmed
2569462
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26274980
uniprot
proteins
pubmed
29077095
uniprot
proteins
pubmed
29652924
uniprot
proteins
pubmed
30804664
uniprot
proteins
pubmed
32144329
uniprot
proteins
pubmed
32303641
uniprot
proteins
pubmed
32995850
uniprot
proteins
pubmed
3304423
uniprot
proteins
pubmed
33589665
uniprot
proteins
pubmed
3390156
uniprot
proteins
pubmed
36736422
uniprot
proteins
pubmed
37269950
uniprot
proteins
pubmed
3799965
uniprot
proteins
pubmed
39098536
uniprot
proteins
pubmed
7499346
uniprot
proteins
pubmed
7744748
uniprot
proteins
pubmed
7842483
uniprot
proteins
pubmed
7897245
uniprot
proteins
pubmed
8194606
uniprot
proteins
pubmed
8454293
uniprot
proteins
pubmed
8896442
uniprot
proteins
pubmed
8920993
uniprot
proteins
pubmed
9000539
uniprot
proteins
pubmed
9111081
uniprot
proteins
pubmed
9536127
uniprot
proteins
sequence_length
255
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:29077095, ECO:0000269|PubMed:8194606}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic granule {ECO:0000269|PubMed:7499346}. Secreted {ECO:0000269|PubMed:29077095, ECO:0000269|PubMed:32144329, ECO:0000269|PubMed:3390156}. Cytoplasm, cytosol {ECO:0000269|PubMed:29077095}. Lysosome {ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:29077095}. Nucleus {ECO:0000269|PubMed:11259672}. Note=Secreted by activated neutrophils (PubMed:3390156). Detected in synovial fluid (PubMed:32144329). Localizes to lysosomes in B cells where it is not endogenously synthesized but is internalized from the cell membrane (PubMed:15100291). Localizes to the nucleus during apoptosis (PubMed:11259672). {ECO:0000269|PubMed:11259672, ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:32144329, ECO:0000269|PubMed:3390156}.
uniprot
proteins