ID CATG_HUMAN Reviewed; 255 AA. AC P08311; Q6IBJ6; Q9UCA5; Q9UCU6; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 2. DT 24-JAN-2024, entry version 214. DE RecName: Full=Cathepsin G; DE Short=CG; DE EC=3.4.21.20 {ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:29077095, ECO:0000269|PubMed:29652924, ECO:0000269|PubMed:7744748, ECO:0000269|PubMed:7842483, ECO:0000269|PubMed:8194606}; DE Contains: DE RecName: Full=Cathepsin G, C-terminal truncated form {ECO:0000305|PubMed:26274980}; DE Flags: Precursor; GN Name=CTSG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3304423; DOI=10.1021/bi00382a032; RA Salvesen G., Farley D., Shuman J., Przybyla A., Reilly C., Travis J.; RT "Molecular cloning of human cathepsin G: structural similarity to mast cell RT and cytotoxic T lymphocyte proteinases."; RL Biochemistry 26:2289-2293(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2569462; DOI=10.1016/s0021-9258(18)80012-6; RA Hohn P.A., Popescu N.C., Hanson R.D., Salvesen G., Ley T.J.; RT "Genomic organization and chromosomal localization of the human cathepsin G RT gene."; RL J. Biol. Chem. 264:13412-13419(1989). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 21-52, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION. RC TISSUE=Monocyte; RX PubMed=8194606; DOI=10.1016/0014-5793(94)00410-2; RA Avril L.E., Di Martino-Ferrer M., Pignede G., Seman M., Gauthier F.; RT "Identification of the U-937 membrane-associated proteinase interacting RT with the V3 loop of HIV-1 gp120 as cathepsin G."; RL FEBS Lett. 345:81-86(1994). RN [7] RP PROTEIN SEQUENCE OF 21-45, AND TISSUE SPECIFICITY. RX PubMed=3799965; DOI=10.1016/0003-2697(86)90612-3; RA Heck L.W., Rostand K.S., Hunter F.A., Bhown A.; RT "Isolation, characterization, and amino-terminal amino acid sequence RT analysis of human neutrophil cathepsin G from normal donors."; RL Anal. Biochem. 158:217-227(1986). RN [8] RP PROTEIN SEQUENCE OF 21-36. RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610; RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., RA Seeger M., Nathan C.F.; RT "Antibiotic proteins of human polymorphonuclear leukocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989). RN [9] RP PROTEIN SEQUENCE OF 21-30, FUNCTION, AND ACTIVITY REGULATION. RC TISSUE=Monocyte; RX PubMed=1861080; RA Maison C.M., Villiers C.L., Colomb M.G.; RT "Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin RT G."; RL J. Immunol. 147:921-926(1991). RN [10] RP PROTEIN SEQUENCE OF 21-30. RC TISSUE=Neutrophil; RX PubMed=7897245; DOI=10.1016/0022-1759(94)00295-8; RA Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D.; RT "Use of proteinase 3 purified by reverse phase HPLC to detect RT autoantibodies in systemic vasculitis."; RL J. Immunol. Methods 180:25-33(1995). RN [11] RP PROTEIN SEQUENCE OF 67-74, GLYCOSYLATION AT ASN-71, AND ALTERNATIVE RP C-TERMINAL PROCESSING. RX PubMed=26274980; DOI=10.3390/biom5031832; RA Loke I., Packer N.H., Thaysen-Andersen M.; RT "Complementary LC-MS/MS-Based N-Glycan, N-Glycopeptide, and Intact N- RT Glycoprotein Profiling Reveals Unconventional Asn71-Glycosylation of Human RT Neutrophil Cathepsin G."; RL Biomolecules 5:1832-1854(2015). RN [12] RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION. RX PubMed=3390156; DOI=10.1042/bj2510293; RA Selak M.A., Chignard M., Smith J.B.; RT "Cathepsin G is a strong platelet agonist released by neutrophils."; RL Biochem. J. 251:293-299(1988). RN [13] RP PROTEOLYTIC PROCESSING. RX PubMed=2383548; DOI=10.1021/bi00474a013; RA Salvesen G., Enghild J.J.; RT "An unusual specificity in the activation of neutrophil serine proteinase RT zymogens."; RL Biochemistry 29:5304-5308(1990). RN [14] RP FUNCTION, AND REGIONS IMPORTANT FOR ANTIMICROBIAL ACTIVITY. RX PubMed=2116408; DOI=10.1016/s0021-9258(18)77388-2; RA Bangalore N., Travis J., Onunka V.C., Pohl J., Shafer W.M.; RT "Identification of the primary antimicrobial domains in human neutrophil RT cathepsin G."; RL J. Biol. Chem. 265:13584-13588(1990). RN [15] RP FUNCTION. RX PubMed=2117044; DOI=10.1099/00221287-136-6-997; RA Alford C.E., Amaral E., Campbell P.A.; RT "Listericidal activity of human neutrophil cathepsin G."; RL J. Gen. Microbiol. 136:997-1000(1990). RN [16] RP FUNCTION. RX PubMed=2126324; DOI=10.1111/j.1365-2958.1990.tb00706.x; RA Shafer W.M., Onunka V.C., Jannoun M., Huthwaite L.W.; RT "Molecular mechanism for the antigonococcal action of lysosomal cathepsin RT G."; RL Mol. Microbiol. 4:1269-1277(1990). RN [17] RP FUNCTION AS A MICROBICIDE, AND ACTIVITY REGULATION. RX PubMed=1937776; DOI=10.1128/iai.59.11.4193-4200.1991; RA Wasiluk K.R., Skubitz K.M., Gray B.H.; RT "Comparison of granule proteins from human polymorphonuclear leukocytes RT which are bactericidal toward Pseudomonas aeruginosa."; RL Infect. Immun. 59:4193-4200(1991). RN [18] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=7842483; DOI=10.1016/0008-8749(95)80005-4; RA Hase-Yamazaki T., Aoki Y.; RT "Stimulation of human lymphocytes by cathepsin G."; RL Cell. Immunol. 160:24-32(1995). RN [19] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=7744748; DOI=10.1074/jbc.270.19.11168; RA Molino M., Blanchard N., Belmonte E., Tarver A.P., Abrams C., Hoxie J.A., RA Cerletti C., Brass L.F.; RT "Proteolysis of the human platelet and endothelial cell thrombin receptor RT by neutrophil-derived cathepsin G."; RL J. Biol. Chem. 270:11168-11175(1995). RN [20] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-71. RX PubMed=7499346; DOI=10.1074/jbc.270.47.28413; RA Garwicz D., Lindmark A., Gullberg U.; RT "Human cathepsin G lacking functional glycosylation site is proteolytically RT processed and targeted for storage in granules after transfection to the RT rat basophilic/mast cell line RBL or the murine myeloid cell line 32D."; RL J. Biol. Chem. 270:28413-28418(1995). RN [21] RP FUNCTION. RX PubMed=8920993; DOI=10.1042/bj3190873; RA Plescia J., Altieri D.C.; RT "Activation of Mac-1 (CD11b/CD18)-bound factor X by released cathepsin G RT defines an alternative pathway of leucocyte initiation of coagulation."; RL Biochem. J. 319:873-879(1996). RN [22] RP FUNCTION. RX PubMed=9000539; DOI=10.1002/jlb.61.1.73; RA Yamazaki T., Aoki Y.; RT "Cathepsin G binds to human lymphocytes."; RL J. Leukoc. Biol. 61:73-79(1997). RN [23] RP FUNCTION. RX PubMed=9536127; DOI=10.1046/j.1365-2567.1998.00397.x; RA Yamazaki T., Aoki Y.; RT "Cathepsin G enhances human natural killer cytotoxicity."; RL Immunology 93:115-121(1998). RN [24] RP FUNCTION. RX PubMed=10702240; DOI=10.1074/jbc.275.10.6819; RA Sambrano G.R., Huang W., Faruqi T., Mahrus S., Craik C., Coughlin S.R.; RT "Cathepsin G activates protease-activated receptor-4 in human platelets."; RL J. Biol. Chem. 275:6819-6823(2000). RN [25] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11259672; DOI=10.1073/pnas.071057398; RA Biggs J.R., Yang J., Gullberg U., Muchardt C., Yaniv M., Kraft A.S.; RT "The human brm protein is cleaved during apoptosis: the role of cathepsin RT G."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3814-3819(2001). RN [26] RP FUNCTION, AND INDUCTION. RX PubMed=15385470; DOI=10.1128/iai.72.10.5712-5721.2004; RA Rivera-Marrero C.A., Stewart J., Shafer W.M., Roman J.; RT "The down-regulation of cathepsin G in THP-1 monocytes after infection with RT Mycobacterium tuberculosis is associated with increased intracellular RT survival of bacilli."; RL Infect. Immun. 72:5712-5721(2004). RN [27] RP FUNCTION. RX PubMed=15210802; DOI=10.4049/jimmunol.173.1.428; RA Sun R., Iribarren P., Zhang N., Zhou Y., Gong W., Cho E.H., Lockett S., RA Chertov O., Bednar F., Rogers T.J., Oppenheim J.J., Wang J.M.; RT "Identification of neutrophil granule protein cathepsin G as a novel RT chemotactic agonist for the G protein-coupled formyl peptide receptor."; RL J. Immunol. 173:428-436(2004). RN [28] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=15100291; DOI=10.4049/jimmunol.172.9.5495; RA Burster T., Beck A., Tolosa E., Marin-Esteban V., Roetzschke O., Falk K., RA Lautwein A., Reich M., Brandenburg J., Schwarz G., Wiendl H., Melms A., RA Lehmann R., Stevanovic S., Kalbacher H., Driessen C.; RT "Cathepsin G, and not the asparagine-specific endoprotease, controls the RT processing of myelin basic protein in lysosomes from human B lymphocytes."; RL J. Immunol. 172:5495-5503(2004). RN [29] RP FUNCTION. RX PubMed=16963625; DOI=10.1189/jlb.0406290; RA Lim J.K., Lu W., Hartley O., DeVico A.L.; RT "N-terminal proteolytic processing by cathepsin G converts RANTES/CCL5 and RT related analogs into a truncated 4-68 variant."; RL J. Leukoc. Biol. 80:1395-1404(2006). RN [30] RP FUNCTION. RX PubMed=18586676; DOI=10.1074/jbc.m710286200; RA Mambole A., Baruch D., Nusbaum P., Bigot S., Suzuki M., Lesavre P., RA Fukuda M., Halbwachs-Mecarelli L.; RT "The cleavage of neutrophil leukosialin (CD43) by cathepsin G releases its RT extracellular domain and triggers its intramembrane proteolysis by RT presenilin/gamma-secretase."; RL J. Biol. Chem. 283:23627-23635(2008). RN [31] RP FUNCTION. RX PubMed=18217133; DOI=10.1160/th07-08-0495; RA Gale A.J., Rozenshteyn D.; RT "Cathepsin G, a leukocyte protease, activates coagulation factor VIII."; RL Thromb. Haemost. 99:44-51(2008). RN [32] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [33] RP ACTIVITY REGULATION (MICROBIAL INFECTION), INTERACTION WITH M.TUBERCULOSIS RP RV3364C (MICROBIAL INFECTION), AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22275911; DOI=10.3389/fmicb.2011.00281; RA Danelishvili L., Everman J.L., McNamara M.J., Bermudez L.E.; RT "Inhibition of the plasma-membrane-associated serine protease cathepsin G RT by Mycobacterium tuberculosis Rv3364c suppresses caspase-1 and pyroptosis RT in macrophages."; RL Front. Microbiol. 2:281-281(2011). RN [34] RP FUNCTION. RX PubMed=22879591; DOI=10.1074/jbc.m112.394452; RA Woloszynek J.C., Hu Y., Pham C.T.; RT "Cathepsin G-regulated release of formyl peptide receptor agonists modulate RT neutrophil effector functions."; RL J. Biol. Chem. 287:34101-34109(2012). RN [35] RP FUNCTION. RX PubMed=22307629; DOI=10.1073/pnas.1115884109; RA Lefrancais E., Roga S., Gautier V., Gonzalez-de-Peredo A., Monsarrat B., RA Girard J.P., Cayrol C.; RT "IL-33 is processed into mature bioactive forms by neutrophil elastase and RT cathepsin G."; RL Proc. Natl. Acad. Sci. U.S.A. 109:1673-1678(2012). RN [36] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [37] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH CASP4, RP SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=29077095; DOI=10.1038/cdd.2017.167; RA Jun H.K., Jung Y.J., Ji S., An S.J., Choi B.K.; RT "Caspase-4 activation by a bacterial surface protein is mediated by RT cathepsin G in human gingival fibroblasts."; RL Cell Death Differ. 25:380-391(2018). RN [38] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=29652924; DOI=10.1371/journal.pone.0195077; RA Thorpe M., Fu Z., Chahal G., Akula S., Kervinen J., de Garavilla L., RA Hellman L.; RT "Extended cleavage specificity of human neutrophil cathepsin G: A low RT activity protease with dual chymase and tryptase-type specificities."; RL PLoS ONE 13:e0195077-e0195077(2018). RN [39] RP FUNCTION. RX PubMed=30804664; DOI=10.2147/dddt.s194765; RA Guo J., Tu J., Hu Y., Song G., Yin Z.; RT "Cathepsin G cleaves and activates IL-36gamma and promotes the inflammation RT of psoriasis."; RL Drug Des. Dev. Ther. 13:581-588(2019). RN [40] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=32144329; DOI=10.1038/s41598-020-61161-5; RA Huang S., Thomsson K.A., Jin C., Alweddi S., Struglics A., Rolfson O., RA Bjoerkman L.I., Kalamajski S., Schmidt T.A., Jay G.D., Krawetz R., RA Karlsson N.G., Eisler T.; RT "Cathepsin g Degrades Both Glycosylated and Unglycosylated Regions of RT Lubricin, a Synovial Mucin."; RL Sci. Rep. 10:4215-4215(2020). RN [41] RP ERRATUM OF PUBMED:32144329. RX PubMed=33589665; DOI=10.1038/s41598-020-77619-5; RA Huang S., Thomsson K.A., Jin C., Alweddi S., Struglics A., Rolfson O., RA Bjoerkman L.I., Kalamajski S., Schmidt T.A., Jay G.D., Krawetz R., RA Karlsson N.G., Eisler T.; RL Sci. Rep. 11:4238-4238(2021). RN [42] RP FUNCTION. RX PubMed=32995850; DOI=10.1093/infdis/jiaa612; RA Kavanaugh J.S., Leidal K.G., Nauseef W.M., Horswill A.R.; RT "Cathepsin G Degrades Staphylococcus aureus Biofilms."; RL J. Infect. Dis. 223:1865-1869(2021). RN [43] {ECO:0007744|PDB:1CGH} RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=8896442; DOI=10.1002/j.1460-2075.1996.tb00933.x; RA Hof P., Mayr I., Huber R., Korzus E., Potempa J., Travis J., Powers J.C., RA Bode W.; RT "The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val- RT Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite RT specificities."; RL EMBO J. 15:5481-5491(1996). RN [44] {ECO:0007744|PDB:1AU8} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND DISULFIDE BONDS. RA Medrano F.J., Bode W., Banbula A., Potempa J.; RL Submitted (SEP-1997) to the PDB data bank. RN [45] {ECO:0007744|PDB:1KYN} RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 21-255 IN COMPLEX WITH INHIBITOR, RP AND DISULFIDE BONDS. RX PubMed=11942800; DOI=10.1021/ja017506h; RA Greco M.N., Hawkins M.J., Powell E.T., Almond H.R. Jr., Corcoran T.W., RA de Garavilla L., Kauffman J.A., Recacha R., Chattopadhyay D., RA Andrade-Gordon P., Maryanoff B.E.; RT "Nonpeptide inhibitors of cathepsin G: optimization of a novel beta- RT ketophosphonic acid lead by structure-based drug design."; RL J. Am. Chem. Soc. 124:3810-3811(2002). RN [46] {ECO:0007744|PDB:1T32} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 21-244 IN COMPLEX WITH INHIBITOR, RP AND DISULFIDE BONDS. RX PubMed=15741158; DOI=10.1074/jbc.m501302200; RA de Garavilla L., Greco M.N., Sukumar N., Chen Z.W., Pineda A.O., RA Mathews F.S., Di Cera E., Giardino E.C., Wells G.I., Haertlein B.J., RA Kauffman J.A., Corcoran T.W., Derian C.K., Eckardt A.J., Damiano B.P., RA Andrade-Gordon P., Maryanoff B.E.; RT "A novel, potent dual inhibitor of the leukocyte proteases cathepsin G and RT chymase: molecular mechanisms and anti-inflammatory activity in vivo."; RL J. Biol. Chem. 280:18001-18007(2005). RN [47] {ECO:0007744|PDB:6VTM} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 21-244 IN COMPLEX WITH S.AUREUS RP EAPH1, ACTIVITY REGULATION, AND DISULFIDE BONDS. RX PubMed=32303641; DOI=10.1074/jbc.ra120.013601; RA Herdendorf T.J., Stapels D.A.C., Rooijakkers S.H.M., Geisbrecht B.V.; RT "Local structural plasticity of the Staphylococcus aureus evasion protein RT EapH1 enables engagement with multiple neutrophil serine proteases."; RL J. Biol. Chem. 295:7753-7762(2020). RN [48] RP VARIANT SER-125. RX PubMed=8454293; DOI=10.1007/bf00230230; RA Luedecke B., Poller W., Olek K., Bartholome K.; RT "Sequence variant of the human cathepsin G gene."; RL Hum. Genet. 91:83-84(1993). CC -!- FUNCTION: Serine protease with trypsin- and chymotrypsin-like CC specificity (PubMed:8194606, PubMed:29652924). Also displays CC antibacterial activity against Gram-negative and Gram-positive bacteria CC independent of its protease activity (PubMed:2116408, PubMed:2117044). CC Prefers Phe and Tyr residues in the P1 position of substrates but also CC cleaves efficiently after Trp and Leu (PubMed:29652924). Shows a CC preference for negatively charged amino acids in the P2' position and CC for aliphatic amino acids both upstream and downstream of the cleavage CC site (PubMed:29652924). Required for recruitment and activation of CC platelets which is mediated by the F2RL3/PAR4 platelet receptor CC (PubMed:3390156, PubMed:10702240). Binds reversibly to and stimulates B CC cells and CD4(+) and CD8(+) T cells (PubMed:7842483, PubMed:9000539). CC Also binds reversibly to natural killer (NK) cells and enhances NK cell CC cytotoxicity through its protease activity (PubMed:9000539, CC PubMed:9536127). Cleaves complement C3 (PubMed:1861080). Cleaves CC vimentin (By similarity). Cleaves thrombin receptor F2R/PAR1 and acts CC as either an agonist or an inhibitor, depending on the F2R cleavage CC site (PubMed:10702240, PubMed:7744748). Cleavage of F2R at '41-Arg-|- CC Ser-42' results in receptor activation while cleavage at '55-Phe-|-Trp- CC 56' results in inhibition of receptor activation (PubMed:7744748). CC Cleaves the synovial mucin-type protein PRG4/lubricin CC (PubMed:32144329). Cleaves and activates IL36G which promotes CC expression of chemokines CXCL1 and CXLC8 in keratinocytes CC (PubMed:30804664). Cleaves IL33 into mature forms which have greater CC activity than the unprocessed form (PubMed:22307629). Cleaves CC coagulation factor F8 to produce a partially activated form CC (PubMed:18217133). Also cleaves and activates coagulation factor F10 CC (PubMed:8920993). Cleaves leukocyte cell surface protein SPN/CD43 to CC releases its extracellular domain and trigger its intramembrane CC proteolysis by gamma-secretase, releasing the CD43 cytoplasmic tail CC chain (CD43-ct) which translocates to the nucleus (PubMed:18586676). CC Cleaves CCL5/RANTES to produce RANTES(4-68) lacking the N-terminal CC three amino acids which exhibits reduced chemotactic and antiviral CC activities (PubMed:16963625). During apoptosis, cleaves SMARCA2/BRM to CC produce a 160 kDa cleavage product which localizes to the cytosol CC (PubMed:11259672). Cleaves myelin basic protein MBP in B cell lysosomes CC at '224-Phe-|-Lys-225' and '248-Phe-|-Ser-249', degrading the major CC immunogenic MBP epitope and preventing the activation of MBP-specific CC autoreactive T cells (PubMed:15100291). Cleaves annexin ANXA1 and CC antimicrobial peptide CAMP to produce peptides which act on neutrophil CC N-formyl peptide receptors to enhance the release of CXCL2 CC (PubMed:22879591). Acts as a ligand for the N-formyl peptide receptor CC FPR1, enhancing phagocyte chemotaxis (PubMed:15210802). Has CC antibacterial activity against the Gram-negative bacteria N.gonorrhoeae CC and P.aeruginosa (PubMed:2116408, PubMed:1937776). Likely to act CC against N.gonorrhoeae by interacting with N.gonorrhoeae penA/PBP2 CC (PubMed:2126324). Exhibits potent antimicrobial activity against the CC Gram-positive bacterium L.monocytogenes (PubMed:2117044). Has CC antibacterial activity against the Gram-positive bacterium S.aureus and CC degrades S.aureus biofilms, allowing polymorphonuclear leukocytes to CC penetrate the biofilm and phagocytose bacteria (PubMed:2117044, CC PubMed:32995850). Has antibacterial activity against M.tuberculosis CC (PubMed:15385470). Mediates CASP4 activation induced by the Td92 CC surface protein of the periodontal pathogen T.denticola, causing CC production and secretion of IL1A and leading to pyroptosis of gingival CC fibroblasts (PubMed:29077095). {ECO:0000250|UniProtKB:P28293, CC ECO:0000269|PubMed:10702240, ECO:0000269|PubMed:11259672, CC ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:15210802, CC ECO:0000269|PubMed:15385470, ECO:0000269|PubMed:16963625, CC ECO:0000269|PubMed:18217133, ECO:0000269|PubMed:18586676, CC ECO:0000269|PubMed:1861080, ECO:0000269|PubMed:1937776, CC ECO:0000269|PubMed:2116408, ECO:0000269|PubMed:2117044, CC ECO:0000269|PubMed:2126324, ECO:0000269|PubMed:22307629, CC ECO:0000269|PubMed:22879591, ECO:0000269|PubMed:29077095, CC ECO:0000269|PubMed:29652924, ECO:0000269|PubMed:30804664, CC ECO:0000269|PubMed:32144329, ECO:0000269|PubMed:32995850, CC ECO:0000269|PubMed:3390156, ECO:0000269|PubMed:7744748, CC ECO:0000269|PubMed:7842483, ECO:0000269|PubMed:8194606, CC ECO:0000269|PubMed:8920993, ECO:0000269|PubMed:9000539, CC ECO:0000269|PubMed:9536127}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Specificity similar to chymotrypsin C.; EC=3.4.21.20; CC Evidence={ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:29077095, CC ECO:0000269|PubMed:29652924, ECO:0000269|PubMed:7744748, CC ECO:0000269|PubMed:7842483, ECO:0000269|PubMed:8194606}; CC -!- ACTIVITY REGULATION: Inhibited by soybean trypsin inhibitor, CC benzamidine, the synthetic peptide R13K, Z-Gly-Leu-Phe-CH2Cl, CC phenylmethylsulfonyl fluoride, 3,4-dichloroisocoumarin, DFP, SBTI and CC alpha-1-antitrypsin. Inhibited by LPS from P.aeruginosa but not by LPS CC from S.minnesota. Not inhibited by elastinal, CMK, TLCK, ETDA or CC leupeptin. {ECO:0000269|PubMed:1861080, ECO:0000269|PubMed:1937776, CC ECO:0000269|PubMed:3390156, ECO:0000269|PubMed:8194606}. CC -!- ACTIVITY REGULATION: (Microbial infection) Inhibited reversibly by CC S.aureus EapH1. {ECO:0000269|PubMed:32303641}. CC -!- ACTIVITY REGULATION: (Microbial infection) Activity is induced by the CC Td92 surface protein of the periodontal pathogen T.denticola. CC {ECO:0000269|PubMed:29077095}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.15 mM for Z-Lys-SBzl {ECO:0000269|PubMed:8194606}; CC KM=0.26 mM for Suc-Ala-Ala-Pro-Phe-SBzl {ECO:0000269|PubMed:8194606}; CC -!- SUBUNIT: (Microbial infection) Interacts with CASP4; the interaction is CC promoted by the Td92 surface protein of the periodontal pathogen CC T.denticola and leads to CASP4 activation. CC {ECO:0000269|PubMed:29077095}. CC -!- SUBUNIT: (Microbial infection) Interacts with M.tuberculosis protein CC Rv3364c. {ECO:0000269|PubMed:22275911}. CC -!- SUBUNIT: (Microbial infection) Interacts with S.aureus EapH1; EapH1 CC acts as a reversible inhibitor of CATG activity. CC {ECO:0000269|PubMed:32303641}. CC -!- INTERACTION: CC P08311; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-5462635, EBI-3867333; CC P08311; Q15323: KRT31; NbExp=3; IntAct=EBI-5462635, EBI-948001; CC P08311; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-5462635, EBI-945833; CC P08311; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-5462635, EBI-79165; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15100291, CC ECO:0000269|PubMed:29077095, ECO:0000269|PubMed:8194606}; Peripheral CC membrane protein {ECO:0000305}. Cytoplasmic granule CC {ECO:0000269|PubMed:7499346}. Secreted {ECO:0000269|PubMed:29077095, CC ECO:0000269|PubMed:32144329, ECO:0000269|PubMed:3390156}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:29077095}. Lysosome CC {ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:29077095}. Nucleus CC {ECO:0000269|PubMed:11259672}. Note=Secreted by activated neutrophils CC (PubMed:3390156). Detected in synovial fluid (PubMed:32144329). CC Localizes to lysosomes in B cells where it is not endogenously CC synthesized but is internalized from the cell membrane CC (PubMed:15100291). Localizes to the nucleus during apoptosis CC (PubMed:11259672). {ECO:0000269|PubMed:11259672, CC ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:32144329, CC ECO:0000269|PubMed:3390156}. CC -!- TISSUE SPECIFICITY: Expressed in neutrophils (at protein level) CC (PubMed:3799965). Expressed in B cells (PubMed:15100291). CC {ECO:0000269|PubMed:15100291, ECO:0000269|PubMed:3799965}. CC -!- INDUCTION: Induced by the Td92 surface protein of the periodontal CC pathogen T.denticola (PubMed:29077095). Down-regulated in monocytes CC following M.tuberculosis infection and exposure to bacterial CC lipopolysaccharide which coincides with increased M.tuberculosis CC replication and intracellular survival (PubMed:15385470). CC {ECO:0000269|PubMed:15385470, ECO:0000269|PubMed:29077095}. CC -!- PTM: Two C-terminal truncation variants have been identified, one which CC ends at Arg-243 and one which ends at Ser-244. CC {ECO:0000269|PubMed:26274980}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE- CC ProRule:PRU00274}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M16117; AAA52126.1; -; mRNA. DR EMBL; J04990; AAA51919.1; -; Genomic_DNA. DR EMBL; CR456807; CAG33088.1; -; mRNA. DR EMBL; CR541704; CAG46505.1; -; mRNA. DR EMBL; CH471078; EAW66006.1; -; Genomic_DNA. DR EMBL; BC014460; AAH14460.1; -; mRNA. DR CCDS; CCDS9631.1; -. DR PIR; A32627; A27122. DR RefSeq; NP_001902.1; NM_001911.2. DR PDB; 1AU8; X-ray; 1.90 A; A=21-244. DR PDB; 1CGH; X-ray; 1.80 A; A=21-244. DR PDB; 1KYN; X-ray; 3.50 A; A/B=21-255. DR PDB; 1T32; X-ray; 1.85 A; A=21-244. DR PDB; 6VTM; X-ray; 1.60 A; A/C/D/G=21-244. DR PDB; 8D4S; X-ray; 1.95 A; A/C/E/G=21-243. DR PDB; 8D4V; X-ray; 1.85 A; A/C=21-243. DR PDB; 8D7I; X-ray; 3.63 A; C/F/I/L/O/R=21-243. DR PDB; 8D7K; X-ray; 3.10 A; C/F/I/L=21-243. DR PDB; 8G24; X-ray; 1.82 A; A=21-243. DR PDB; 8G25; X-ray; 1.80 A; A/F/I=21-243. DR PDB; 8G26; X-ray; 1.85 A; A=21-243. DR PDBsum; 1AU8; -. DR PDBsum; 1CGH; -. DR PDBsum; 1KYN; -. DR PDBsum; 1T32; -. DR PDBsum; 6VTM; -. DR PDBsum; 8D4S; -. DR PDBsum; 8D4V; -. DR PDBsum; 8D7I; -. DR PDBsum; 8D7K; -. DR PDBsum; 8G24; -. DR PDBsum; 8G25; -. DR PDBsum; 8G26; -. DR AlphaFoldDB; P08311; -. DR SMR; P08311; -. DR BioGRID; 107891; 102. DR CORUM; P08311; -. DR IntAct; P08311; 24. DR MINT; P08311; -. DR STRING; 9606.ENSP00000216336; -. DR BindingDB; P08311; -. DR ChEMBL; CHEMBL4071; -. DR DrugBank; DB04016; 2-[3-({Methyl[1-(2-Naphthoyl)Piperidin-4-Yl]Amino}Carbonyl)-2-Naphthyl]-1-(1-Naphthyl)-2-Oxoethylphosphonic Acid. DR DrugBank; DB02360; Bis-Napthyl Beta-Ketophosphonic Acid. DR DrugCentral; P08311; -. DR GuidetoPHARMACOLOGY; 2348; -. DR MEROPS; S01.133; -. DR GlyCosmos; P08311; 1 site, No reported glycans. DR GlyGen; P08311; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; P08311; -. DR PhosphoSitePlus; P08311; -. DR BioMuta; CTSG; -. DR DMDM; 115725; -. DR EPD; P08311; -. DR jPOST; P08311; -. DR MassIVE; P08311; -. DR MaxQB; P08311; -. DR PaxDb; 9606-ENSP00000216336; -. DR PeptideAtlas; P08311; -. DR PRIDE; P08311; -. DR ProteomicsDB; 52105; -. DR Pumba; P08311; -. DR TopDownProteomics; P08311; -. DR Antibodypedia; 3597; 457 antibodies from 35 providers. DR DNASU; 1511; -. DR Ensembl; ENST00000216336.3; ENSP00000216336.2; ENSG00000100448.4. DR GeneID; 1511; -. DR KEGG; hsa:1511; -. DR MANE-Select; ENST00000216336.3; ENSP00000216336.2; NM_001911.3; NP_001902.1. DR UCSC; uc001wpq.4; human. DR AGR; HGNC:2532; -. DR CTD; 1511; -. DR DisGeNET; 1511; -. DR GeneCards; CTSG; -. DR HGNC; HGNC:2532; CTSG. DR HPA; ENSG00000100448; Tissue enriched (bone). DR MIM; 116830; gene. DR neXtProt; NX_P08311; -. DR OpenTargets; ENSG00000100448; -. DR PharmGKB; PA27032; -. DR VEuPathDB; HostDB:ENSG00000100448; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT01030000234551; -. DR HOGENOM; CLU_006842_1_0_1; -. DR InParanoid; P08311; -. DR OMA; QLDQMEI; -. DR OrthoDB; 2540265at2759; -. DR PhylomeDB; P08311; -. DR TreeFam; TF333630; -. DR BRENDA; 3.4.21.20; 2681. DR PathwayCommons; P08311; -. DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix. DR Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases. DR Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-448706; Interleukin-1 processing. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6803157; Antimicrobial peptides. DR Reactome; R-HSA-9635465; Suppression of apoptosis. DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection. DR SABIO-RK; P08311; -. DR SignaLink; P08311; -. DR SIGNOR; P08311; -. DR BioGRID-ORCS; 1511; 8 hits in 1151 CRISPR screens. DR ChiTaRS; CTSG; human. DR EvolutionaryTrace; P08311; -. DR GeneWiki; Cathepsin_G; -. DR GenomeRNAi; 1511; -. DR Pharos; P08311; Tchem. DR PRO; PR:P08311; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; P08311; Protein. DR Bgee; ENSG00000100448; Expressed in trabecular bone tissue and 140 other cell types or tissues. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0005764; C:lysosome; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0030141; C:secretory granule; IDA:MGI. DR GO; GO:0089720; F:caspase binding; IPI:UniProtKB. DR GO; GO:0008201; F:heparin binding; IDA:MGI. DR GO; GO:0008233; F:peptidase activity; IDA:MGI. DR GO; GO:0048018; F:receptor ligand activity; IDA:UniProtKB. DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB. DR GO; GO:0008236; F:serine-type peptidase activity; IMP:UniProtKB. DR GO; GO:0002003; P:angiotensin maturation; TAS:Reactome. DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB. DR GO; GO:0098786; P:biofilm matrix disassembly; IDA:UniProtKB. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050832; P:defense response to fungus; IEA:Ensembl. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB. DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB. DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0002548; P:monocyte chemotaxis; IDA:UniProtKB. DR GO; GO:0050868; P:negative regulation of T cell activation; IDA:UniProtKB. DR GO; GO:0042119; P:neutrophil activation; IDA:UniProtKB. DR GO; GO:0070946; P:neutrophil-mediated killing of gram-positive bacterium; IEA:Ensembl. DR GO; GO:0030168; P:platelet activation; IDA:UniProtKB. DR GO; GO:0050778; P:positive regulation of immune response; IEA:Ensembl. DR GO; GO:1901731; P:positive regulation of platelet aggregation; IDA:UniProtKB. DR GO; GO:0019538; P:protein metabolic process; TAS:Reactome. DR GO; GO:0006468; P:protein phosphorylation; IDA:CACAO. DR GO; GO:0016485; P:protein processing; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB. DR GO; GO:0035590; P:purinergic nucleotide receptor signaling pathway; TAS:Reactome. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24271:SF13; CATHEPSIN G; 1. DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR Genevisible; P08311; HS. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; Cell membrane; Chemotaxis; KW Cytoplasm; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Hydrolase; Lysosome; Membrane; Nucleus; Protease; Reference proteome; KW Secreted; Serine protease; Signal; Zymogen. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT PROPEP 19..20 FT /note="Activation peptide" FT /evidence="ECO:0000269|PubMed:1861080, FT ECO:0000269|PubMed:2383548, ECO:0000269|PubMed:2501794, FT ECO:0000269|PubMed:3799965, ECO:0000269|PubMed:7897245, FT ECO:0000269|PubMed:8194606" FT /id="PRO_0000027512" FT CHAIN 21..244 FT /note="Cathepsin G" FT /id="PRO_0000027513" FT CHAIN 21..243 FT /note="Cathepsin G, C-terminal truncated form" FT /evidence="ECO:0000269|PubMed:26274980" FT /id="PRO_0000454551" FT PROPEP 245..255 FT /evidence="ECO:0000269|PubMed:2383548" FT /id="PRO_0000454552" FT DOMAIN 21..243 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT REGION 21..25 FT /note="Important for antimicrobial activity" FT /evidence="ECO:0000269|PubMed:2116408" FT REGION 97..111 FT /note="Important for antimicrobial activity" FT /evidence="ECO:0000269|PubMed:2116408" FT ACT_SITE 64 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 108 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT ACT_SITE 201 FT /note="Charge relay system" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT CARBOHYD 71 FT /note="N-linked (GlcNAc...) (complex) asparagine; FT alternate" FT /evidence="ECO:0000269|PubMed:26274980" FT CARBOHYD 71 FT /note="N-linked (GlcNAc...) (paucimannose) asparagine; FT alternate" FT /evidence="ECO:0000269|PubMed:26274980" FT DISULFID 49..65 FT /evidence="ECO:0000269|PubMed:11942800, FT ECO:0000269|PubMed:15741158, ECO:0000269|PubMed:32303641, FT ECO:0000269|PubMed:8896442, ECO:0000269|Ref.44, FT ECO:0007744|PDB:1AU8, ECO:0007744|PDB:1CGH, FT ECO:0007744|PDB:1KYN, ECO:0007744|PDB:1T32, FT ECO:0007744|PDB:6VTM" FT DISULFID 142..207 FT /evidence="ECO:0000269|PubMed:11942800, FT ECO:0000269|PubMed:15741158, ECO:0000269|PubMed:32303641, FT ECO:0000269|PubMed:8896442, ECO:0000269|Ref.44, FT ECO:0007744|PDB:1AU8, ECO:0007744|PDB:1CGH, FT ECO:0007744|PDB:1KYN, ECO:0007744|PDB:1T32, FT ECO:0007744|PDB:6VTM" FT DISULFID 172..186 FT /evidence="ECO:0000269|PubMed:11942800, FT ECO:0000269|PubMed:15741158, ECO:0000269|PubMed:32303641, FT ECO:0000269|PubMed:8896442, ECO:0000269|Ref.44, FT ECO:0007744|PDB:1AU8, ECO:0007744|PDB:1CGH, FT ECO:0007744|PDB:1KYN, ECO:0007744|PDB:1T32, FT ECO:0007744|PDB:6VTM" FT VARIANT 125 FT /note="N -> S (in dbSNP:rs45567233)" FT /evidence="ECO:0000269|PubMed:8454293" FT /id="VAR_006491" FT MUTAGEN 71 FT /note="N->A: No effect on proteolytic processing, enzyme FT activation or sorting to cytoplasmic granules." FT /evidence="ECO:0000269|PubMed:7499346" FT STRAND 35..42 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 45..55 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 58..61 FT /evidence="ECO:0007829|PDB:6VTM" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 68..75 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 87..96 FT /evidence="ECO:0007829|PDB:6VTM" FT TURN 102..105 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 110..116 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:8G26" FT STRAND 141..147 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 150..153 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 160..166 FT /evidence="ECO:0007829|PDB:6VTM" FT HELIX 169..175 FT /evidence="ECO:0007829|PDB:6VTM" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 184..187 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:8D4V" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 210..218 FT /evidence="ECO:0007829|PDB:6VTM" FT STRAND 226..230 FT /evidence="ECO:0007829|PDB:6VTM" FT HELIX 231..234 FT /evidence="ECO:0007829|PDB:6VTM" FT HELIX 235..242 FT /evidence="ECO:0007829|PDB:6VTM" SQ 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 //