CATG_HUMAN
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 03-AUG-2022, entry version 206.
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 ---------------------------------------------------------------------------
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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 PDBsum; 1AU8; -.
DR PDBsum; 1CGH; -.
DR PDBsum; 1KYN; -.
DR PDBsum; 1T32; -.
DR PDBsum; 6VTM; -.
DR AlphaFoldDB; P08311; -.
DR SMR; P08311; -.
DR BioGRID; 107891; 98.
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 GlyGen; P08311; 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; P08311; -.
DR PeptideAtlas; P08311; -.
DR PRIDE; P08311; -.
DR ProteomicsDB; 52105; -.
DR TopDownProteomics; P08311; -.
DR Antibodypedia; 3597; 419 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 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; 1076876at2759; -.
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; 6 hits in 1073 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 139 other tissues.
DR Genevisible; P08311; HS.
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: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; -; 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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
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 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 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
