Cathepsin G

Details

Name
Cathepsin G
Synonyms
  • 3.4.21.20
  • CG
Gene Name
CTSG
Organism
Humans
Amino acid sequence
>lcl|BSEQ0016283|Cathepsin G
MQPLLLLLAFLLPTGAEAGEIIGGRESRPHSRPYMAYLQIQSPAGQSRCGGFLVREDFVL
TAAHCWGSNINVTLGAHNIQRRENTQQHITARRAIRHPQYNQRTIQNDIMLLQLSRRVRR
NRNVNPVALPRAQEGLRPGTLCTVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIFGSYD
PRRQICVGDRRERKAAFKGDSGGPLLCNNVAHGIVSYGKSSGVPPEVFTRVSSFLPWIRT
TMRSFKLLDQMETPL
Number of residues
255
Molecular Weight
28836.99
Theoretical pI
11.69
GO Classification
Functions
heparin binding / peptidase activity / serine-type endopeptidase activity
Processes
angiotensin maturation / cellular protein metabolic process / defense response to fungus / extracellular matrix disassembly / extracellular matrix organization / immune response / negative regulation of growth of symbiont in host / neutrophil mediated killing of gram-positive bacterium / positive regulation of immune response / protein phosphorylation / protein processing / proteolysis / response to lipopolysaccharide
Components
cell surface / cytoplasm / extracellular exosome / extracellular region / extracellular space / nucleus / plasma membrane / secretory granule
General Function
Serine-type endopeptidase activity
Specific 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cell surface
Gene sequence
>lcl|BSEQ0016284|Cathepsin G (CTSG)
ATGCAGCCACTCCTGCTTCTGCTGGCCTTTCTCCTACCCACTGGGGCTGAGGCAGGGGAG
ATCATCGGAGGCCGGGAGAGCAGGCCCCACTCCCGCCCCTACATGGCGTATCTTCAGATC
CAGAGTCCAGCAGGTCAGAGCAGATGTGGAGGGTTCCTGGTGCGAGAAGACTTTGTGCTG
ACAGCAGCTCATTGCTGGGGAAGCAATATAAATGTCACCCTGGGCGCCCACAATATCCAG
AGACGGGAAAACACCCAGCAACACATCACTGCGCGCAGAGCCATCCGCCACCCTCAATAT
AATCAGCGGACCATCCAGAATGACATCATGTTATTGCAGCTGAGCAGAAGAGTCAGACGG
AATCGAAACGTGAACCCAGTGGCTCTGCCTAGAGCCCAGGAGGGACTGAGACCCGGGACG
CTGTGCACTGTGGCCGGCTGGGGCAGGGTCAGCATGAGGAGGGGAACAGATACACTCCGA
GAGGTGCAGCTGAGAGTGCAGAGGGATAGGCAGTGCCTCCGCATCTTCGGTTCCTACGAC
CCCCGAAGGCAGATTTGTGTGGGGGACCGGCGGGAACGGAAGGCTGCCTTCAAGGGGGAT
TCCGGAGGCCCCCTGCTGTGTAACAATGTGGCCCACGGCATCGTCTCCTATGGAAAGTCG
TCAGGGGTTCCTCCAGAAGTCTTCACCAGGGTCTCAAGTTTCCTGCCCTGGATAAGGACA
ACAATGAGAAGCTTCAAACTGCTGGATCAGATGGAGACCCCCCTGTGA
Chromosome Location
14
Locus
14q11.2
External Identifiers
ResourceLink
UniProtKB IDP08311
UniProtKB Entry NameCATG_HUMAN
GenBank Protein ID181182
GenBank Gene IDM16117
GenAtlas IDCTSG
HGNC IDHGNC:2532
General References
  1. 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. 1987 Apr 21;26(8):2289-93. [Article]
  2. Hohn PA, Popescu NC, Hanson RD, Salvesen G, Ley TJ: Genomic organization and chromosomal localization of the human cathepsin G gene. J Biol Chem. 1989 Aug 15;264(23):13412-9. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Avril LE, 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. 1994 May 23;345(1):81-6. [Article]
  5. Heck LW, Rostand KS, Hunter FA, Bhown A: Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors. Anal Biochem. 1986 Oct;158(1):217-27. [Article]
  6. Gabay JE, Scott RW, Campanelli D, Griffith J, Wilde C, Marra MN, Seeger M, Nathan CF: Antibiotic proteins of human polymorphonuclear leukocytes. Proc Natl Acad Sci U S A. 1989 Jul;86(14):5610-4. [Article]
  7. Maison CM, Villiers CL, Colomb MG: Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G. J Immunol. 1991 Aug 1;147(3):921-6. [Article]
  8. Gaskin G, Kendal H, Coulthart A, Turner N, Pusey CD: Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis. J Immunol Methods. 1995 Mar 13;180(1):25-33. [Article]
  9. Wasiluk KR, Skubitz KM, Gray BH: Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa. Infect Immun. 1991 Nov;59(11):4193-200. [Article]
  10. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  11. Vaca Jacome AS, 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. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  12. Hof P, Mayr I, Huber R, Korzus E, Potempa J, Travis J, Powers JC, 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. 1996 Oct 15;15(20):5481-91. [Article]
  13. Ludecke B, Poller W, Olek K, Bartholome K: Sequence variant of the human cathepsin G gene. Hum Genet. 1993 Mar;91(1):83-4. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02360Bis-Napthyl Beta-Ketophosphonic AcidexperimentalunknownDetails
DB040162-[3-({Methyl[1-(2-Naphthoyl)Piperidin-4-Yl]Amino}Carbonyl)-2-Naphthyl]-1-(1-Naphthyl)-2-Oxoethylphosphonic AcidexperimentalunknownDetails