Record in detail


General Info

  • lamp_id:L03A000326
  • Name:CATG_HUMAN
  • FullName:Cathepsin G
  • Source:Homo sapiens
  • Mass:2430.9 Da
  • Sequence Length:22 aa
  • Isoelectric Point:12.68
  • Activity:Antimicrobial
  • Sequence
        RPGTLRLCTVAGWGRVSMRRGT
  • 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.

Cross-Linking

  •   Cross-linking
  •   1  Database:Uniprot  P08311
  •   2  Database:AMD  CGB_HUMAN

Top similar AMPs

  • Top similar AMPs on LAMP
  • 1. L03A000326    From 1 To 22 E-value: 0.0000003 Score: 45.4
        RPGTLRLCTVAGWGRVSMRRGT
  • 2. L01A001572    From 1 To 20 E-value: 0.00009 Score: 37.4
        RPGTL--CTVAGWGRVSMRRGT
  • 3. L01A001555    From 1 To 15 E-value: 0.002 Score: 33.1
        CTVAGWGRVSMRRGT
  • 4. L01A001556    From 1 To 13 E-value: 0.96 Score: 23.9
        RPG-LTLCTVAGWG
  • 5. L01A001554    From 1 To 10 E-value: 1.3 Score: 23.5
        WGRVSMRRGT

Structure

  •   Domains
  •   1  Name:Pept_cys/ser_Trypsin-like    Interpro Link:IPR009003
  •   2  Name:Peptidase_S1/S6_AS    Interpro Link:IPR018114
  •   3  Name:Peptidase_S1_S6    Interpro Link:IPR001254
  •   4  Name:Peptidase_S1A    Interpro Link:IPR001314
  •   Structures
  •   1
    PDB:1AU8

    Method:X-ray
    Chains:A=21-244
  •   2
    PDB:1CGH

    Method:X-ray
    Chains:A=21-244
  •   3
    PDB:1KYN

    Method:X-ray
    Chains:A/B=21-255
  •   4
    PDB:1T32

    Method:X-ray
    Chains:A=21-239

Activity

  •   Antibacterial Activities

  •     No MICs found on LAMP database

Toxicity

  •   Toxicity

  •     No toxicity records found on LAMP database

Reference

  •   Reference
  •   [1]  Bhown A.,Hunter F.A.,Rostand K.S.,Heck L.W.,
  •   Title:Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors.
  •   Journal:Anal. Biochem., 1986, 158, 217-227  [MEDLINE:87097924]
  •   [2]  Reilly C.,Przybyla A.,Shuman J.,Farley D.,Salvesen G.,
  •   Title:Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases.
  •   Journal:Biochemistry, 1987, 26, 2289-2293  [MEDLINE:87299663]
  •   [3]  Wilde C.,Griffith J.,Campanelli D.,Scott R.W.,Gabay J.E.,
  •   Title:Antibiotic proteins of human polymorphonuclear leukocytes.
  •   Journal:Proc. Natl. Acad. Sci. U.S.A., 1989, 86, 5610-5614  [MEDLINE:89315847]
  •   [4]  Ley T.J.,Salvesen G.,Hanson R.D.,Popescu N.C.,Hohn P.A.,
  •   Title:Genomic organization and chromosomal localization of the human cathepsin G gene.
  •   Journal:J. Biol. Chem., 1989, 264, 13412-13419  [MEDLINE:89340411]
  •   [5]  Gray B.H.,Skubitz K.M.,Wasiluk K.R.,
  •   Title:Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa.
  •   Journal:Infect. Immun., 1991, 59, 4193-4200  [MEDLINE:92040097]
  •   [6]  Colomb M.G.,Villiers C.L.,Maison C.M.,
  •   Title:Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G.
  •   Journal:J. Immunol., 1991, 147, 921-926  [MEDLINE:91318179]
  •   [7]  Bartholome K.,Olek K.,Poller W.,Luedecke B.,
  •   Title:Sequence variant of the human cathepsin G gene.
  •   Journal:Hum. Genet., 1993, 91, 83-84  [MEDLINE:93202661]
  •   [8]  Gauthier F.,Seman M.,Pignede G.,Di Martino-Ferrer M.,Avril L.E.,
  •   Title:Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G.
  •   Journal:FEBS Lett., 1994, 345, 81-86  [MEDLINE:94252410]
  •   [9]  Pusey C.D.,Turner N.,Coulthart A.,Kendal H.,Gaskin G.,
  •   Title:Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis.
  •   Journal:J. Immunol. Methods, 1995, 180, 25-33  [MEDLINE:95204964]
  •   [10]  Potempa J.,Korzus E.,Huber R.,Mayr I.,Hof P.,
  •   Title: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.
  •   Journal:EMBO J., 1996, 15, 5481-5491  [MEDLINE:97051807]
  •   [11]  
  •   Title:The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
  •   Journal:Genome Res., 2004, 14, 2121-2127  [PubMed:15489334]

Comments

  •   Comments

  •     No comments found on LAMP database



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