Reviewed,
UniProtKB/Swiss-Prot P08311 (CATG_HUMAN)
Last modified
November 3, 2009.
Version 104.
History...
Clusters with 100%,
90%,
50% identity |
Documents (7) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cathepsin G Short name=CG EC=3.4.21.20 | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 255 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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. Ref.6 Ref.9 Ref.11 |
| Catalytic activity | Specificity similar to chymotrypsin C. |
| Enzyme 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 and ETDA. Ref.6 Ref.9 Ref.11 |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain. |
| Biophysicochemical properties | Kinetic parameters: KM=1.15 mM for Z-Lys-SBzl KM=0.26 mM for Suc-Ala-Ala-Pro-Phe-SBzl |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Polymorphism |
| Domain | Signal |
| Molecular function | Antibiotic Antimicrobial Hydrolase Protease Serine protease |
| PTM | Disulfide bond Glycoprotein Zymogen |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW immune response Ref.2Traceable author statement. Source: ProtInc proteolysis Ref.9Inferred from direct assay. Source: UniProtKB |
| Cellular component | cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Ref.9Inferred from direct assay. Source: UniProtKB |
| Molecular function | protein binding Inferred from direct assay. Source: MGI serine-type endopeptidase activity Ref.6Inferred from direct assay. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | |||||||||||||||||||||||||||||||||||||
| Propeptide | 19 – 20 | 2 | Activation peptide | PRO_0000027512 | |||||||||||||||||||||||||||||||||||
| Chain | 21 – 255 | 235 | Cathepsin G | PRO_0000027513 | |||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||
| Domain | 21 – 243 | 223 | Peptidase S1 | ||||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||||
| Active site | 64 | 1 | Charge relay system | ||||||||||||||||||||||||||||||||||||
| Active site | 108 | 1 | Charge relay system | ||||||||||||||||||||||||||||||||||||
| Active site | 201 | 1 | Charge relay system | ||||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||||
| Glycosylation | 71 | 1 | N-linked (GlcNAc...) | ||||||||||||||||||||||||||||||||||||
| Disulfide bond | 49 ↔ 65 | ||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 142 ↔ 207 | ||||||||||||||||||||||||||||||||||||||
| Disulfide bond | 172 ↔ 186 | ||||||||||||||||||||||||||||||||||||||
Natural variations | |||||||||||||||||||||||||||||||||||||||
| Natural variant | 125 | 1 | N → S | VAR_006491 | |||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||
| Turn | 41 – 43 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 55 – 61 | 7 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 71 – 75 | 5 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 87 – 96 | 10 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 102 – 104 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 110 – 116 | 7 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 141 – 147 | 7 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 150 – 153 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 160 – 165 | 6 | |||||||||||||||||||||||||||||||||||||
| Helix | 169 – 173 | 5 | |||||||||||||||||||||||||||||||||||||
| Turn | 181 – 183 | 3 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 184 – 187 | 4 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 204 – 217 | 14 | |||||||||||||||||||||||||||||||||||||
| Beta strand | 226 – 230 | 5 | |||||||||||||||||||||||||||||||||||||
| Helix | 231 – 233 | 3 | |||||||||||||||||||||||||||||||||||||
| Helix | 235 – 242 | 8 | |||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases." Salvesen G., Farley D., Shuman J., Przybyla A., Reilly C., Travis J. Biochemistry 26:2289-2293(1987) [PubMed: 3304423] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Genomic organization and chromosomal localization of the human cathepsin G gene." Hohn P.A., Popescu N.C., Hanson R.D., Salvesen G., Ley T.J. J. Biol. Chem. 264:13412-13419(1989) [PubMed: 2569462] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [4] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin. |
| [6] | "Identification of the U-937 membrane-associated proteinase interacting with the V3 loop of HIV-1 gp120 as cathepsin G." Avril L.E., Di Martino-Ferrer M., Pignede G., Seman M., Gauthier F. FEBS Lett. 345:81-86(1994) [PubMed: 8194606] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-52, FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION. Tissue: Monocyte. |
| [7] | "Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors." Heck L.W., Rostand K.S., Hunter F.A., Bhown A. Anal. Biochem. 158:217-227(1986) [PubMed: 3799965] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-45. |
| [8] | "Antibiotic proteins of human polymorphonuclear leukocytes." Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., Seeger M., Nathan C.F. Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989) [PubMed: 2501794] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-36. |
| [9] | "Proteolysis of C3 on U937 cell plasma membranes. Purification of cathepsin G." Maison C.M., Villiers C.L., Colomb M.G. J. Immunol. 147:921-926(1991) [PubMed: 1861080] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-30, FUNCTION, ENZYME REGULATION. Tissue: Monocyte. |
| [10] | "Use of proteinase 3 purified by reverse phase HPLC to detect autoantibodies in systemic vasculitis." Gaskin G., Kendal H., Coulthart A., Turner N., Pusey C.D. J. Immunol. Methods 180:25-33(1995) [PubMed: 7897245] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-30. Tissue: Neutrophil. |
| [11] | "Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa." Wasiluk K.R., Skubitz K.M., Gray B.H. Infect. Immun. 59:4193-4200(1991) [PubMed: 1937776] [Abstract] Cited for: FUNCTION AS A MICROBICIDE, ENZYME REGULATION. |
| [12] | "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." Hof P., Mayr I., Huber R., Korzus E., Potempa J., Travis J., Powers J.C., Bode W. EMBO J. 15:5481-5491(1996) [PubMed: 8896442] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). |
| [13] | Medrano F.J., Bode W., Banbula A., Potempa J. Submitted (SEP-1997) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). |
| [14] | "Sequence variant of the human cathepsin G gene." Luedecke B., Poller W., Olek K., Bartholome K. Hum. Genet. 91:83-84(1993) [PubMed: 8454293] [Abstract] Cited for: VARIANT SER-125. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M16117 mRNA. Translation: AAA52126.1. J04990 Genomic DNA. Translation: AAA51919.1. CR456807 mRNA. Translation: CAG33088.1. CR541704 mRNA. Translation: CAG46505.1. CH471078 Genomic DNA. Translation: EAW66006.1. BC014460 mRNA. Translation: AAH14460.1. | |||||||||||||||||||||||||||||||
| IPI | IPI00028064. | ||||||||||||||||||||||||||||||
| PIR | A27122. A32627. | ||||||||||||||||||||||||||||||
| RefSeq | NP_001902.1. | ||||||||||||||||||||||||||||||
| UniGene | Hs.421724 | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| STRING | P08311. | ||||||||||||||||||||||||||||||
Protein family/group databases | |||||||||||||||||||||||||||||||
| MEROPS | S01.133. | ||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||
| PeptideAtlas | P08311. | ||||||||||||||||||||||||||||||
| PRIDE | P08311. | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| Ensembl | ENST00000216336; ENSP00000216336; ENSG00000100448; Homo sapiens. [Genome view] | ||||||||||||||||||||||||||||||
| GeneID | 1511. | ||||||||||||||||||||||||||||||
| KEGG | hsa:1511. | ||||||||||||||||||||||||||||||
| UCSC | uc001wpq.1. human. | ||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||
| CTD | 1511. | ||||||||||||||||||||||||||||||
| GeneCards | GC14M024112. | ||||||||||||||||||||||||||||||
| H-InvDB | HIX0011576. | ||||||||||||||||||||||||||||||
| HGNC | HGNC:2532. CTSG. | ||||||||||||||||||||||||||||||
| HPA | CAB000110. | ||||||||||||||||||||||||||||||
| MIM | 116830. gene. | ||||||||||||||||||||||||||||||
| PharmGKB | PA27032. | ||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| HOGENOM | P08311. | ||||||||||||||||||||||||||||||
| HOVERGEN | P08311. | ||||||||||||||||||||||||||||||
| OMA | ICVGDRR. | ||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||
| BRENDA | 3.4.21.20. 247. | ||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||
| ArrayExpress | P08311. | ||||||||||||||||||||||||||||||
| Bgee | P08311. | ||||||||||||||||||||||||||||||
| CleanEx | HS_CTSG. | ||||||||||||||||||||||||||||||
| Genevestigator | P08311. | ||||||||||||||||||||||||||||||
| GermOnline | ENSG00000100448. Homo sapiens. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| InterPro | IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view] | ||||||||||||||||||||||||||||||
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| PRINTS | PR00722. CHYMOTRYPSIN. | ||||||||||||||||||||||||||||||
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| PROSITE | PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] | ||||||||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||||||||
| NextBio | 6257. | ||||||||||||||||||||||||||||||
| PMAP-CutDB | P08311. | ||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | CATG_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P08311 Secondary accession number(s): Q6IBJ6, Q9UCA5, Q9UCU6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 14 Human chromosome 14: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


