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P08311 (CATG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cathepsin G

Short name=CG
EC=3.4.21.20
Gene names
Name:CTSG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cell surface Ref.6.

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 Ref.6

KM=0.26 mM for Suc-Ala-Ala-Pro-Phe-SBzl

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionAntibiotic
Antimicrobial
Hydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiotensin maturation

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

defense response to fungus

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

immune response

Traceable author statement Ref.2. Source: ProtInc

negative regulation of growth of symbiont in host

Inferred from electronic annotation. Source: Ensembl

neutrophil mediated killing of gram-positive bacterium

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of immune response

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from direct assay Ref.9. Source: UniProtKB

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

plasma membrane

Inferred from direct assay Ref.9. Source: UniProtKB

secretory granule

Inferred from direct assay PubMed 11907569. Source: MGI

   Molecular_functionheparin binding

Inferred from direct assay PubMed 11907569. Source: MGI

peptidase activity

Inferred from direct assay PubMed 11907569. Source: MGI

serine-type endopeptidase activity

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Propeptide19 – 202Activation peptide
PRO_0000027512
Chain21 – 255235Cathepsin G
PRO_0000027513

Regions

Domain21 – 243223Peptidase S1

Sites

Active site641Charge relay system
Active site1081Charge relay system
Active site2011Charge relay system

Amino acid modifications

Glycosylation711N-linked (GlcNAc...)
Disulfide bond49 ↔ 65
Disulfide bond142 ↔ 207
Disulfide bond172 ↔ 186

Natural variations

Natural variant1251N → S. Ref.15
Corresponds to variant rs45567233 [ dbSNP | Ensembl ].
VAR_006491

Secondary structure

..................................... 255
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08311 [UniParc].

Last modified January 1, 1990. Version 2.
Checksum: 6228E741E6A43889

FASTA25528,837
        10         20         30         40         50         60 
MQPLLLLLAF LLPTGAEAGE IIGGRESRPH SRPYMAYLQI QSPAGQSRCG GFLVREDFVL 

        70         80         90        100        110        120 
TAAHCWGSNI NVTLGAHNIQ RRENTQQHIT ARRAIRHPQY NQRTIQNDIM LLQLSRRVRR 

       130        140        150        160        170        180 
NRNVNPVALP RAQEGLRPGT LCTVAGWGRV SMRRGTDTLR EVQLRVQRDR QCLRIFGSYD 

       190        200        210        220        230        240 
PRRQICVGDR RERKAAFKGD SGGPLLCNNV AHGIVSYGKS SGVPPEVFTR VSSFLPWIRT 

       250 
TMRSFKLLDQ METPL 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A MICROBICIDE, ENZYME REGULATION.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[14]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).
[15]"Sequence variant of the human cathepsin G gene."
Luedecke B., Poller W., Olek K., Bartholome K.
Hum. Genet. 91:83-84(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9631.1.
PIRA27122. A32627.
RefSeqNP_001902.1. NM_001911.2.
UniGeneHs.421724.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AU8X-ray1.90A21-244[»]
1CGHX-ray1.80A21-244[»]
1KYNX-ray3.50A/B21-255[»]
1T32X-ray1.85A21-239[»]
ProteinModelPortalP08311.
SMRP08311. Positions 21-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107891. 6 interactions.
IntActP08311. 2 interactions.
MINTMINT-4054534.
STRING9606.ENSP00000216336.

Chemistry

BindingDBP08311.
ChEMBLCHEMBL4071.
GuidetoPHARMACOLOGY2348.

Protein family/group databases

MEROPSS01.133.

PTM databases

PhosphoSiteP08311.

Polymorphism databases

DMDM115725.

Proteomic databases

MaxQBP08311.
PaxDbP08311.
PeptideAtlasP08311.
PRIDEP08311.

Protocols and materials databases

DNASU1511.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216336; ENSP00000216336; ENSG00000100448.
GeneID1511.
KEGGhsa:1511.
UCSCuc001wpq.3. human.

Organism-specific databases

CTD1511.
GeneCardsGC14M025042.
HGNCHGNC:2532. CTSG.
HPACAB000110.
HPA047737.
MIM116830. gene.
neXtProtNX_P08311.
PharmGKBPA27032.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251820.
HOVERGENHBG013304.
InParanoidP08311.
KOK01319.
OMAQHITARR.
OrthoDBEOG7RRF7Z.
PhylomeDBP08311.
TreeFamTF333630.

Enzyme and pathway databases

BRENDA3.4.21.20. 2681.
ReactomeREACT_118779. Extracellular matrix organization.
REACT_17015. Metabolism of proteins.
SABIO-RKP08311.

Gene expression databases

BgeeP08311.
CleanExHS_CTSG.
GenevestigatorP08311.

Family and domain databases

InterProIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08311.
GeneWikiCathepsin_G.
GenomeRNAi1511.
NextBio6257.
PMAP-CutDBP08311.
PROP08311.
SOURCESearch...

Entry information

Entry nameCATG_HUMAN
AccessionPrimary (citable) accession number: P08311
Secondary accession number(s): Q6IBJ6, Q9UCA5, Q9UCU6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM