P08311 (CATG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cathepsin G
Short name=CG
EC=3.4.21.20

Gene names

Name:

CTSG

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	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 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 Reference proteome
Gene Ontology (GO)
Biological_process	defense response to fungus Inferred from electronic annotation. Source: Compara extracellular matrix disassembly 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: Compara neutrophil mediated killing of gram-positive bacterium Inferred from electronic annotation. Source: Compara positive regulation of immune response Inferred from electronic annotation. Source: Compara proteolysis Inferred from direct assay Ref.9. Source: UniProtKB response to lipopolysaccharide Inferred from electronic annotation. Source: Compara
Cellular_component	cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL plasma membrane Inferred from direct assay Ref.9. Source: UniProtKB secretory granule Inferred from direct assay PubMed 11907569. Source: MGI
Molecular_function	heparin binding 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 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. Ref.15
Corresponds to variant rs45567233 [ dbSNP | Ensembl ].

VAR_006491

Secondary structure

1

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255

Helix Strand Turn

Details...

Beta strand

35 – 41

7

Turn

42 – 45

4

Beta strand

48 – 55

8

Beta strand

58 – 61

4

Helix

63 – 65

3

Beta strand

68 – 75

8

Beta strand

87 – 96

10

Turn

102 – 105

4

Beta strand

110 – 116

7

Beta strand

141 – 147

7

Beta strand

150 – 153

4

Beta strand

160 – 166

7

Helix

169 – 175

7

Turn

181 – 183

3

Beta strand

184 – 187

4

Beta strand

204 – 207

4

Beta strand

210 – 217

8

Beta strand

226 – 230

5

Helix

231 – 234

4

Helix

235 – 243

9

Sequences

	Sequence		Length	Mass (Da)
	P08311 [UniParc]. Last modified January 1, 1990. Version 2. Checksum: 6228E741E6A43889	FASTA	255	28,837
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00028064.

PIR

A27122. A32627.

RefSeq

NP_001902.1. NM_001911.2.

UniGene

Hs.421724.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AU8	X-ray	1.90	A	21-244	[»]
1CGH	X-ray	1.80	A	21-244	[»]
1KYN	X-ray	3.50	A/B	21-255	[»]
1T32	X-ray	1.85	A	21-239	[»]

ProteinModelPortal

P08311.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08311. 1 interaction.

MINT

MINT-4054534.

STRING

9606.ENSP00000216336.

Protein family/group databases

MEROPS

S01.133.

PTM databases

PhosphoSite

P08311.

Polymorphism databases

DMDM

115725.

Proteomic databases

PaxDb

P08311.

PeptideAtlas

P08311.

PRIDE

P08311.

Protocols and materials databases

DNASU

1511.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216336; ENSP00000216336; ENSG00000100448.

GeneID

1511.

KEGG

hsa:1511.

UCSC

uc001wpq.3. human.

Organism-specific databases

CTD

1511.

GeneCards

GC14M025042.

HGNC

HGNC:2532. CTSG.

HPA

CAB000110.

MIM

116830. gene.

neXtProt

NX_P08311.

PharmGKB

PA27032.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5640.

HOGENOM

HOG000251820.

HOVERGEN

HBG013304.

InParanoid

P08311.

KO

K01319.

OMA

QHITARR.

OrthoDB

EOG4KWJTW.

PhylomeDB

P08311.

Enzyme and pathway databases

BRENDA

3.4.21.20. 2681.

Reactome

REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.
REACT_17015. Metabolism of proteins.

Gene expression databases

Bgee

P08311.

CleanEx

HS_CTSG.

Genevestigator

P08311.

GermOnline

ENSG00000100448. Homo sapiens.

Family and domain databases

InterPro

IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P08311.

ChEMBL

CHEMBL4071.

EvolutionaryTrace

P08311.

GenomeRNAi

1511.

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

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 135 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.