Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cathepsin G

Gene

CTSG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

Specificity similar to chymotrypsin C.

Enzyme regulationi

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.3 Publications

Kineticsi

  1. KM=1.15 mM for Z-Lys-SBzl1 Publication
  2. KM=0.26 mM for Suc-Ala-Ala-Pro-Phe-SBzl1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei64 – 641Charge relay system
Active sitei108 – 1081Charge relay system
Active sitei201 – 2011Charge relay system

GO - Molecular functioni

  1. heparin binding Source: MGI
  2. peptidase activity Source: MGI
  3. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. angiotensin maturation Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. defense response to fungus Source: Ensembl
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. immune response Source: ProtInc
  7. negative regulation of growth of symbiont in host Source: Ensembl
  8. neutrophil mediated killing of gram-positive bacterium Source: Ensembl
  9. positive regulation of immune response Source: Ensembl
  10. protein processing Source: GO_Central
  11. proteolysis Source: UniProtKB
  12. response to lipopolysaccharide Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.20. 2681.
ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
SABIO-RKP08311.

Protein family/group databases

MEROPSiS01.133.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin G (EC:3.4.21.20)
Short name:
CG
Gene namesi
Name:CTSG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:2532. CTSG.

Subcellular locationi

Cell surface 1 Publication

GO - Cellular componenti

  1. cell surface Source: UniProtKB-SubCell
  2. extracellular region Source: Reactome
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: UniProtKB
  7. secretory granule Source: MGI
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27032.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Propeptidei19 – 202Activation peptide5 PublicationsPRO_0000027512
Chaini21 – 255235Cathepsin GPRO_0000027513Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 65
Glycosylationi71 – 711N-linked (GlcNAc...)
Disulfide bondi142 ↔ 207
Disulfide bondi172 ↔ 186

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiP08311.
PaxDbiP08311.
PeptideAtlasiP08311.
PRIDEiP08311.

PTM databases

PhosphoSiteiP08311.

Miscellaneous databases

PMAP-CutDBP08311.

Expressioni

Gene expression databases

BgeeiP08311.
CleanExiHS_CTSG.
GenevestigatoriP08311.

Organism-specific databases

HPAiCAB000110.
HPA047737.

Interactioni

Protein-protein interaction databases

BioGridi107891. 15 interactions.
IntActiP08311. 2 interactions.
MINTiMINT-4054534.
STRINGi9606.ENSP00000216336.

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 417Combined sources
Turni42 – 454Combined sources
Beta strandi48 – 558Combined sources
Beta strandi58 – 614Combined sources
Helixi63 – 653Combined sources
Beta strandi68 – 758Combined sources
Beta strandi87 – 9610Combined sources
Turni102 – 1054Combined sources
Beta strandi110 – 1167Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi150 – 1534Combined sources
Beta strandi160 – 1667Combined sources
Helixi169 – 1757Combined sources
Turni181 – 1833Combined sources
Beta strandi184 – 1874Combined sources
Beta strandi204 – 2074Combined sources
Beta strandi210 – 2178Combined sources
Beta strandi226 – 2305Combined sources
Helixi231 – 2344Combined sources
Helixi235 – 2439Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AU8X-ray1.90A21-244[»]
1CGHX-ray1.80A21-244[»]
1KYNX-ray3.50A/B21-255[»]
1T32X-ray1.85A21-239[»]
ProteinModelPortaliP08311.
SMRiP08311. Positions 21-244.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08311.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 243223Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP08311.
KOiK01319.
OMAiQHITARR.
OrthoDBiEOG7RRF7Z.
PhylomeDBiP08311.
TreeFamiTF333630.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08311-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQPLLLLLAF LLPTGAEAGE IIGGRESRPH SRPYMAYLQI QSPAGQSRCG
60 70 80 90 100
GFLVREDFVL TAAHCWGSNI NVTLGAHNIQ RRENTQQHIT ARRAIRHPQY
110 120 130 140 150
NQRTIQNDIM LLQLSRRVRR NRNVNPVALP RAQEGLRPGT LCTVAGWGRV
160 170 180 190 200
SMRRGTDTLR EVQLRVQRDR QCLRIFGSYD PRRQICVGDR RERKAAFKGD
210 220 230 240 250
SGGPLLCNNV AHGIVSYGKS SGVPPEVFTR VSSFLPWIRT TMRSFKLLDQ

METPL
Length:255
Mass (Da):28,837
Last modified:December 31, 1989 - v2
Checksum:i6228E741E6A43889
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti125 – 1251N → S.1 Publication
Corresponds to variant rs45567233 [ dbSNP | Ensembl ].
VAR_006491

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9631.1.
PIRiA32627. A27122.
RefSeqiNP_001902.1. NM_001911.2.
UniGeneiHs.421724.

Genome annotation databases

EnsembliENST00000216336; ENSP00000216336; ENSG00000100448.
GeneIDi1511.
KEGGihsa:1511.
UCSCiuc001wpq.3. human.

Polymorphism databases

DMDMi115725.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9631.1.
PIRiA32627. A27122.
RefSeqiNP_001902.1. NM_001911.2.
UniGeneiHs.421724.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AU8X-ray1.90A21-244[»]
1CGHX-ray1.80A21-244[»]
1KYNX-ray3.50A/B21-255[»]
1T32X-ray1.85A21-239[»]
ProteinModelPortaliP08311.
SMRiP08311. Positions 21-244.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107891. 15 interactions.
IntActiP08311. 2 interactions.
MINTiMINT-4054534.
STRINGi9606.ENSP00000216336.

Chemistry

BindingDBiP08311.
ChEMBLiCHEMBL4071.
GuidetoPHARMACOLOGYi2348.

Protein family/group databases

MEROPSiS01.133.

PTM databases

PhosphoSiteiP08311.

Polymorphism databases

DMDMi115725.

Proteomic databases

MaxQBiP08311.
PaxDbiP08311.
PeptideAtlasiP08311.
PRIDEiP08311.

Protocols and materials databases

DNASUi1511.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216336; ENSP00000216336; ENSG00000100448.
GeneIDi1511.
KEGGihsa:1511.
UCSCiuc001wpq.3. human.

Organism-specific databases

CTDi1511.
GeneCardsiGC14M025042.
HGNCiHGNC:2532. CTSG.
HPAiCAB000110.
HPA047737.
MIMi116830. gene.
neXtProtiNX_P08311.
PharmGKBiPA27032.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118895.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP08311.
KOiK01319.
OMAiQHITARR.
OrthoDBiEOG7RRF7Z.
PhylomeDBiP08311.
TreeFamiTF333630.

Enzyme and pathway databases

BRENDAi3.4.21.20. 2681.
ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
SABIO-RKP08311.

Miscellaneous databases

EvolutionaryTraceiP08311.
GeneWikiiCathepsin_G.
GenomeRNAii1511.
NextBioi6257.
PMAP-CutDBP08311.
PROiP08311.
SOURCEiSearch...

Gene expression databases

BgeeiP08311.
CleanExiHS_CTSG.
GenevestigatoriP08311.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1986) [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(1988) [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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. 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(2003) [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(1993) [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(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-45.
  8. 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(1990) [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(1994) [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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A MICROBICIDE, ENZYME REGULATION.
  12. 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(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  14. Medrano F.J., Bode W., Banbula A., Potempa J.
    Submitted (AUG-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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-125.

Entry informationi

Entry nameiCATG_HUMAN
AccessioniPrimary (citable) accession number: P08311
Secondary accession number(s): Q6IBJ6, Q9UCA5, Q9UCU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1988
Last sequence update: December 31, 1989
Last modified: March 3, 2015
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.