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UniProtKB/Swiss-Prot entry P08311


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CATG_HUMAN
Primary accession number P08311
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 1, 1990 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 90)
Name and origin of the protein
Protein name Cathepsin G [Precursor]
Synonyms CG
EC 3.4.21.20
Gene name
Name: CTSG
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2569462 [NCBI, ExPASy, EBI, Israel, Japan]
Hohn P.A., Popescu N.C., Hanson R.D., Salvesen G., Ley T.J.;
"Genomic organization and chromosomal localization of the human cathepsin G gene.";
J. Biol. Chem. 264:13412-13419(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00382a032; PubMed=3304423 [NCBI, ExPASy, EBI, Israel, Japan]
Salvesen G., Farley D., Shuman J., Przybyla A., Reilly C., Travis J.;
"Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases.";
Biochemistry 26:2289-2293(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 21-45.
DOI=10.1016/0003-2697(86)90612-3; PubMed=3799965 [NCBI, ExPASy, EBI, Israel, Japan]
Heck L.W., Rostand K.S., Hunter F.A., Bhown A.;
"Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors.";
Anal. Biochem. 158:217-227(1986).
[5]
PROTEIN SEQUENCE OF 21-36.
PubMed=2501794 [NCBI, ExPASy, EBI, Israel, Japan]
Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., Seeger M., Nathan C.F.;
"Antibiotic proteins of human polymorphonuclear leukocytes.";
Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989).
[6]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=8896442 [NCBI, ExPASy, EBI, Israel, Japan]
Hof P., Mayr I., Huber R., Korzus E., Potempa J., Travis J., Powers J.C., Bode W.;
"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.";
EMBO J. 15:5481-5491(1996).
[7]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medrano F.J., Bode W., Banbula A., Potempa J.;
Submitted (SEP-1997) to the PDB data bank.
[8]
VARIANT SER-125.
DOI=10.1007/BF00230230; PubMed=8454293 [NCBI, ExPASy, EBI, Israel, Japan]
Luedecke B., Poller W., Olek K., Bartholome K.;
"Sequence variant of the human cathepsin G gene.";
Hum. Genet. 91:83-84(1993).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M16117; AAA52126.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04990; AAA51919.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014460; AAH14460.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A32627; A27122.
RefSeq NP_001902.1; -.
UniGene Hs.421724
3D structure databases
PDB
1AU8; X-ray; 1.90 A; A=21-244.[ExPASy / RCSB / EBI]
1CGH; X-ray; 1.80 A; A=21-244.[ExPASy / RCSB / EBI]
1KYN; X-ray; 3.50 A; A/B=21-255.[ExPASy / RCSB / EBI]
1T32; X-ray; 1.85 A; A=21-244.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AU8; -.
1CGH; -.
1KYN; -.
1T32; -.
ModBase P08311.
Protein family/group databases
MEROPS S01.133; -.
Organism-specific databases
H-InvDB HIX0011576; -.
HGNC HGNC:2532; CTSG.
GenAtlas CTSG.
HPA CAB000110; -.
MIM 116830; gene. [NCBI / EBI]
PharmGKB PA27032; -.
GeneCards P08311.
Gene expression databases
ArrayExpress P08311; -.
CleanEx HS_CTSG; -.
GermOnline ENSG00000100448; Homo sapiens.
Ontologies
GO
GO:0004252; Molecular function: serine-type endopeptidase activity (traceable author statement from ProtInc).
GO:0006955; Biological process: immune response (traceable author statement from ProtInc).
GO:0006508; Biological process: proteolysis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.
Pfam PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PRINTS PR00722; CHYMOTRYPSIN.
SMART SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P08311.
ProtoNet P08311.
Proteomic databases
PeptideAtlas P08311; -.
Genome annotation databases
Ensembl ENSG00000100448; Homo sapiens. [Contig view]
GeneID 1511; -.
KEGG hsa:1511; -.
Phylogenomic databases
HOGENOM P08311; -.
HOVERGEN P08311; -.
Other
LinkHub P08311; -.
NextBio 6257; -.
SOURCE CTSG; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; Polymorphism; Protease; Serine protease; Signal; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
PROPEP   19    20  2     Activation peptide. PRO_0000027512
CHAIN   21   255  235     Cathepsin G. PRO_0000027513
DOMAIN   21   243  223     Peptidase S1. 
ACT_SITE   64    64        Charge relay system. 
ACT_SITE   108   108        Charge relay system. 
ACT_SITE   201   201        Charge relay system. 
CARBOHYD   71    71        N-linked (GlcNAc...). 
DISULFID   49    65         
DISULFID   142   207         
DISULFID   172   186         
VARIANT   125   125  1     N -> S. VAR_006491 [3D]
CONFLICT   39    39        Q -> E (in Ref. 2). 
CONFLICT   41    43        QSP -> TSG (in Ref. 2). 
TURN   41    43  3      
STRAND   55    61  7      
STRAND   71    75  5      
STRAND   87    96  10      
STRAND   102   104  3      
STRAND   110   116  7      
STRAND   141   147  7      
STRAND   150   153  4      
STRAND   160   165  6      
HELIX   169   173  5      
TURN   181   183  3      
STRAND   184   187  4      
STRAND   204   217  14      
STRAND   226   230  5      
HELIX   231   233  3      
HELIX   235   242  8      
Sequence information
Length: 255 AA [This is the length of the unprocessed precursor] Molecular weight: 28837 Da [This is the MW of the unprocessed precursor] CRC64: 6228E741E6A43889 [This is a checksum on the sequence]
        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 

P08311 in FASTA format

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