[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Swiss Webster; TISSUE=Embryonic fibroblast; PubMed=8453108 [NCBI, ExPASy, EBI, Israel, Japan] Heusel J.W., Scarpati E.M., Jenkins N.A., Gilbert D.J., Copeland N.G., Shapiro S.D., Ley T.J.; "Molecular cloning, chromosomal location, and tissue-specific expression of the murine cathepsin G gene."; Blood 81:1614-1623(1993).
[2]	NUCLEOTIDE SEQUENCE. Kulmburg P., Baumruker T., Werner F.; Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE. STRAIN=Leaden X A1; Huang R., Aveskogh M., Hellman L.T.; Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
[4]	PROTEIN SEQUENCE OF 21-60. PubMed=1577012 [NCBI, ExPASy, EBI, Israel, Japan] Nakamura N., Tsuru A., Hirayoshi K., Nagata K.; "Purification and characterization of a vimentin-specific protease in mouse myeloid leukemia cells. Regulation during differentiation and identity with cathepsin G."; Eur. J. Biochem. 205:947-954(1992).

Comments

FUNCTION: This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis.
CATALYTIC ACTIVITY: Specificity similar to chymotrypsin C.
SUBCELLULAR LOCATION: Membrane. Note=Strongly associated with membranes.
SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

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

M96801; AAA37376.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X70057; CAA49661.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X78544; CAA55290.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S40162; S40162.

NP_031826.1; -.

3D structure databases

HSSP

P00760; 1EZX. [HSSP ENTRY / PDB]

SMR

P28293; 21-243.

ModBase

P28293.

Protein family/group databases

MEROPS

S01.133; -.

Organism-specific databases

MGI

MGI:88563; Ctsg.

Gene expression databases

ArrayExpress

P28293; -.

CleanEx

MM_CTSG; -.

GermOnline

ENSMUSG00000040314; Mus musculus.

Ontologies

GO:0005882;	Cellular component: intermediate filament (inferred from electronic annotation from UniProtKB-KW).
GO:0016020;	Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
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).

Genome annotation databases

Ensembl

ENSMUSG00000040314; Mus musculus. [Contig view]

GeneID

13035; -.

KEGG

mmu:13035; -.

Phylogenomic databases

HOGENOM

P28293; -.

HOVERGEN

P28293; -.

Other

NextBio

282916; -.

SOURCE

Ctsg; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycoprotein; Hydrolase; Intermediate filament; Membrane; Protease; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`	`By similarity.`
`PROPEP`	`19 20`	`2`	`Activation peptide.`	`PRO_0000027514`
`CHAIN`	`21 261`	`241`	`Cathepsin G.`	`PRO_0000027515`
`DOMAIN`	`21 243`	`223`	`Peptidase S1.`
`ACT_SITE`	`64 64`		`Charge relay system (By similarity).`
`ACT_SITE`	`108 108`		`Charge relay system (By similarity).`
`ACT_SITE`	`201 201`		`Charge relay system (By similarity).`
`CARBOHYD`	`71 71`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`49 65`		`By similarity.`
`DISULFID`	`142 207`		`By similarity.`
`DISULFID`	`172 186`		`By similarity.`
`CONFLICT`	`51 51`		`G -> S (in Ref. 4; AA sequence).`
`CONFLICT`	`56 56`		`E -> G (in Ref. 4; AA sequence).`
`CONFLICT`	`60 60`		`L -> P (in Ref. 4; AA sequence).`

Sequence information

Length: 261 AA [This is the length of the unprocessed precursor]

Molecular weight: 29096 Da [This is the MW of the unprocessed precursor]

CRC64: 5EFA1A6E10E1D7FC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQPLLLLLTF ILLQGDEAGK IIGGREARPH SYPYMAFLLI QSPEGLSACG GFLVREDFVL 

        70         80         90        100        110        120 
TAAHCLGSSI NVTLGAHNIQ MRERTQQLIT VLRAIRHPDY NPQNIRNDIM LLQLRRRARR 

       130        140        150        160        170        180 
SGSVKPVALP QASKKLQPGD LCTVAGWGRV SQSRGTNVLQ EVQLRVQMDQ MCANRFQFYN 

       190        200        210        220        230        240 
SQTQICVGNP RERKSAFRGD SGGPLVCSNV AQGIVSYGSN NGNPPAVFTK IQSFMPWIKR 

       250        260 
TMRRFAPRYQ RPANSLSQAQ T

P28293 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools