[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00276893; PubMed=8341259 [NCBI, ExPASy, EBI, Israel, Japan] Dargatz H., Diefenthal T., Witte V., Reipen G., von Wettstein D.; "The heterodimeric protease clostripain from Clostridium histolyticum is encoded by a single gene."; Mol. Gen. Genet. 240:140-145(1993).
[2]	PROTEIN SEQUENCE OF 51-181. PubMed=6391922 [NCBI, ExPASy, EBI, Israel, Japan] Gilles A.M., Lecroisey A., Keil B.; "Primary structure of alpha-clostripain light chain."; Eur. J. Biochem. 145:469-476(1984).
[3]	PRELIMINARY PROTEIN SEQUENCE OF 51-73 AND 191-232. PubMed=6337850 [NCBI, ExPASy, EBI, Israel, Japan] Gilles A.M., de Wolf A., Keil B.; "Amino-acid sequences of the active-site sulfhydryl peptide and other thiol peptides from the cysteine proteinase alpha-clostripain."; Eur. J. Biochem. 130:473-479(1983).

Comments

FUNCTION: Cysteine endopeptidase with strict specificity.
CATALYTIC ACTIVITY: Preferential cleavage: Arg-|-Xaa, including Arg-|-Pro bond, but not Lys-|-Xaa.
SUBUNIT: Heterodimer of a light chain and an heavy chain held together by strong noncovalent forces rather than by intramolecular disulfide bridges.
SIMILARITY: Belongs to the peptidase C11 family [view classification].
WEB RESOURCE: Name=Worthington enzyme manual; URL="http://www.worthington-biochem.com/CP/";.

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

X63673; CAA45212.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A29174; A29174.
A29175; A29175.
B29175; B29175.
S35190; S35190.

3D structure databases

ModBase

P09870.

Protein family/group databases

MEROPS

C11.001; -.

Ontologies

GO:0008234;	Molecular function: cysteine-type peptidase activity (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR014173; Pept_C11_CLOspp.
IPR005077; Peptidase_C11.
Graphical view of domain structure.

Pfam

PF03415; Peptidase_C11; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02806; clostrip; 1.

Other

ProtoNet

P09870.

UniRef

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

Keywords

Direct protein sequencing; Hydrolase; Protease; Signal; Thiol protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 27`	`27`	`Potential.`
`PROPEP`	`28 50`	`23`	`Potential.`	`PRO_0000028511`
`CHAIN`	`51 181`	`131`	`Clostripain light chain.`	`PRO_0000028512`
`PROPEP`	`182 190`	`9`	`Linker.`	`PRO_0000028513`
`CHAIN`	`191 526`	`336`	`Clostripain heavy chain.`	`PRO_0000028514`
`ACT_SITE`	`231 231`
`CONFLICT`	`127 127`		`R -> NQL (in Ref. 2; AA sequence).`
`CONFLICT`	`176 179`		`HGGG -> GDGH (in Ref. 2; AA sequence).`
`CONFLICT`	`197 197`		`S -> H (in Ref. 3; AA sequence).`
`CONFLICT`	`213 213`		`I -> L (in Ref. 3; AA sequence).`
`CONFLICT`	`216 216`		`H -> T (in Ref. 3; AA sequence).`
`CONFLICT`	`232 232`		`L -> M (in Ref. 3; AA sequence).`

Sequence information

Length: 526 AA [This is the length of the unprocessed precursor]

Molecular weight: 59733 Da [This is the MW of the unprocessed precursor]

CRC64: E151372FF6C95BE7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLRRKVSTLL MTALITTSFL NSKPVYANPV TKSKDNNLKE VQQVTSKSNK NKNQKVTIMY 

        70         80         90        100        110        120 
YCDADNNLEG SLLNDIEEMK TGYKDSPNLN LIALVDRSPR YSSDEKVLGE DFSDTRLYKI 

       130        140        150        160        170        180 
EHNKANRLDG KNEFPEISTT SKYEANMGDP EVLKKFIDYC KSNYEADKYV LIMANHGGGA 

       190        200        210        220        230        240 
REKSNPRLNR AICWDDSNLD KNGEADCLYM GEISDHLTEK QSVDLLAFDA CLMGTAEVAY 

       250        260        270        280        290        300 
QYRPGNGGFS ADTLVASSPV VWGPGFKYDK IFDRIKAGGG TNNEDDLTLG GKEQNFDPAT 

       310        320        330        340        350        360 
ITNEQLGALF VEEQRDSTHA NGRYDQHLSF YDLKKAESVK RAIDNLAVNL SNENKKSEIE 

       370        380        390        400        410        420 
KLRGSGIHTD LMHYFDEYSE GEWVEYPYFD VYDLCEKINK SENFSSKTKD LASNAMNKLN 

       430        440        450        460        470        480 
EMIVYSFGDP SNNFKEGKNG LSIFLPNGDK KYSTYYTSTK IPHWTMQSWY NSIDTVKYGL 

       490        500        510        520 
NPYGKLSWCK DGQDPEINKV GNWFELLDSW FDKTNDVTGG VNHYQW

P09870 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