[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Crossbred X Angus; TISSUE=Ileum; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[2]	PROTEIN SEQUENCE OF 115-331. TISSUE=Spleen; DOI=10.1016/0014-5793(91)80620-I; PubMed=2044774 [NCBI, ExPASy, EBI, Israel, Japan] Ritonja A., Colic A., Dolenc I., Ogrinc T., Podobnik M., Turk V.; "The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L."; FEBS Lett. 283:329-331(1991).
[3]	PROTEIN SEQUENCE OF 115-331. TISSUE=Spleen; PubMed=1515067 [NCBI, ExPASy, EBI, Israel, Japan] Dolenc I., Ritonja A., Colic A., Podobnik M., Ogrinc T., Turk V.; "Bovine cathepsins S and L: isolation and amino acid sequences."; Biol. Chem. Hoppe-Seyler 373:407-412(1992).
[4]	PROTEIN SEQUENCE OF 115-331, AND NUCLEOTIDE SEQUENCE [MRNA] OF 136-331. TISSUE=Spleen; DOI=10.1016/0014-5793(91)80971-5; PubMed=1864368 [NCBI, ExPASy, EBI, Israel, Japan] Wiederanders B., Broemme D., Kirschke H., Kalkkinen N., Rinne A., Paquette T., Toothman P.; "Primary structure of bovine cathepsin S. Comparison to cathepsins L, H, B and papain."; FEBS Lett. 286:189-192(1991).
[5]	CHARACTERIZATION. PubMed=2604727 [NCBI, ExPASy, EBI, Israel, Japan] Broemme D., Steinert A., Friebe S., Fittkau S., Wiederanders B., Kirschke H.; "The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsins L and B."; Biochem. J. 264:475-481(1989).

Comments

FUNCTION: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
CATALYTIC ACTIVITY: Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Lysosome.
SIMILARITY: Belongs to the peptidase C1 family [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

BC102245; AAI02246.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M95211; AAA30435.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X62001; CAA43971.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S15844; S15844.

NP_001028787.1; -.

3D structure databases

HSSP

P25774; 1MS6. [HSSP ENTRY / PDB]

SMR

P25326; 18-331.

ModBase

P25326.

Protein family/group databases

MEROPS

C01.034; -.

Ontologies

GO:0005764;	Cellular component: lysosome (inferred from electronic annotation from UniProtKB-KW).
GO:0004197;	Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000169; Pept_cys_AS.
IPR013128; Peptidase_C1A.
IPR000668; Peptidase_C1A_C.
IPR013201; Prot_inhib_I29.
Graphical view of domain structure.

PANTHER

PTHR12411; Peptidase_C1A; 1.

Pfam

PF08246; Inhibitor_I29; 1.
PF00112; Peptidase_C1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00705; PAPAIN.

ProDom

PD000158; Peptidase_C1; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00645; Pept_C1; 1.
SMART graphical view of domain structure.

PROSITE

PS00640; THIOL_PROTEASE_ASN; 1.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; 1.

ProtoNet

P25326.

Genome annotation databases

Ensembl

ENSBTAG00000017135; Bos taurus. [Contig view]

GeneID

327711; -.

KEGG

bta:327711; -.

Phylogenomic databases

HOVERGEN

P25326; -.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 16`	`16`	`Potential.`
`PROPEP`	`17 114`	`98`	`Activation peptide.`	`PRO_0000238120`
`CHAIN`	`115 331`	`217`	`Cathepsin S.`	`PRO_0000050543`
`ACT_SITE`	`139 139`		`By similarity.`
`ACT_SITE`	`278 278`		`By similarity.`
`ACT_SITE`	`298 298`		`By similarity.`
`CARBOHYD`	`104 104`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`126 224`		`By similarity.`
`DISULFID`	`136 180`		`By similarity.`
`DISULFID`	`170 213`		`By similarity.`
`DISULFID`	`272 320`		`By similarity.`

Sequence information

Length: 331 AA [This is the length of the unprocessed precursor]

Molecular weight: 37176 Da [This is the MW of the unprocessed precursor]

CRC64: 7F5547389F75DD58 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNWLVWALLL CSSAMAHVHR DPTLDHHWDL WKKTYGKQYK EKNEEVARRL IWEKNLKTVT 

        70         80         90        100        110        120 
LHNLEHSMGM HSYELGMNHL GDMTSEEVIS LMSSLRVPSQ WPRNVTYKSD PNQKLPDSMD 

       130        140        150        160        170        180 
WREKGCVTEV KYQGACGSCW AFSAVGALEA QVKLKTGKLV SLSAQNLVDC STAKYGNKGC 

       190        200        210        220        230        240 
NGGFMTEAFQ YIIDNNGIDS EASYPYKAMD GKCQYDVKNR AATCSRYIEL PFGSEEALKE 

       250        260        270        280        290        300 
AVANKGPVSV GIDASHSSFF LYKTGVYYDP SCTQNVNHGV LVVGYGNLDG KDYWLVKNSW 

       310        320        330 
GLHFGDQGYI RMARNSGNHC GIANYPSYPE I

P25326 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