Reviewed, UniProtKB/Swiss-Prot P25326 (CATS_BOVIN)

Names and origin

Protein names

Recommended name:
    Cathepsin S
    EC=3.4.22.27

Gene names

Name:

CTSS

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 structure	Monomer.
Subcellular location	Lysosome.
Sequence similarities	Belongs to the peptidase C1 family.

Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Hydrolase Protease Thiol protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 16	16	Potential
	Propeptide	17 – 114	98	Activation peptide		PRO_0000238120
	Chain	115 – 331	217	Cathepsin S		PRO_0000050543
Sites
	Active site	139	1	By similarity
	Active site	278	1	By similarity
	Active site	298	1	By similarity
Amino acid modifications
	Glycosylation	104	1	N-linked (GlcNAc...) Potential
	Disulfide bond	126 ↔ 224		By similarity
	Disulfide bond	136 ↔ 180		By similarity
	Disulfide bond	170 ↔ 213		By similarity
	Disulfide bond	272 ↔ 320		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P25326-1 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: 7F5547389F75DD58	FASTA	331	37,176
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.
[2]	"The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L." Ritonja A., Colic A., Dolenc I., Ogrinc T., Podobnik M., Turk V. FEBS Lett. 283:329-331(1991) [PubMed: 2044774] [Abstract] Cited for: PROTEIN SEQUENCE OF 115-331. Tissue: Spleen.
[3]	"Bovine cathepsins S and L: isolation and amino acid sequences." Dolenc I., Ritonja A., Colic A., Podobnik M., Ogrinc T., Turk V. Biol. Chem. Hoppe-Seyler 373:407-412(1992) [PubMed: 1515067] [Abstract] Cited for: PROTEIN SEQUENCE OF 115-331. Tissue: Spleen.
[4]	"Primary structure of bovine cathepsin S. Comparison to cathepsins L, H, B and papain." Wiederanders B., Broemme D., Kirschke H., Kalkkinen N., Rinne A., Paquette T., Toothman P. FEBS Lett. 286:189-192(1991) [PubMed: 1864368] [Abstract] Cited for: PROTEIN SEQUENCE OF 115-331, NUCLEOTIDE SEQUENCE [MRNA] OF 136-331. Tissue: Spleen.
[5]	"The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsins L and B." Broemme D., Steinert A., Friebe S., Fittkau S., Wiederanders B., Kirschke H. Biochem. J. 264:475-481(1989) [PubMed: 2604727] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC102245 mRNA. Translation: AAI02246.1. M95211 mRNA. Translation: AAA30435.1. X62001 mRNA. Translation: CAA43971.1.
IPI	IPI00702008.
PIR	S15844.
RefSeq	NP_001028787.1.
UniGene	Bt.7938
3D structure databases
HSSP	HSSP built from PDB template 1MS6 based on UniProtKB P25774.
SMR	P25326. Positions 18-331.
ModBase	Search...
Protein-protein interaction databases
STRING	P25326.
Protein family/group databases
MEROPS	C01.034.
Genome annotation databases
Ensembl	ENSBTAT00000022774; ENSBTAP00000022774; ENSBTAG00000017135; Bos taurus. [Genome view]
GeneID	327711.
KEGG	bta:327711.
Organism-specific databases
CTD	327711.
Phylogenomic databases
HOVERGEN	P25326.
Enzyme and pathway databases
BRENDA	3.4.22.27. 251.
Family and domain databases
InterPro	IPR000169. Pept_cys_AS. IPR013128. Peptidase_C1A. IPR000668. Peptidase_C1A_C. IPR013201. Prot_inhib_I29. [Graphical view]
PANTHER	PTHR12411. Peptidase_C1A. 1 hit.
Pfam	PF08246. Inhibitor_I29. 1 hit. PF00112. Peptidase_C1. 1 hit. [Graphical view]
PRINTS	PR00705. PAPAIN.
ProDom	PD000158. Peptidase_C1. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00645. Pept_C1. 1 hit. [Graphical view]
PROSITE	PS00640. THIOL_PROTEASE_ASN. 1 hit. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATS_BOVIN

Accession

Primary (citable) accession number: P25326
Secondary accession number(s): Q3T0V8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 30, 2006
Last modified:	September 1, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)