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Reviewed, UniProtKB/Swiss-Prot O70370 (CATS_MOUSE)

Last modified March 3, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cathepsin S
    EC=3.4.22.27
Gene names
Name: Ctss
Synonyms: Cats
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Subcellular location

Lysosome.

Tissue specificity

Widely expressed with highest expression found in non-skeletal tissues. Relatively high levels found in skeletal tissues. Ref.3

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Gene Ontology (GO)
   Biological processproteolysis

Inferred from direct assay. Source: MGI

   Cellular componentlysosome

Inferred from direct assay. Source: MGI

membrane

Inferred from direct assay. Source: MGI

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 122105Activation peptide Potential
PRO_0000026315
Chain123 – 340218Cathepsin S
PRO_0000026316

Sites

Active site1471 By similarity
Active site2871 By similarity
Active site3071 By similarity

Amino acid modifications

Glycosylation1201N-linked (GlcNAc...) Potential
Disulfide bond134 ↔ 233 By similarity
Disulfide bond144 ↔ 189 By similarity
Disulfide bond178 ↔ 222 By similarity
Disulfide bond281 ↔ 329 By similarity

Natural variations

Natural variant2181T → M

Experimental info

Sequence conflict1 – 2929MRAPG…QLQRD → MAVLDAPGVLCGNGATAER Ref.2
Sequence conflict341Y → H in CAA05360. Ref.2
Sequence conflict971S → L in CAA05360. Ref.2
Sequence conflict1061S → P in CAA05360. Ref.2
Sequence conflict1461A → S Ref.3

Secondary structure

................................................ 340
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O70370-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 068E61126E2E0C0E

FASTA34038,438
        10         20         30         40         50         60 
MRAPGHAAIR WLFWMPLVCS VAMEQLQRDP TLDYHWDLWK KTHEKEYKDK NEEEVRRLIW 

        70         80         90        100        110        120 
EKNLKFIMIH NLEYSMGMHT YQVGMNDMGD MTNEEISCRM GALRISRQSP KTVTFRSYSN 

       130        140        150        160        170        180 
RTLPDTVDWR EKGCVTEVKY QGSCGACWAF SAVGALEGQL KLKTGKLISL SAQNLVDCSN 

       190        200        210        220        230        240 
EEKYGNKGCG GGYMTEAFQY IIDNGGIEAD ASYPYKATDE KCHYNSKNRA ATCSRYIQLP 

       250        260        270        280        290        300 
FGDEDALKEA VATKGPVSVG IDASHSSFFF YKSGVYDDPS CTGNVNHGVL VVGYGTLDGK 

       310        320        330        340 
DYWLVKNSWG LNFGDQGYIR MARNNKNHCG IASYCSYPEI 

« Hide

References

[1]Doh-ura K.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/Sv and BALB/c.
Tissue: Brain.
[2]Rommerskirch W.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen.
[3]"Cathepsin expression during skeletal development."
Soederstroem M., Salminen H., Glumoff V., Kirschke H., Aro H., Vuorio E.
Biochim. Biophys. Acta 1446:35-46(1999) [PubMed: 10395917] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 144-306, TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Cartilage.
[4]"Gene expression in scrapie. Cloning of a new scrapie-responsive gene and the identification of increased levels of seven other mRNA transcripts."
Dandoy-Dron F., Guillo F., Benboudjema L., Deslys J.-P., Lasmesas C., Dormont D., Tovey M.G., Dron M.
J. Biol. Chem. 273:7691-7697(1998) [PubMed: 9516475] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 296-340.
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF051732 expand/collapse EMBL AC list , AF051727, AF051728, AF051729, AF051726, AF051730, AF051731 Genomic DNA. Translation: AAC05781.1.
AF038546 mRNA. Translation: AAB94925.1.
AJ002386 mRNA. Translation: CAA05360.1.
Y18466 mRNA. Translation: CAA77184.1.
AJ223208 mRNA. Translation: CAA11182.1.
IPIIPI00877231.
UniGeneMm.3619

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1M0Hmodel-A1-340[»]
SMRO70370. Positions 26-340.
ModBaseSearch...

Protein family/group databases

MEROPSC01.034.

Proteomic databases

PRIDEO70370.

Genome annotation databases

EnsemblENSMUSG00000038642. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:107341. Ctss.

Phylogenomic databases

HOVERGENO70370.

Enzyme and pathway databases

BRENDA3.4.22.27. 244.

Gene expression databases

ArrayExpressO70370.
BgeeO70370.
CleanExMM_CTSS.
GermOnlineENSMUSG00000038642. Mus musculus.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. Peptidase_C1A. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
ProDomPD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBO70370.
SOURCESearch...

Entry information

Entry nameCATS_MOUSE
AccessionPrimary (citable) accession number: O70370
Secondary accession number(s): O54973
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: August 1, 1998
Last modified: March 3, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents