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O70370

- CATS_MOUSE

UniProt

O70370 - CATS_MOUSE

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Protein
Cathepsin S
Gene
Ctss, Cats
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei147 – 1471 By similarity
Active sitei287 – 2871 By similarity
Active sitei307 – 3071 By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. peptidase activity Source: MGI

GO - Biological processi

  1. basement membrane disassembly Source: BHF-UCL
  2. positive regulation of inflammatory response Source: MGI
  3. proteolysis Source: MGI
  4. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.27. 3474.
ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_197101. Endosomal/Vacuolar pathway.
REACT_198976. Trafficking and processing of endosomal TLR.
REACT_199052. Degradation of the extracellular matrix.
REACT_199112. Endosomal/Vacuolar pathway.

Protein family/group databases

MEROPSiC01.034.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin S (EC:3.4.22.27)
Gene namesi
Name:Ctss
Synonyms:Cats
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:107341. Ctss.

Subcellular locationi

GO - Cellular componenti

  1. early endosome lumen Source: Reactome
  2. lysosome Source: MGI
  3. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed prediction
Add
BLAST
Propeptidei18 – 122105Activation peptide Reviewed prediction
PRO_0000026315Add
BLAST
Chaini123 – 340218Cathepsin S
PRO_0000026316Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi120 – 1201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi134 ↔ 233 By similarity
Disulfide bondi144 ↔ 189 By similarity
Disulfide bondi178 ↔ 222 By similarity
Disulfide bondi281 ↔ 329 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiO70370.
PaxDbiO70370.
PRIDEiO70370.

PTM databases

PhosphoSiteiO70370.

Expressioni

Tissue specificityi

Widely expressed with highest expression found in non-skeletal tissues. Relatively high levels found in skeletal tissues.1 Publication

Gene expression databases

ArrayExpressiO70370.
BgeeiO70370.
CleanExiMM_CTSS.
GenevestigatoriO70370.

Interactioni

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi129 – 1324
Helixi147 – 16418
Helixi172 – 1787
Turni182 – 1843
Helixi188 – 1903
Helixi194 – 20411
Beta strandi207 – 2093
Turni210 – 2123
Helixi226 – 2283
Beta strandi229 – 2313
Beta strandi235 – 2384
Helixi244 – 25310
Beta strandi257 – 2615
Helixi267 – 2704
Beta strandi287 – 29711
Beta strandi300 – 3067
Beta strandi318 – 3225
Beta strandi324 – 3274
Helixi328 – 3303
Turni331 – 3333
Beta strandi336 – 3394

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M0Hmodel-A1-340[»]
4BPVX-ray2.00A/B/C/D/E/K116-340[»]
4BQVX-ray1.70A/B/C/D/E/F/G/H116-340[»]
4BS5X-ray1.25A116-340[»]
4BS6X-ray1.20A/B116-340[»]
4BSQX-ray1.96A116-340[»]
ProteinModelPortaliO70370.
SMRiO70370. Positions 26-340.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4870.
GeneTreeiENSGT00740000115447.
HOVERGENiHBG011513.
KOiK01368.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O70370-1 [UniParc]FASTAAdd to Basket

« Hide

MRAPGHAAIR WLFWMPLVCS VAMEQLQRDP TLDYHWDLWK KTHEKEYKDK    50
NEEEVRRLIW EKNLKFIMIH NLEYSMGMHT YQVGMNDMGD MTNEEILCRM 100
GALRIPRQSP KTVTFRSYSN RTLPDTVDWR EKGCVTEVKY QGSCGACWAF 150
SAVGALEGQL KLKTGKLISL SAQNLVDCSN EEKYGNKGCG GGYMTEAFQY 200
IIDNGGIEAD ASYPYKATDE KCHYNSKNRA ATCSRYIQLP FGDEDALKEA 250
VATKGPVSVG IDASHSSFFF YKSGVYDDPS CTGNVNHGVL VVGYGTLDGK 300
DYWLVKNSWG LNFGDQGYIR MARNNKNHCG IASYCSYPEI 340
Length:340
Mass (Da):38,475
Last modified:July 27, 2011 - v2
Checksum:i10550C5106318C47
GO

Sequence cautioni

The sequence CAA05360.1 differs from that shown. Reason: Frameshift at position 30.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341Y → H in CAA05360. 1 Publication
Sequence conflicti97 – 971L → S in AAB94925. 1 Publication
Sequence conflicti97 – 971L → S in AAC05781. 1 Publication
Sequence conflicti106 – 1061P → S in AAB94925. 1 Publication
Sequence conflicti106 – 1061P → S in AAC05781. 1 Publication
Sequence conflicti146 – 1461A → S in CAA77184. 1 Publication
Sequence conflicti218 – 2181T → M in AAB94925. 1 Publication
Sequence conflicti218 – 2181T → M in CAA05360. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF051732
, AF051727, AF051728, AF051729, AF051726, AF051730, AF051731 Genomic DNA. Translation: AAC05781.1.
AF038546 mRNA. Translation: AAB94925.1.
AJ002386 mRNA. Translation: CAA05360.1. Frameshift.
AC092203 Genomic DNA. No translation available.
Y18466 mRNA. Translation: CAA77184.1.
AJ223208 mRNA. Translation: CAA11182.1.
CCDSiCCDS50992.1.
RefSeqiNP_067256.4. NM_021281.3.
UniGeneiMm.3619.

Genome annotation databases

EnsembliENSMUST00000116304; ENSMUSP00000112006; ENSMUSG00000038642.
GeneIDi13040.
KEGGimmu:13040.
UCSCiuc008qjz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF051732
, AF051727 , AF051728 , AF051729 , AF051726 , AF051730 , AF051731 Genomic DNA. Translation: AAC05781.1 .
AF038546 mRNA. Translation: AAB94925.1 .
AJ002386 mRNA. Translation: CAA05360.1 . Frameshift.
AC092203 Genomic DNA. No translation available.
Y18466 mRNA. Translation: CAA77184.1 .
AJ223208 mRNA. Translation: CAA11182.1 .
CCDSi CCDS50992.1.
RefSeqi NP_067256.4. NM_021281.3.
UniGenei Mm.3619.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M0H model - A 1-340 [» ]
4BPV X-ray 2.00 A/B/C/D/E/K 116-340 [» ]
4BQV X-ray 1.70 A/B/C/D/E/F/G/H 116-340 [» ]
4BS5 X-ray 1.25 A 116-340 [» ]
4BS6 X-ray 1.20 A/B 116-340 [» ]
4BSQ X-ray 1.96 A 116-340 [» ]
ProteinModelPortali O70370.
SMRi O70370. Positions 26-340.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi O70370.
ChEMBLi CHEMBL4098.

Protein family/group databases

MEROPSi C01.034.

PTM databases

PhosphoSitei O70370.

Proteomic databases

MaxQBi O70370.
PaxDbi O70370.
PRIDEi O70370.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000116304 ; ENSMUSP00000112006 ; ENSMUSG00000038642 .
GeneIDi 13040.
KEGGi mmu:13040.
UCSCi uc008qjz.2. mouse.

Organism-specific databases

CTDi 1520.
MGIi MGI:107341. Ctss.

Phylogenomic databases

eggNOGi COG4870.
GeneTreei ENSGT00740000115447.
HOVERGENi HBG011513.
KOi K01368.

Enzyme and pathway databases

BRENDAi 3.4.22.27. 3474.
Reactomei REACT_196550. MHC class II antigen presentation.
REACT_197101. Endosomal/Vacuolar pathway.
REACT_198976. Trafficking and processing of endosomal TLR.
REACT_199052. Degradation of the extracellular matrix.
REACT_199112. Endosomal/Vacuolar pathway.

Miscellaneous databases

ChiTaRSi CTSS. mouse.
NextBioi 282932.
PROi O70370.
SOURCEi Search...

Gene expression databases

ArrayExpressi O70370.
Bgeei O70370.
CleanExi MM_CTSS.
Genevestigatori O70370.

Family and domain databases

InterProi IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view ]
PANTHERi PTHR12411. PTHR12411. 1 hit.
Pfami PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view ]
PRINTSi PR00705. PAPAIN.
SMARTi SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view ]
PROSITEi PS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 144-306, TISSUE SPECIFICITY.
    Strain: C57BL/6.
    Tissue: Cartilage.
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 296-340.
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiCATS_MOUSE
AccessioniPrimary (citable) accession number: O70370
Secondary accession number(s): E9QK18, O54973
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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