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Q02765 (CATS_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cathepsin S

EC=3.4.22.27
Gene names
Name:Ctss
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length330 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 By similarity. May be involved in thyroid hormone biosynthesis.

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.

Tissue specificity

Highest levels occur in the ileum followed by spleen, brain, thyroid, ovary and uterus. Low levels are found in the liver, kidney, jejunum and lung with lowest levels in the heart.

Induction

By thyroid-stimulating hormone.

Sequence similarities

Belongs to the peptidase C1 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 11295Activation peptide
PRO_0000026317
Chain113 – 330218Cathepsin S
PRO_0000026318

Sites

Active site1371 By similarity
Active site2771 By similarity
Active site2971 By similarity

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1101N-linked (GlcNAc...) Potential
Disulfide bond124 ↔ 222 By similarity
Disulfide bond134 ↔ 179 By similarity
Disulfide bond168 ↔ 211 By similarity
Disulfide bond271 ↔ 319 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02765 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 670E3F08D7749EFE

FASTA33036,833
        10         20         30         40         50         60 
MAVLGAPGVL CDNGATAERP TLDHHWDLWK KTRMRRNTDQ NEEDVRRLIW EKNLKFIMLH 

        70         80         90        100        110        120 
NLEHSMGMHS YSVGMNHMGD MTPEEVIGYM GSLRIPRPWN RSGTLKSSSN QTLPDSVDWR 

       130        140        150        160        170        180 
EKGCVTNVKY QGSCGSCWAF SAEGALEGQL KLKTGKLVSL SAQNLVDCST EEKYGNKGCG 

       190        200        210        220        230        240 
GGFMTEAFQY IIDTSIDSEA SYPYKAMDEK CLYDPKNRAA TCSRYIELPF GDEEALKEAV 

       250        260        270        280        290        300 
ATKGPVSVGI DDASHSSFFL YQSGVYDDPS CTENMNHGVL VVGYGTLDGK DYWLVKNSWG 

       310        320        330 
LHFGDQGYIR MARNNKNHCG IASYCSYPEI 

« Hide

References

[1]"Sequence analysis, tissue distribution, and expression of rat cathepsin S."
Petanceska S., Devi L.
J. Biol. Chem. 267:26038-26043(1992) [PubMed: 1281481] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L03201 mRNA. Translation: AAA40994.1.
IPIIPI00210228.
PIRA45087.
RefSeqNP_059016.1. NM_017320.1.
UniGeneRn.11347.

3D structure databases

ProteinModelPortalQ02765.
ModBaseSearch...

Protein family/group databases

MEROPSC01.034.

Proteomic databases

PRIDEQ02765.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID50654.
KEGGrno:50654.

Organism-specific databases

CTD1520.
RGD621513. Ctss.

Phylogenomic databases

eggNOGmaNOG06336.
HOVERGENHBG011513.

Enzyme and pathway databases

BRENDA3.4.22.27. 5301.

Gene expression databases

GenevestigatorQ02765.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
KOK01368.
PANTHERPTHR12411. Peptidase_C1A. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. 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

NextBio610462.

Entry information

Entry nameCATS_RAT
AccessionPrimary (citable) accession number: Q02765
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 16, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families