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Protein

Cathepsin S

Gene

Ctss

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity). May be involved in thyroid hormone biosynthesis.By similarity

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 sitei137 – 1371By similarity
Active sitei277 – 2771By similarity
Active sitei297 – 2971By similarity

GO - Molecular functioni

  • cysteine-type peptidase activity Source: RGD

GO - Biological processi

  • bone resorption Source: RGD
  • metanephros development Source: UniProtKB
  • regulation of sensory perception of pain Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BRENDAi3.4.22.27. 5301.

Protein family/group databases

MEROPSiI29.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin S (EC:3.4.22.27)
Gene namesi
Name:Ctss
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621513. Ctss.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: RGD
  • extracellular region Source: Reactome
  • lysosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075217.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Propeptidei18 – 11295Activation peptidePRO_0000026317Add
BLAST
Chaini113 – 330218Cathepsin SPRO_0000026318Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence analysis
Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi124 ↔ 222By similarity
Disulfide bondi134 ↔ 179By similarity
Disulfide bondi168 ↔ 211By similarity
Disulfide bondi271 ↔ 319By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiQ02765.

PTM databases

PhosphoSiteiQ02765.

Expressioni

Tissue specificityi

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.

Inductioni

By thyroid-stimulating hormone.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliQ02765.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG011513.
InParanoidiQ02765.
KOiK01368.
PhylomeDBiQ02765.

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.

Q02765-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVLGAPGVL CDNGATAERP TLDHHWDLWK KTRMRRNTDQ NEEDVRRLIW
60 70 80 90 100
EKNLKFIMLH NLEHSMGMHS YSVGMNHMGD MTPEEVIGYM GSLRIPRPWN
110 120 130 140 150
RSGTLKSSSN QTLPDSVDWR EKGCVTNVKY QGSCGSCWAF SAEGALEGQL
160 170 180 190 200
KLKTGKLVSL SAQNLVDCST EEKYGNKGCG GGFMTEAFQY IIDTSIDSEA
210 220 230 240 250
SYPYKAMDEK CLYDPKNRAA TCSRYIELPF GDEEALKEAV ATKGPVSVGI
260 270 280 290 300
DDASHSSFFL YQSGVYDDPS CTENMNHGVL VVGYGTLDGK DYWLVKNSWG
310 320 330
LHFGDQGYIR MARNNKNHCG IASYCSYPEI
Length:330
Mass (Da):36,833
Last modified:July 1, 1993 - v1
Checksum:i670E3F08D7749EFE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03201 mRNA. Translation: AAA40994.1.
PIRiA45087.
RefSeqiNP_059016.1. NM_017320.1.
UniGeneiRn.11347.

Genome annotation databases

GeneIDi50654.
KEGGirno:50654.
UCSCiRGD:621513. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L03201 mRNA. Translation: AAA40994.1.
PIRiA45087.
RefSeqiNP_059016.1. NM_017320.1.
UniGeneiRn.11347.

3D structure databases

ProteinModelPortaliQ02765.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL1075217.

Protein family/group databases

MEROPSiI29.004.

PTM databases

PhosphoSiteiQ02765.

Proteomic databases

PRIDEiQ02765.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi50654.
KEGGirno:50654.
UCSCiRGD:621513. rat.

Organism-specific databases

CTDi1520.
RGDi621513. Ctss.

Phylogenomic databases

HOVERGENiHBG011513.
InParanoidiQ02765.
KOiK01368.
PhylomeDBiQ02765.

Enzyme and pathway databases

BRENDAi3.4.22.27. 5301.

Miscellaneous databases

NextBioi610462.
PROiQ02765.

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]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiCATS_RAT
AccessioniPrimary (citable) accession number: Q02765
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 11, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.