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Protein

Cathepsin E

Gene

Ctse

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain (By similarity).By similarity

Catalytic activityi

Similar to cathepsin D, but slightly broader specificity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei98 – 981PROSITE-ProRule annotation
Active sitei283 – 2831PROSITE-ProRule annotation

GO - Molecular functioni

  • aspartic-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  • antigen processing and presentation of exogenous peptide antigen via MHC class II Source: UniProtKB
  • protein autoprocessing Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.23.34. 5301.

Protein family/group databases

MEROPSiA01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin E (EC:3.4.23.34)
Gene namesi
Name:Ctse
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi2446. Ctse.

Subcellular locationi

GO - Cellular componenti

  • endosome Source: UniProtKB
  • extracellular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121By similarityAdd
BLAST
Propeptidei22 – 5837Activation peptide1 PublicationPRO_0000025980Add
BLAST
Chaini59 – 398340Cathepsin EPRO_0000025981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi62 – 62InterchainCurated
Glycosylationi92 – 921N-linked (GlcNAc...)Curated
Disulfide bondi111 ↔ 116By similarity
Disulfide bondi274 ↔ 278By similarity

Post-translational modificationi

Glycosylated. The nature of the carbohydrate chain varies between cell types. In brain microglia, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In stomach and spleen, the mature enzyme contains a high mannose-type oligosaccharide. In erythrocyte membranes, the mature enzyme contains a complex-type oligosaccharide.3 Publications

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP16228.
PRIDEiP16228.

Expressioni

Tissue specificityi

Expressed abundantly in lymphocytes and macrophages of the thymus and spleen, and in the M cells of the intestine. In the brain, expression is limited to reactive microglial cells, the large pyrimidial neurons in the cerebral cortex, the CA1 and CA3 pyrimidial neurons of the hippocampus, the large neurons of the neostriatum, and the Purkinje neurons of the cerebellum.5 Publications

Developmental stagei

Expression increases in all brain regions examined with age, and increases markedly in reactive microglial cells amd CA1 pyrimidial neurons following ischemic injury. In the thymus expression increased steadily up to 8 weeks of age before decreasing to a much lower level by 52 weeks. Expression levels in the spleen and stomach do not appear to vary with age.1 Publication

Gene expression databases

GenevisibleiP16228. RN.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000048353.

Structurei

3D structure databases

ProteinModelPortaliP16228.
SMRiP16228. Positions 70-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 394315Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP16228.
KOiK01382.
OMAiGEYAMEC.
OrthoDBiEOG7HQN88.
PhylomeDBiP16228.
TreeFamiTF314990.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR033145. Cathepsin_E.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PTHR13683:SF81. PTHR13683:SF81. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P16228-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKPLFVLLLL LLLLDLAQAQ GVLHRVPLRR HQSLRKKLRA QGQLSDFWRS
60 70 80 90 100
HNLDMIEFSE SCNVDKGINE PLINYLDMEY FGTVSIGSPS QNFTVIFDTG
110 120 130 140 150
SSNLWVPSVY CTSPACKAHP VFHPSQSSTY MEVGNHFSIQ YGTGSLTGII
160 170 180 190 200
GADQVSVEGL TVEGQQFGES VKEPGQTFVN AEFDGILGLG YPSLAVGGVT
210 220 230 240 250
PVFDNMMAQN LVALPMFSVY LSSDPQGGSG SELTFGGYDP SHFSGSLNWI
260 270 280 290 300
PVTKQGYWQI ALDGIQVGDT VMFCSEGCQA IVDTGTSLIT GPPKKIKQLQ
310 320 330 340 350
EAIGATPMDG EYAVDCATLN MMPNVTFLIN GVSYTLSPTA YILPDLVDGM
360 370 380 390
QFCGSGFQGL DIQPPAGPLW ILGDVFIRKF YSVFDRGNNQ VGLAPAVP
Length:398
Mass (Da):43,021
Last modified:July 15, 1998 - v3
Checksum:i25F123E67C46EB5F
GO
Isoform 2 (identifier: P16228-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     312-344: Missing.

Show »
Length:365
Mass (Da):39,445
Checksum:i7AED1AB6B6A447D7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551M → V in AAH62002 (PubMed:15489334).Curated
Sequence conflicti79 – 791E → N AA sequence (PubMed:2105725).Curated
Sequence conflicti83 – 842TV → SR AA sequence (PubMed:2105725).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti114 – 1141P → S.1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei312 – 34433Missing in isoform 2. 1 PublicationVSP_005224Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38104 mRNA. Translation: BAA07285.1.
D45187 mRNA. Translation: BAA08128.1.
BC062002 mRNA. Translation: AAH62002.1.
PIRiA34657.
S66465.
S66466.
RefSeqiNP_037070.1. NM_012938.1.
XP_006249810.1. XM_006249748.2. [P16228-1]
XP_006249811.1. XM_006249749.2. [P16228-1]
UniGeneiRn.92738.

Genome annotation databases

EnsembliENSRNOT00000009241; ENSRNOP00000009242; ENSRNOG00000006963. [P16228-2]
ENSRNOT00000048391; ENSRNOP00000048353; ENSRNOG00000006963. [P16228-1]
GeneIDi25424.
KEGGirno:25424.
UCSCiRGD:2446. rat. [P16228-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38104 mRNA. Translation: BAA07285.1.
D45187 mRNA. Translation: BAA08128.1.
BC062002 mRNA. Translation: AAH62002.1.
PIRiA34657.
S66465.
S66466.
RefSeqiNP_037070.1. NM_012938.1.
XP_006249810.1. XM_006249748.2. [P16228-1]
XP_006249811.1. XM_006249749.2. [P16228-1]
UniGeneiRn.92738.

3D structure databases

ProteinModelPortaliP16228.
SMRiP16228. Positions 70-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000048353.

Protein family/group databases

MEROPSiA01.010.

Proteomic databases

PaxDbiP16228.
PRIDEiP16228.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009241; ENSRNOP00000009242; ENSRNOG00000006963. [P16228-2]
ENSRNOT00000048391; ENSRNOP00000048353; ENSRNOG00000006963. [P16228-1]
GeneIDi25424.
KEGGirno:25424.
UCSCiRGD:2446. rat. [P16228-1]

Organism-specific databases

CTDi1510.
RGDi2446. Ctse.

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP16228.
KOiK01382.
OMAiGEYAMEC.
OrthoDBiEOG7HQN88.
PhylomeDBiP16228.
TreeFamiTF314990.

Enzyme and pathway databases

BRENDAi3.4.23.34. 5301.

Miscellaneous databases

PROiP16228.

Gene expression databases

GenevisibleiP16228. RN.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR033145. Cathepsin_E.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PTHR13683:SF81. PTHR13683:SF81. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequencing of two cDNA clones encoding rat spleen cathepsin E and analysis of the activation of purified procathepsin E."
    Okamoto K., Yu H., Misumi Y., Ikehara Y., Yamamoto K.
    Arch. Biochem. Biophys. 322:103-111(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT SER-114.
    Tissue: Spleen.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Prostate.
  3. "Structural studies of rat cathepsin E: amino-terminal structure and carbohydrate units of mature enzyme."
    Yonezawa S., Takahashi T., Ichinose M., Miki K., Tanaka J., Gasa S.
    Biochem. Biophys. Res. Commun. 166:1032-1038(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 59-110, GLYCOSYLATION.
  4. "Isolation and biochemical characterization of procathepsin E from human erythrocyte membranes."
    Takeda-Ezaki M., Yamamoto K.
    Arch. Biochem. Biophys. 304:352-358(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  5. "Transient forebrain ischemia induces increased expression and specific localization of cathepsins E and D in rat hippocampus and neostriatum."
    Nakanishi H., Tsukuba T., Kondou T., Tanaka T., Yamamoto K.
    Exp. Neurol. 121:215-223(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Cathepsin E in follicle associated epithelium of intestine and tonsils: localization to M cells and possible role in antigen processing."
    Finzi G., Cornaggia M., Capella C., Fiocca R., Bosi F., Solcia E., Samloff I.M.
    Histochemistry 99:201-211(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "Age-related changes in activities and localizations of cathepsins D, E, B, and L in the rat brain tissues."
    Nakanishi H., Tominaga K., Amano T., Hirotsu I., Inoue T., Yamamoto K.
    Exp. Neurol. 126:119-128(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. "Age-related and dexamethasone-induced changes in cathepsins E and D in rat thymic and splenic cells."
    Nishishita K., Sakai H., Sakai E., Kato Y., Yamamoto K.
    Arch. Biochem. Biophys. 333:349-358(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEXAMETHASONE ADMINISTRATION.
  9. "Identification of cellular compartments involved in processing of cathepsin E in primary cultures of rat microglia."
    Sastradipura D.F., Nakanishi H., Tsukuba T., Nishishita K., Sakai H., Kato Y., Gotow T., Uchiyama Y., Yamamoto K.
    J. Neurochem. 70:2045-2056(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.

Entry informationi

Entry nameiCATE_RAT
AccessioniPrimary (citable) accession number: P16228
Secondary accession number(s): Q63701
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 15, 1998
Last modified: June 8, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Administration of dexamethasone results in the conversion of the proenzyme to the mature form in thymocytes.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.