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Protein

Cathepsin E

Gene

Ctse

Organism
Mus musculus (Mouse)
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.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei97 – 971PROSITE-ProRule annotation
Active sitei282 – 2821PROSITE-ProRule annotation

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB
  2. protein homodimerization activity Source: MGI

GO - Biological processi

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

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Cathepsin E (EC:3.4.23.34)
Gene namesi
Name:Ctse
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:107361. Ctse.

Subcellular locationi

Endosome 1 Publication
Note: The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome.

GO - Cellular componenti

  1. endosome Source: UniProtKB
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020By similarityAdd
BLAST
Propeptidei21 – 5939Activation peptideBy similarityPRO_0000025976Add
BLAST
Chaini60 – 397338Cathepsin EPRO_0000025977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi61 – 61InterchainCurated
Glycosylationi91 – 911N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi110 ↔ 115By similarity
Disulfide bondi273 ↔ 277By similarity
Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated. The nature of the carbohydrate chain varies between cell types. In fibroblasts, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide.1 Publication

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP70269.
PRIDEiP70269.

PTM databases

PhosphoSiteiP70269.

Miscellaneous databases

PMAP-CutDBP70269.

Expressioni

Tissue specificityi

Expressed abundantly in the stomach, Clara cells and alveolar macrophages of the lung, brain microglia, spleen and activated B-lymphocytes. Not expressed in resting B-lymphocytes.2 Publications

Gene expression databases

BgeeiP70269.
CleanExiMM_CTSE.
ExpressionAtlasiP70269. baseline and differential.
GenevestigatoriP70269.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000112235.

Structurei

3D structure databases

ProteinModelPortaliP70269.
SMRiP70269. Positions 22-396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG248684.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP70269.
KOiK01382.
OMAiWVPVTQQ.
OrthoDBiEOG7HQN88.
TreeFamiTF314990.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P70269-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKPLLVLLLL LLLDLAQAQG ALHRVPLRRH QSLRKKLRAQ GQLSEFWRSH
60 70 80 90 100
NLDMTRLSES CNVYSSVNEP LINYLDMEYF GTISIGTPPQ NFTVIFDTGS
110 120 130 140 150
SNLWVPSVYC TSPACKAHPV FHPSQSDTYT EVGNHFSIQY GTGSLTGIIG
160 170 180 190 200
ADQVSVEGLT VDGQQFGESV KEPGQTFVNA EFDGILGLGY PSLAAGGVTP
210 220 230 240 250
VFDNMMAQNL VALPMFSVYL SSDPQGGSGS ELTFGGYDPS HFSGSLNWIP
260 270 280 290 300
VTKQAYWQIA LDGIQVGDTV MFCSEGCQAI VDTGTSLITG PPDKIKQLQE
310 320 330 340 350
AIGATPIDGE YAVDCATLDT MPNVTFLINE VSYTLNPTDY ILPDLVEGMQ
360 370 380 390
FCGSGFQGLD IPPPAGPLWI LGDVFIRQFY SVFDRGNNQV GLAPAVP
Length:397
Mass (Da):42,938
Last modified:July 27, 2011 - v2
Checksum:iDF6AEFD5F78B3747
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti297 – 2971Q → H in CAA66056. (PubMed:9180269)Curated
Sequence conflicti297 – 2971Q → H in CAJ18460. 1 PublicationCurated
Sequence conflicti297 – 2971Q → H in AAH05432. (PubMed:15489334)Curated
Sequence conflicti347 – 3471E → D in CAA66056. (PubMed:9180269)Curated
Sequence conflicti347 – 3471E → D in CAA71859. (PubMed:9602058)Curated
Sequence conflicti347 – 3471E → D in CAJ18460. 1 PublicationCurated
Sequence conflicti347 – 3471E → D in AAH05432. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97399 mRNA. Translation: CAA66056.1.
Y10928 Genomic DNA. Translation: CAA71859.1.
AJ009840
, AJ009841, AJ009842, AJ009843, AJ009844, AJ009845, AJ009846, AJ009847, AJ009848 Genomic DNA. Translation: CAA08880.2.
AK143581 mRNA. Translation: BAE25449.1.
AK145875 mRNA. Translation: BAE26716.1.
AK157907 mRNA. Translation: BAE34257.1.
AK165271 mRNA. Translation: BAE38113.1.
CT010252 mRNA. Translation: CAJ18460.1.
CH466520 Genomic DNA. Translation: EDL39705.1.
BC005432 mRNA. Translation: AAH05432.1.
CCDSiCCDS15271.1.
RefSeqiNP_031825.2. NM_007799.3.
UniGeneiMm.230249.

Genome annotation databases

EnsembliENSMUST00000073350; ENSMUSP00000073072; ENSMUSG00000004552.
GeneIDi13034.
KEGGimmu:13034.
UCSCiuc007cnn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97399 mRNA. Translation: CAA66056.1.
Y10928 Genomic DNA. Translation: CAA71859.1.
AJ009840
, AJ009841, AJ009842, AJ009843, AJ009844, AJ009845, AJ009846, AJ009847, AJ009848 Genomic DNA. Translation: CAA08880.2.
AK143581 mRNA. Translation: BAE25449.1.
AK145875 mRNA. Translation: BAE26716.1.
AK157907 mRNA. Translation: BAE34257.1.
AK165271 mRNA. Translation: BAE38113.1.
CT010252 mRNA. Translation: CAJ18460.1.
CH466520 Genomic DNA. Translation: EDL39705.1.
BC005432 mRNA. Translation: AAH05432.1.
CCDSiCCDS15271.1.
RefSeqiNP_031825.2. NM_007799.3.
UniGeneiMm.230249.

3D structure databases

ProteinModelPortaliP70269.
SMRiP70269. Positions 22-396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000112235.

Chemistry

ChEMBLiCHEMBL1681627.

Protein family/group databases

MEROPSiA01.010.

PTM databases

PhosphoSiteiP70269.

Proteomic databases

PaxDbiP70269.
PRIDEiP70269.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000073350; ENSMUSP00000073072; ENSMUSG00000004552.
GeneIDi13034.
KEGGimmu:13034.
UCSCiuc007cnn.2. mouse.

Organism-specific databases

CTDi1510.
MGIiMGI:107361. Ctse.

Phylogenomic databases

eggNOGiNOG248684.
GeneTreeiENSGT00760000118929.
HOGENOMiHOG000197681.
HOVERGENiHBG000482.
InParanoidiP70269.
KOiK01382.
OMAiWVPVTQQ.
OrthoDBiEOG7HQN88.
TreeFamiTF314990.

Miscellaneous databases

NextBioi282912.
PMAP-CutDBP70269.
PROiP70269.
SOURCEiSearch...

Gene expression databases

BgeeiP70269.
CleanExiMM_CTSE.
ExpressionAtlasiP70269. baseline and differential.
GenevestigatoriP70269.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression and characterisation of murine procathepsin E."
    Tatnell P.J., Lees W.E., Kay J.
    FEBS Lett. 408:62-66(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY.
    Strain: BALB/c.
    Tissue: Spleen.
  2. "Mouse procathepsin E gene: molecular organisation and chromosomal localisation."
    Tatnell P.J., Roth W., Deussing J., Peters C., Kay J.
    Biochim. Biophys. Acta 1398:57-66(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/SvJ.
  3. "Cathepsin E gene in mouse."
    Yonezawa S., Masaki S., Hanai A., Ono T., Sonta S., Hirai H., Ichinose M., Miki K., Takahashi K., Kageyama T.
    Biomed. Res. 19:327-334(1998)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Strain: 129/SvJ.
    Tissue: Gastric mucosa.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Inner ear, Liver and Spleen.
  5. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  8. "Antigen processing for presentation by class II major histocompatibility complex requires cleavage by cathepsin E."
    Bennett K., Levine T., Ellis J.S., Peanasky R.J., Samloff I.M., Kay J., Chain B.M.
    Eur. J. Immunol. 22:1519-1524(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Subcellular localization and targeting of cathepsin E."
    Finley E.M., Kornfeld S.
    J. Biol. Chem. 269:31259-31266(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  10. "Regulation of human and mouse procathepsin E gene expression."
    Cook M., Caswell R.C., Richards R.J., Kay J., Tatnell P.J.
    Eur. J. Biochem. 268:2658-2668(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. Cited for: FUNCTION.

Entry informationi

Entry nameiCATE_MOUSE
AccessioniPrimary (citable) accession number: P70269
Secondary accession number(s): O35647, Q3UKT5, Q4FK00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 124 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.