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P70269

- CATE_MOUSE

UniProt

P70269 - CATE_MOUSE

Protein

Cathepsin E

Gene

Ctse

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiP70269.
    BgeeiP70269.
    CleanExiMM_CTSE.
    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.
    GeneTreeiENSGT00710000106265.
    HOGENOMiHOG000197681.
    HOVERGENiHBG000482.
    InParanoidiQ3UKT5.
    KOiK01382.
    OMAiTVMFCSE.
    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

    MKPLLVLLLL LLLDLAQAQG ALHRVPLRRH QSLRKKLRAQ GQLSEFWRSH    50
    NLDMTRLSES CNVYSSVNEP LINYLDMEYF GTISIGTPPQ NFTVIFDTGS 100
    SNLWVPSVYC TSPACKAHPV FHPSQSDTYT EVGNHFSIQY GTGSLTGIIG 150
    ADQVSVEGLT VDGQQFGESV KEPGQTFVNA EFDGILGLGY PSLAAGGVTP 200
    VFDNMMAQNL VALPMFSVYL SSDPQGGSGS ELTFGGYDPS HFSGSLNWIP 250
    VTKQAYWQIA LDGIQVGDTV MFCSEGCQAI VDTGTSLITG PPDKIKQLQE 300
    AIGATPIDGE YAVDCATLDT MPNVTFLINE VSYTLNPTDY ILPDLVEGMQ 350
    FCGSGFQGLD IPPPAGPLWI LGDVFIRQFY SVFDRGNNQV GLAPAVP 397
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS15271.1.
    RefSeqi NP_031825.2. NM_007799.3.
    UniGenei Mm.230249.

    3D structure databases

    ProteinModelPortali P70269.
    SMRi P70269. Positions 22-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000112235.

    Chemistry

    ChEMBLi CHEMBL1681627.

    Protein family/group databases

    MEROPSi A01.010.

    PTM databases

    PhosphoSitei P70269.

    Proteomic databases

    PaxDbi P70269.
    PRIDEi P70269.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000073350 ; ENSMUSP00000073072 ; ENSMUSG00000004552 .
    GeneIDi 13034.
    KEGGi mmu:13034.
    UCSCi uc007cnn.2. mouse.

    Organism-specific databases

    CTDi 1510.
    MGIi MGI:107361. Ctse.

    Phylogenomic databases

    eggNOGi NOG248684.
    GeneTreei ENSGT00710000106265.
    HOGENOMi HOG000197681.
    HOVERGENi HBG000482.
    InParanoidi Q3UKT5.
    KOi K01382.
    OMAi TVMFCSE.
    OrthoDBi EOG7HQN88.
    TreeFami TF314990.

    Miscellaneous databases

    NextBioi 282912.
    PMAP-CutDB P70269.
    PROi P70269.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P70269.
    Bgeei P70269.
    CleanExi MM_CTSE.
    Genevestigatori P70269.

    Family and domain databases

    Gene3Di 2.40.70.10. 2 hits.
    InterProi IPR001461. Aspartic_peptidase.
    IPR001969. Aspartic_peptidase_AS.
    IPR012848. Aspartic_peptidase_N.
    IPR021109. Peptidase_aspartic_dom.
    [Graphical view ]
    PANTHERi PTHR13683. PTHR13683. 1 hit.
    Pfami PF07966. A1_Propeptide. 1 hit.
    PF00026. Asp. 1 hit.
    [Graphical view ]
    PRINTSi PR00792. PEPSIN.
    SUPFAMi SSF50630. SSF50630. 1 hit.
    PROSITEi PS00141. ASP_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 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

    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