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Q800A0

- CATE_LITCT

UniProt

Q800A0 - CATE_LITCT

Protein

Cathepsin E

Gene

CTSE

Organism
Lithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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 By similarity.By similarity

    Catalytic activityi

    Similar to cathepsin D, but slightly broader specificity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei92 – 921By similarityPROSITE-ProRule annotation
    Active sitei277 – 2771By similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: UniProtKB

    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
    Synonyms:CE
    OrganismiLithobates catesbeiana (American bullfrog) (Rana catesbeiana)Imported
    Taxonomic identifieri8400 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

    Subcellular locationi

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

    GO - Cellular componenti

    1. endosome Source: UniProtKB

    Keywords - Cellular componenti

    Endosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 16161 PublicationAdd
    BLAST
    Propeptidei17 – 4933Activation peptide1 PublicationPRO_0000025982Add
    BLAST
    Chaini50 – 397348Cathepsin E1 PublicationPRO_0000025983Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi105 ↔ 110By similarity
    Glycosylationi139 – 1391N-linked (GlcNAc...)Curated
    Disulfide bondi268 ↔ 272By similarity
    Disulfide bondi310 ↔ 344By similarity

    Post-translational modificationi

    Glycosylated. Contains high mannose-type oligosaccharide.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Expressioni

    Tissue specificityi

    Found in the larval foregut and adult stomach.1 Publication

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ800A0.
    SMRiQ800A0. Positions 64-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG000482.

    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.

    Q800A0-1 [UniParc]FASTAAdd to Basket

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    MKQFLVVLLI LSFVHGIIRV PLKRQKSMRK ILKEKGKLSH LWTKQGNEFL    50
    QLSDSCSSPE TASEPLMNYL DVEYFGQISI GTPPQQFTVI FDTGSSNLWV 100
    PSIYCTSQAC TKHNRYRPSE STTYVSNGEA FFIQYGTGNL TGILGIDQVT 150
    VQGITVQSQT FAESVSEPGS TFQDSNFDGI LGLAYPNLAV DNCIPVFDNM 200
    IAQNLVELPL FGVYMNRDPN SADGGELVLG GFDTSRFSGQ LNWVPITVQG 250
    YWQIQVDSIQ VAGQVIFCSD GCQAIVDTGT SLITGPSGDI EQLQNYIGVT 300
    NTNGEYGVSC STLSLMPSVT FTINGLDYSL TPEQYMLEDG GGYCSSGFQG 350
    LDISPPSGPL WILGDVFIGQ YYSVFDRGNN RVGFAPVVFY ETTTNGA 397
    Length:397
    Mass (Da):43,307
    Last modified:June 1, 2003 - v1
    Checksum:i4F2D59D7F50F06B4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB093036 mRNA. Translation: BAC75398.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB093036 mRNA. Translation: BAC75398.1 .

    3D structure databases

    ProteinModelPortali Q800A0.
    SMRi Q800A0. Positions 64-388.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi A01.010.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG000482.

    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. "Molecular cloning of preprocathepsin E cDNA from the stomach of bullfrog Rana catesbeiana."
      Inokuchi T., Ikuzawa M., Mineta T., Yasumasu S., Kobayashi K.
      Comp. Biochem. Physiol. 135B:647-655(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-42 AND 50-69, TISSUE SPECIFICITY, GLYCOSYLATION.
      Tissue: StomachImported.

    Entry informationi

    Entry nameiCATE_LITCT
    AccessioniPrimary (citable) accession number: Q800A0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 56 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

    Direct protein sequencing

    Documents

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

    External Data

    Dasty 3