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P08884

- GRAE_MOUSE

UniProt

P08884 - GRAE_MOUSE

Protein

Granzyme E

Gene

Gzme

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    Functioni

    This enzyme is probably necessary for target cell lysis in cell-mediated immune responses.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei65 – 651Charge relay systemBy similarity
    Active sitei109 – 1091Charge relay systemBy similarity
    Active sitei204 – 2041Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: RefGenome

    GO - Biological processi

    1. cytolysis Source: UniProtKB-KW
    2. proteolysis Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Cytolysis

    Enzyme and pathway databases

    ReactomeiREACT_208000. Activation, myristolyation of BID and translocation to mitochondria.

    Protein family/group databases

    MEROPSiS01.399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Granzyme E (EC:3.4.21.-)
    Alternative name(s):
    CTL serine protease 2
    Cytotoxic cell protease 3
    Short name:
    CCP3
    Cytotoxic serine protease 2
    D12
    MCSP2
    Gene namesi
    Name:Gzme
    Synonyms:Ccp3, Ctla-6, Ctla6
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:109265. Gzme.

    Subcellular locationi

    Cytoplasmic granule
    Note: Cytoplasmic granules of cytolytic T-lymphocytes.

    GO - Cellular componenti

    1. secretory granule Source: RefGenome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Add
    BLAST
    Propeptidei19 – 2021 PublicationPRO_0000027407
    Chaini21 – 248228Granzyme EPRO_0000027408Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi50 ↔ 66PROSITE-ProRule annotation
    Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi143 ↔ 210PROSITE-ProRule annotation
    Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi175 ↔ 189PROSITE-ProRule annotation
    Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP08884.
    PRIDEiP08884.

    Expressioni

    Gene expression databases

    BgeeiP08884.
    CleanExiMM_GZME.
    GenevestigatoriP08884.

    Interactioni

    Protein-protein interaction databases

    IntActiP08884. 1 interaction.
    MINTiMINT-4096698.
    STRINGi10090.ENSMUSP00000015588.

    Structurei

    3D structure databases

    ProteinModelPortaliP08884.
    SMRiP08884. Positions 21-248.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 246226Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family. Granzyme subfamily.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00740000115234.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    KOiK01362.
    OMAiNSECFIL.
    OrthoDBiEOG7RRF7Z.
    PhylomeDBiP08884.
    TreeFamiTF333630.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P08884-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPVLILLTL LLPLGAGAEE IIGGHVVKPH SRPYMAFVKS VDIEGNRRYC    50
    GGFLVQDDFV LTAAHCRNRT MTVTLGAHNI KAKEETQQII PVAKAIPHPD 100
    YNATAFFSDI MLLKLESKAK RTKAVRPLKL PRPNARVKPG DVCSVAGWGS 150
    RSINDTKASA RLREAQLVIQ EDEECKKRFR HYTETTEICA GDLKKIKTPF 200
    KGDSGGPLVC DNKAYGLLAY AKNRTISSGV FTKIVHFLPW ISRNMKLL 248
    Length:248
    Mass (Da):27,494
    Last modified:November 1, 1988 - v1
    Checksum:i3A31912A45E93D3F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51L → P in AAB19192. (PubMed:8917549)Curated
    Sequence conflicti132 – 1321R → K in AAA37487. (PubMed:3053963)Curated
    Sequence conflicti132 – 1321R → K in CAA32255. (PubMed:3053963)Curated
    Sequence conflicti150 – 1501S → P(PubMed:8917549)Curated
    Sequence conflicti150 – 1501S → P(PubMed:3260382)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36901 mRNA. Translation: AAA37487.1.
    X12821 mRNA. Translation: CAA31308.1.
    U66474 Genomic DNA. Translation: AAB19192.1.
    X56988 Genomic DNA. Translation: CAA40306.1.
    J03256 mRNA. Translation: AAA37737.1.
    X14093 mRNA. Translation: CAA32255.1.
    CCDSiCCDS27143.1.
    PIRiS01006.
    RefSeqiNP_034503.2. NM_010373.3.
    UniGeneiMm.14424.

    Genome annotation databases

    EnsembliENSMUST00000089549; ENSMUSP00000086978; ENSMUSG00000022156.
    GeneIDi14942.
    KEGGimmu:14942.
    UCSCiuc007ubo.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36901 mRNA. Translation: AAA37487.1 .
    X12821 mRNA. Translation: CAA31308.1 .
    U66474 Genomic DNA. Translation: AAB19192.1 .
    X56988 Genomic DNA. Translation: CAA40306.1 .
    J03256 mRNA. Translation: AAA37737.1 .
    X14093 mRNA. Translation: CAA32255.1 .
    CCDSi CCDS27143.1.
    PIRi S01006.
    RefSeqi NP_034503.2. NM_010373.3.
    UniGenei Mm.14424.

    3D structure databases

    ProteinModelPortali P08884.
    SMRi P08884. Positions 21-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08884. 1 interaction.
    MINTi MINT-4096698.
    STRINGi 10090.ENSMUSP00000015588.

    Protein family/group databases

    MEROPSi S01.399.

    Proteomic databases

    PaxDbi P08884.
    PRIDEi P08884.

    Protocols and materials databases

    DNASUi 14942.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000089549 ; ENSMUSP00000086978 ; ENSMUSG00000022156 .
    GeneIDi 14942.
    KEGGi mmu:14942.
    UCSCi uc007ubo.1. mouse.

    Organism-specific databases

    CTDi 14942.
    MGIi MGI:109265. Gzme.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00740000115234.
    HOGENOMi HOG000251820.
    HOVERGENi HBG013304.
    KOi K01362.
    OMAi NSECFIL.
    OrthoDBi EOG7RRF7Z.
    PhylomeDBi P08884.
    TreeFami TF333630.

    Enzyme and pathway databases

    Reactomei REACT_208000. Activation, myristolyation of BID and translocation to mitochondria.

    Miscellaneous databases

    NextBioi 287275.
    PROi P08884.
    SOURCEi Search...

    Gene expression databases

    Bgeei P08884.
    CleanExi MM_GZME.
    Genevestigatori P08884.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of two cDNA sequences which encode cytotoxic cell proteases."
      Bleackley R.C., Duggan B., Ehrman N., Lobe C.G.
      FEBS Lett. 234:153-159(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Prendergast J.A., Pinkoski M., Wolfenden A., Bleackley R.C.
      Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    3. "Long-range disruption of gene expression by a selectable marker cassette."
      Pham C.T.N., MacIvor D.M., Hug B.A., Heusel J.W., Ley T.J.
      Proc. Natl. Acad. Sci. U.S.A. 93:13090-13095(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    4. "Identification and sequencing of cDNA clones encoding the granule-associated serine proteases granzymes D, E, and F of cytolytic T lymphocytes."
      Jenne D.E., Rey C., Haefliger J.-A., Qiao B.-Y., Groscurth P., Tschopp J.
      Proc. Natl. Acad. Sci. U.S.A. 85:4814-4818(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-248.
    5. "Isolation and sequence analysis of serine protease cDNAs from mouse cytolytic T lymphocytes."
      Kwon B.S., Kestler D., Lee E., Wakulchik M., Young J.D.-E.
      J. Exp. Med. 168:1839-1854(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-248.
      Tissue: Cytotoxic T-cell.
    6. "A family of serine esterases in lytic granules of cytolytic T lymphocytes."
      Masson D., Tschopp J.
      Cell 49:679-685(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-40.

    Entry informationi

    Entry nameiGRAE_MOUSE
    AccessioniPrimary (citable) accession number: P08884
    Secondary accession number(s): P97389
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 122 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, Direct protein sequencing, 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