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P42280

- TRYZ_DROME

UniProt

P42280 - TRYZ_DROME

Protein

Trypsin zeta

Gene

zetaTry

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (16 Aug 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei87 – 871Charge relay systemBy similarity
    Active sitei134 – 1341Charge relay systemBy similarity
    Sitei228 – 2281Required for specificityBy similarity
    Active sitei234 – 2341Charge relay systemBy similarity

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: FlyBase

    GO - Biological processi

    1. proteolysis Source: FlyBase

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Protein family/group databases

    MEROPSiS01.116.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trypsin zeta (EC:3.4.21.4)
    Gene namesi
    Name:zetaTry
    ORF Names:CG12387
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0011556. zetaTry.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222CuratedAdd
    BLAST
    Propeptidei23 – 3816Activation peptidePRO_0000028287Add
    BLAST
    Chaini39 – 280242Trypsin zetaPRO_0000028288Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi72 ↔ 88PROSITE-ProRule annotation
    Disulfide bondi198 ↔ 218PROSITE-ProRule annotation
    Disulfide bondi230 ↔ 254PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiP42280.

    Expressioni

    Gene expression databases

    BgeeiP42280.

    Interactioni

    Protein-protein interaction databases

    BioGridi62009. 2 interactions.
    IntActiP42280. 2 interactions.
    MINTiMINT-297272.
    STRINGi7227.FBpp0087260.

    Structurei

    3D structure databases

    ProteinModelPortaliP42280.
    SMRiP42280. Positions 39-274.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 278240Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00620000088101.
    InParanoidiP42280.
    KOiK01312.
    OrthoDBiEOG75B84T.
    PhylomeDBiP42280.

    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.

    P42280-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSWIVGLL AFLVSLVALT QGLPLLEDLD EKSVPDGRIV GGYATDIAQV    50
    PYQISLRYKG ITTPENPFRH RCGGSIFNET TIVTAAHCVI GTVASQYKVV 100
    AGTNFQTGSD GVITNVKEIV MHEGYYSGAA YNNDIAILFV DPPLPLNNFT 150
    IKAIKLALEQ PIEGTVSKVS GWGTTSPGGY SSNQLLAVDV PIVSNELCDQ 200
    DYEDFGDETY RITSAMLCAG KRGVGGADAC QGDSGGPLAV RDELYGVVSW 250
    GNSCALPNYP GVYANVAYLR PWIDAVLAGL 280
    Length:280
    Mass (Da):29,738
    Last modified:August 16, 2005 - v2
    Checksum:i99A2D76557C308FC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti86 – 861A → G in AAA17456. (PubMed:10486967)Curated
    Sequence conflicti145 – 1451P → A in AAA17456. (PubMed:10486967)Curated
    Sequence conflicti153 – 1531A → G in AAA17456. (PubMed:10486967)Curated
    Sequence conflicti158 – 1581L → S in AAA17456. (PubMed:10486967)Curated
    Sequence conflicti222 – 2221R → P in AAA17456. (PubMed:10486967)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04853 Genomic DNA. Translation: AAA17456.1.
    AE013599 Genomic DNA. Translation: AAF58663.1.
    AY113523 mRNA. Translation: AAM29528.1.
    RefSeqiNP_523691.1. NM_078967.4.
    UniGeneiDm.2633.

    Genome annotation databases

    EnsemblMetazoaiFBtr0088164; FBpp0087260; FBgn0011556.
    GeneIDi36216.
    KEGGidme:Dmel_CG12387.
    UCSCiCG12387-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04853 Genomic DNA. Translation: AAA17456.1 .
    AE013599 Genomic DNA. Translation: AAF58663.1 .
    AY113523 mRNA. Translation: AAM29528.1 .
    RefSeqi NP_523691.1. NM_078967.4.
    UniGenei Dm.2633.

    3D structure databases

    ProteinModelPortali P42280.
    SMRi P42280. Positions 39-274.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62009. 2 interactions.
    IntActi P42280. 2 interactions.
    MINTi MINT-297272.
    STRINGi 7227.FBpp0087260.

    Protein family/group databases

    MEROPSi S01.116.

    Proteomic databases

    PaxDbi P42280.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088164 ; FBpp0087260 ; FBgn0011556 .
    GeneIDi 36216.
    KEGGi dme:Dmel_CG12387.
    UCSCi CG12387-RA. d. melanogaster.

    Organism-specific databases

    CTDi 36216.
    FlyBasei FBgn0011556. zetaTry.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00620000088101.
    InParanoidi P42280.
    KOi K01312.
    OrthoDBi EOG75B84T.
    PhylomeDBi P42280.

    Miscellaneous databases

    GenomeRNAii 36216.
    NextBioi 797384.

    Gene expression databases

    Bgeei P42280.

    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. "Concerted evolution within a trypsin gene cluster in Drosophila."
      Wang S., Magoulas C., Hickey D.A.
      Mol. Biol. Evol. 16:1117-1124(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Oregon-R.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.

    Entry informationi

    Entry nameiTRYZ_DROME
    AccessioniPrimary (citable) accession number: P42280
    Secondary accession number(s): Q9V5X8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: August 16, 2005
    Last modified: October 1, 2014
    This is version 116 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3