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P42279

- TRYU_DROME

UniProt

P42279 - TRYU_DROME

Protein

Trypsin eta

Gene

etaTry

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 106 (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 sitei74 – 741Charge relay systemBy similarity
    Active sitei120 – 1201Charge relay systemBy similarity
    Sitei209 – 2091Required for specificityBy similarity
    Active sitei215 – 2151Charge 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

    MEROPSiS01.117.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trypsin eta (EC:3.4.21.4)
    Gene namesi
    Name:etaTry
    ORF Names:CG12386
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0011554. etaTry.

    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 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 275Activation peptidePRO_0000028283
    Chaini28 – 262235Trypsin etaPRO_0000028284Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi59 ↔ 75PROSITE-ProRule annotation
    Disulfide bondi185 ↔ 200PROSITE-ProRule annotation
    Disulfide bondi211 ↔ 235PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiP42279.

    Expressioni

    Gene expression databases

    BgeeiP42279.

    Interactioni

    Protein-protein interaction databases

    BioGridi62010. 1 interaction.
    MINTiMINT-317423.

    Structurei

    3D structure databases

    ProteinModelPortaliP42279.
    SMRiP42279. Positions 28-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 259232Peptidase 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.
    InParanoidiP42279.
    KOiK01312.
    OMAiYWRPISE.
    OrthoDBiEOG75B84T.
    PhylomeDBiP42279.

    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.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P42279-1 [UniParc]FASTAAdd to Basket

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    MNKVILRILA VLFLLGIYAV SAQSDGRIVG GADTSSYYTK YVVQLRRRSS    50
    SSSSYAQTCG GCILDAVTIA TAAHCVYNRE AENFLVVAGD DSRGGMNGVV 100
    VRVSKLIPHE LYNSSTMDND IALVVVDPPL PLDSFSTMEA IEIASEQPAV 150
    GVQATISGWG YTKENGLSSD QLQQVKVPIV DSEKCQEAYY WRPISEGMLC 200
    AGLSEGGKDA CQGDSGGPLV VANKLAGIVS WGEGCARPNY PGVYANVAYY 250
    KDWIAKQRTS YV 262
    Length:262
    Mass (Da):28,088
    Last modified:August 16, 2005 - v2
    Checksum:iBE908F7602A611DC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81I → V in AAA17455. (PubMed:10486967)Curated
    Sequence conflicti24 – 241S → P in AAA17455. (PubMed:10486967)Curated
    Sequence conflicti88 – 881A → S in AAA17455. (PubMed:10486967)Curated
    Sequence conflicti97 – 971N → Y in AAA17455. (PubMed:10486967)Curated
    Sequence conflicti105 – 1051K → Q in AAA17455. (PubMed:10486967)Curated
    Sequence conflicti142 – 1421E → V in AAA17455. (PubMed:10486967)Curated
    Sequence conflicti149 – 1491A → P in AAA17455. (PubMed:10486967)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04853 Genomic DNA. Translation: AAA17455.1.
    AE013599 Genomic DNA. Translation: AAF58662.1.
    BT012306 mRNA. Translation: AAS77431.1.
    RefSeqiNP_523692.1. NM_078968.2.
    UniGeneiDm.23664.

    Genome annotation databases

    EnsemblMetazoaiFBtr0088163; FBpp0087259; FBgn0011554.
    GeneIDi36217.
    KEGGidme:Dmel_CG12386.
    UCSCiCG12386-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04853 Genomic DNA. Translation: AAA17455.1 .
    AE013599 Genomic DNA. Translation: AAF58662.1 .
    BT012306 mRNA. Translation: AAS77431.1 .
    RefSeqi NP_523692.1. NM_078968.2.
    UniGenei Dm.23664.

    3D structure databases

    ProteinModelPortali P42279.
    SMRi P42279. Positions 28-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62010. 1 interaction.
    MINTi MINT-317423.

    Protein family/group databases

    MEROPSi S01.117.

    Proteomic databases

    PaxDbi P42279.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088163 ; FBpp0087259 ; FBgn0011554 .
    GeneIDi 36217.
    KEGGi dme:Dmel_CG12386.
    UCSCi CG12386-RA. d. melanogaster.

    Organism-specific databases

    CTDi 36217.
    FlyBasei FBgn0011554. etaTry.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00620000088101.
    InParanoidi P42279.
    KOi K01312.
    OMAi YWRPISE.
    OrthoDBi EOG75B84T.
    PhylomeDBi P42279.

    Miscellaneous databases

    GenomeRNAii 36217.
    NextBioi 797389.

    Gene expression databases

    Bgeei P42279.

    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.
    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. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-262.
      Strain: Berkeley.
      Tissue: Larva and Pupae.

    Entry informationi

    Entry nameiTRYU_DROME
    AccessioniPrimary (citable) accession number: P42279
    Secondary accession number(s): Q6NLM5, Q9V5X9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: August 16, 2005
    Last modified: October 1, 2014
    This is version 106 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