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P04814

- TRYA_DROME

UniProt

P04814 - TRYA_DROME

Protein

Trypsin alpha

Gene

alphaTry

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 132 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei71 – 711Charge relay systemBy similarity
    Active sitei116 – 1161Charge relay systemBy similarity
    Sitei204 – 2041Required for specificityBy similarity
    Active sitei210 – 2101Charge 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

    MEROPSiS01.110.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trypsin alpha (EC:3.4.21.4)
    Gene namesi
    Name:alphaTry
    Synonyms:TRY-ALPHA
    ORF Names:CG18444
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0003863. alphaTry.

    Subcellular locationi

    Secretedextracellular space 1 Publication

    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 – 308Activation peptidePRO_0000028261
    Chaini31 – 256226Trypsin alphaPRO_0000028262Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi56 ↔ 72PROSITE-ProRule annotation
    Disulfide bondi180 ↔ 197PROSITE-ProRule annotation
    Disulfide bondi206 ↔ 230PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Zymogen

    Proteomic databases

    PRIDEiP04814.

    Expressioni

    Tissue specificityi

    Synthesized in the midgut of both larvae and adults, primarily in the ventriculus and gastric caeca.1 Publication

    Gene expression databases

    BgeeiP04814.

    Interactioni

    Protein-protein interaction databases

    BioGridi71314. 7 interactions.
    DIPiDIP-20031N.
    MINTiMINT-1642116.

    Structurei

    3D structure databases

    ProteinModelPortaliP04814.
    SMRiP04814. Positions 31-253.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 254224Peptidase 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

    eggNOGiNOG241902.
    GeneTreeiENSGT00620000088101.
    InParanoidiP04814.
    KOiK01312.
    OMAiMICARAT.
    OrthoDBiEOG7MKW6Q.
    PhylomeDBiP04814.

    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.

    P04814-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLKIVILLSA VVCALGGTVP EGLLPQLDGR IVGGSATTIS SFPWQISLQR    50
    SGSHSCGGSI YSANIIVTAA HCLQSVSASV LQVRAGSTYW SSGGVVAKVS 100
    SFKNHEGYNA NTMVNDIAVI RLSSSLSFSS SIKAISLATY NPANGASAAV 150
    SGWGTQSSGS SSIPSQLQYV NVNIVSQSQC ASSTYGYGSQ IRNTMICAAA 200
    SGKDACQGDS GGPLVSGGVL VGVVSWGYGC AYSNYPGVYA DVAVLRSWVV 250
    STANSI 256
    Length:256
    Mass (Da):26,041
    Last modified:August 13, 1987 - v1
    Checksum:i8B5634992F2E7C63
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02989 Genomic DNA. Translation: CAA26732.1.
    M96372 Genomic DNA. Translation: AAA28982.1.
    U04853 Genomic DNA. Translation: AAA17453.1.
    AE013599 Genomic DNA. Translation: AAF58659.1.
    AY071341 mRNA. Translation: AAL48963.1.
    PIRiA23493. TRFF.
    RefSeqiNP_476771.1. NM_057423.4.
    UniGeneiDm.1525.

    Genome annotation databases

    EnsemblMetazoaiFBtr0088161; FBpp0087257; FBgn0003863.
    GeneIDi48316.
    KEGGidme:Dmel_CG18444.
    UCSCiCG18444-RA. d. melanogaster.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02989 Genomic DNA. Translation: CAA26732.1 .
    M96372 Genomic DNA. Translation: AAA28982.1 .
    U04853 Genomic DNA. Translation: AAA17453.1 .
    AE013599 Genomic DNA. Translation: AAF58659.1 .
    AY071341 mRNA. Translation: AAL48963.1 .
    PIRi A23493. TRFF.
    RefSeqi NP_476771.1. NM_057423.4.
    UniGenei Dm.1525.

    3D structure databases

    ProteinModelPortali P04814.
    SMRi P04814. Positions 31-253.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 71314. 7 interactions.
    DIPi DIP-20031N.
    MINTi MINT-1642116.

    Protein family/group databases

    MEROPSi S01.110.

    Proteomic databases

    PRIDEi P04814.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088161 ; FBpp0087257 ; FBgn0003863 .
    GeneIDi 48316.
    KEGGi dme:Dmel_CG18444.
    UCSCi CG18444-RA. d. melanogaster.

    Organism-specific databases

    CTDi 48316.
    FlyBasei FBgn0003863. alphaTry.

    Phylogenomic databases

    eggNOGi NOG241902.
    GeneTreei ENSGT00620000088101.
    InParanoidi P04814.
    KOi K01312.
    OMAi MICARAT.
    OrthoDBi EOG7MKW6Q.
    PhylomeDBi P04814.

    Miscellaneous databases

    GenomeRNAii 48316.
    NextBioi 839305.

    Gene expression databases

    Bgeei P04814.

    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. "A gene family in Drosophila melanogaster coding for trypsin-like enzymes."
      Davis C.A., Riddell D.C., Higgins M.J., Holden J.J.A., White B.N.
      Nucleic Acids Res. 13:6605-6619(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "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].
    3. Wang S., Magoulas C., Hickey D.A.
      Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Oregon-R.
    4. "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.
    5. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.

    Entry informationi

    Entry nameiTRYA_DROME
    AccessioniPrimary (citable) accession number: P04814
    Secondary accession number(s): Q541G0, Q9V5Y2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 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