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Q24145

- SHARK_DROME

UniProt

Q24145 - SHARK_DROME

Protein

Tyrosine-protein kinase shark

Gene

shark

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    May be involved in signal transduction on the apical surface of ectodermal epithelia regulating their polarity during invagination. Crumbs (crb) may be the intracellular signal.1 Publication

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei698 – 6981ATPPROSITE-ProRule annotation
    Active sitei789 – 7891Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi668 – 6769ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. non-membrane spanning protein tyrosine kinase activity Source: FlyBase
    3. protein tyrosine kinase activity Source: FlyBase

    GO - Biological processi

    1. apoptotic cell clearance Source: FlyBase
    2. dorsal appendage formation Source: FlyBase
    3. dorsal closure Source: FlyBase
    4. dorsal closure, elongation of leading edge cells Source: FlyBase
    5. eggshell chorion assembly Source: FlyBase
    6. JNK cascade Source: FlyBase
    7. maintenance of epithelial cell apical/basal polarity Source: UniProtKB
    8. neuron projection morphogenesis Source: FlyBase
    9. peptidyl-tyrosine phosphorylation Source: GOC
    10. protein phosphorylation Source: FlyBase

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 1994.
    SignaLinkiQ24145.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase shark (EC:2.7.10.2)
    Gene namesi
    Name:shark
    Synonyms:Tk7
    ORF Names:CG18247
    OrganismiDrosophila melanogaster (Fruit fly)Imported
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0015295. shark.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: Apical expression in cephalic furrow and tracheal cells. Limited to luminal surface and absent from the basal surface.

    GO - Cellular componenti

    1. cell cortex Source: FlyBase
    2. cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 939939Tyrosine-protein kinase sharkPRO_0000088137Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei927 – 9271PhosphotyrosineSequence Analysis

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ24145.

    Expressioni

    Tissue specificityi

    Gastrulation embryos show expression in ectodermal cells along the cephalic furrow and ventral midline. Proctodeum, stomodeum and their derived structures (foregut, atrium, pharynx, esophagus and hindgut) continue to show expression from stage 8-9 to late embryos. Other ectodermally derived structures (frontal sac, salivary gland and labium) and developing tracheal system also show expression.1 Publication

    Developmental stagei

    Embryos only.1 Publication

    Gene expression databases

    BgeeiQ24145.

    Interactioni

    Protein-protein interaction databases

    BioGridi68999. 1 interaction.
    DIPiDIP-59843N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ24145.
    SMRiQ24145. Positions 10-274, 285-404, 614-928.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 10697SH2 1CuratedPROSITE-ProRule annotationAdd
    BLAST
    Repeati153 – 18533ANK 1CuratedAdd
    BLAST
    Repeati186 – 21833ANK 2CuratedAdd
    BLAST
    Repeati220 – 25233ANK 3CuratedAdd
    BLAST
    Domaini288 – 403116SH2 2CuratedPROSITE-ProRule annotationAdd
    BLAST
    Domaini662 – 921260Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family.PROSITE-ProRule annotation
    Contains 3 ANK repeats.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 2 SH2 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat, SH2 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000115195.
    InParanoidiQ24145.
    KOiK17512.
    OMAiHGEDAFF.
    OrthoDBiEOG70W3CT.
    PhylomeDBiQ24145.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    3.30.505.10. 2 hits.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF00023. Ank. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 2 hits.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00248. ANK. 4 hits.
    SM00252. SH2. 2 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF55550. SSF55550. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 3 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q24145-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRDSDPMKW YHGNLSREAA DELLKQGYED GTFLVRESST AAGDFVLSLL    50
    CQGEVCHYQV RRHGGEDAFF SIDDKVQTKI LHGLDTLVDY YQQAANGLPT 100
    KLTVPLIRDL PPHNTRSHGV TNLLHRATSK NESKVVFELL KCGYRNFDAK 150
    NQDGQTALHL AALHSDEDIL KHLLNAKVQV NSSDSFGCQP LHYAARSKPA 200
    SFIRTLISAQ ANVQGRNIDN GYVPLHEAAK HGNLEAVQEL LLAEAPPLPR 250
    TSSGEFPFDL AKEAGQTAVE EFLLNYKLPP ANTTRDQWYH GTLTREEAVA 300
    ILKKHAKELL AKQPEVDTSG CFLVRYSESP AASGLVLTLL CDQVVKNFRI 350
    SQADLYQNGN KVQSGGSKFL YIDDGPYWPS VEHLIAHFMR FSYGLPVSLK 400
    YPVPPQPKPE VPSFATIPRS NMKPKAASPA TPPTPVSPHS HHQHPHVPAL 450
    TITKKKQKEN SSSMFNTLRL TSPKKALFDM NSLRKNKSKG KRSDSESSVS 500
    GSLAGTEQEL QAAAPMLKSL SFSTEFSTFN ADGVTGSGAA AAGEVYNVPR 550
    NNTPIEIDLP PIAQKTEAEV EYFTKSDVAI ERERAGQWIG NGYQPTMDVL 600
    SLLDQQIKAP AVARLNSLGP NASTESEMAS YLHRKCSGTP STPSATEVEA 650
    AKLRFFIEPE KLVLDREIGH GEFGSVHSGW LLRKSGAGEE SRLEVAIKML 700
    SDEHSNKQEF LREASVMMRL EHKCIVRLIG IAKGEMLMMV QELAPLGSML 750
    QYILDHGHEI TANAELKVWA SQIACGMHYL ESQHFVHRDL AARNILLTAR 800
    HQAKISDFGM SRSLRPGSTE YQFTQGGRWP IRWYAPESFN LGIFSHASDV 850
    WSFGVTIWEM FSLGAPPYGE ISNVDAIKLV DSGERLPQPN LCPAYIYAVM 900
    QSCWKERPKD RPTFVYLTEF FARDPDYQNL PELVQTVHI 939
    Length:939
    Mass (Da):104,273
    Last modified:October 1, 2000 - v2
    Checksum:i37CC2C3DA25D3F52
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191A → V in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti39 – 391S → R in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti50 – 501L → F in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti85 – 851D → E in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti129 – 1291S → T in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti199 – 1991P → T in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti341 – 3411C → S in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti505 – 5062GT → RA in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti597 – 5971M → V in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti611 – 6111A → P in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti732 – 7321A → S in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti898 – 8981A → P in AAA79851. (PubMed:7892198)Curated
    Sequence conflicti935 – 9395QTVHI → KRFTFNPVSIFHFFRC in AAA79851. (PubMed:7892198)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37773 mRNA. Translation: AAA79851.1.
    AE013599 Genomic DNA. Translation: AAF58044.1.
    AY051937 mRNA. Translation: AAK93361.1.
    S55982 Genomic DNA. Translation: AAB19909.1.
    PIRiS18015.
    RefSeqiNP_524743.2. NM_080004.3.
    UniGeneiDm.6764.

    Genome annotation databases

    EnsemblMetazoaiFBtr0087244; FBpp0086382; FBgn0015295.
    GeneIDi44353.
    KEGGidme:Dmel_CG18247.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37773 mRNA. Translation: AAA79851.1 .
    AE013599 Genomic DNA. Translation: AAF58044.1 .
    AY051937 mRNA. Translation: AAK93361.1 .
    S55982 Genomic DNA. Translation: AAB19909.1 .
    PIRi S18015.
    RefSeqi NP_524743.2. NM_080004.3.
    UniGenei Dm.6764.

    3D structure databases

    ProteinModelPortali Q24145.
    SMRi Q24145. Positions 10-274, 285-404, 614-928.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68999. 1 interaction.
    DIPi DIP-59843N.

    Proteomic databases

    PaxDbi Q24145.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0087244 ; FBpp0086382 ; FBgn0015295 .
    GeneIDi 44353.
    KEGGi dme:Dmel_CG18247.

    Organism-specific databases

    CTDi 44353.
    FlyBasei FBgn0015295. shark.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115195.
    InParanoidi Q24145.
    KOi K17512.
    OMAi HGEDAFF.
    OrthoDBi EOG70W3CT.
    PhylomeDBi Q24145.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 1994.
    SignaLinki Q24145.

    Miscellaneous databases

    ChiTaRSi shark. drosophila.
    GenomeRNAii 44353.
    NextBioi 837182.

    Gene expression databases

    Bgeei Q24145.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    3.30.505.10. 2 hits.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF00023. Ank. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 2 hits.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00248. ANK. 4 hits.
    SM00252. SH2. 2 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF55550. SSF55550. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 3 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Shark, a Src homology 2, ankyrin repeat, tyrosine kinase, is expressed on the apical surfaces of ectodermal epithelia."
      Ferrante A.W. Jr., Reinke R., Stanley E.R.
      Proc. Natl. Acad. Sci. U.S.A. 92:1911-1915(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Embryo.
    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.
    5. "Identification of seven novel protein-tyrosine kinase genes of Drosophila by the polymerase chain reaction."
      Shishido E., Emori Y., Saigo K.
      FEBS Lett. 289:235-238(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 793-849.

    Entry informationi

    Entry nameiSHARK_DROME
    AccessioniPrimary (citable) accession number: Q24145
    Secondary accession number(s): Q26299, Q9V7K5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 130 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3