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P13678

- KPC3_DROME

UniProt

P13678 - KPC3_DROME

Protein

Protein kinase C

Gene

Pkc98E

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 145 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei332 – 3321ATPPROSITE-ProRule annotation
    Active sitei427 – 4271Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri71 – 12151Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri146 – 19651Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi309 – 3179ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein kinase C activity Source: FlyBase
    4. protein serine/threonine kinase activity Source: FlyBase

    GO - Biological processi

    1. dorsal/ventral axis specification Source: FlyBase
    2. Golgi organization Source: FlyBase
    3. I-kappaB phosphorylation Source: FlyBase
    4. lipid particle organization Source: FlyBase
    5. long-term memory Source: FlyBase
    6. negative regulation of cell proliferation Source: FlyBase
    7. neuron projection morphogenesis Source: FlyBase
    8. protein phosphorylation Source: FlyBase
    9. response to ethanol Source: FlyBase

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Calcium, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BRENDAi2.7.11.13. 1994.
    ReactomeiREACT_181716. Role of phospholipids in phagocytosis.
    REACT_209941. DAG and IP3 signaling.
    SignaLinkiP13678.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C (EC:2.7.11.13)
    Short name:
    PKC
    Alternative name(s):
    dPKC98F
    Gene namesi
    Name:Pkc98E
    Synonyms:Pkc3
    ORF Names:CG1954
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0003093. Pkc98E.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 634634Protein kinase CPRO_0000055732Add
    BLAST

    Proteomic databases

    PaxDbiP13678.
    PRIDEiP13678.

    Expressioni

    Gene expression databases

    BgeeiP13678.

    Interactioni

    Protein-protein interaction databases

    BioGridi68299. 16 interactions.
    IntActiP13678. 1 interaction.
    MINTiMINT-155042.

    Structurei

    3D structure databases

    ProteinModelPortaliP13678.
    SMRiP13678. Positions 70-196, 302-625.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini303 – 560258Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini561 – 63272AGC-kinase C-terminalAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 2 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri71 – 12151Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri146 – 19651Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    InParanoidiP13678.
    KOiK18050.
    OrthoDBiEOG77M8QM.
    PhylomeDBiP13678.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR014376. Prot_kin_PKC_delta.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00130. C1_1. 2 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000551. PKC_delta. 1 hit.
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 2 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS00479. ZF_DAG_PE_1. 2 hits.
    PS50081. ZF_DAG_PE_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P13678-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQSETAVQDL WVNLEPQGKI HVIIELKNRT DKAKAEAVVE HTVAVNKEFK    50
    ERAGFNRRRG AMRRRVHQVN GHKFMATFLR QPTFCSHCRE FIWGIGKQGY 100
    QCQVCTLVVH KKCHLSVVSK CPGMRDEQPA KVEMVPAGQR FNVNLPHRFV 150
    VHSYKRFTFC DHCGSLLYGL IKQGLQCETC GMNVHKRCQK NVANTCGINT 200
    KQMAEILSSL GISPDKQQPR RSKYLNQQGG EDNYGASLGA DGDGAPGQSF 250
    RSCALSVDSL ATSTTTMTSG YNSSSCMSLA VTGSGGVGAT GETRPGKCSL 300
    LDFNFIKVLG KGSFGKVMLA EKKGTDEIYA IKVLKKDAII QDDDVDCTMT 350
    EKRILALAAN HPFLTALHSC FQTPDRLFFV MEYVNGGDLM FQIQKARRFE 400
    ASRAAFYAAE VTLALQFLHT HGVIYRDLKL DNILLDQEGH CKLADFGMCK 450
    EGIMNGMLTT TFCGTPDYIA PEILKEQEYG ASVDWWALGV LMYEMMAGQP 500
    PFEADNEDEL FDSIMHDDVL YPVWLSREAV SILKGFLTKN PEQRLGCTGD 550
    ENEIRKHPFF AKLDWKELEK RNIKPPFRPK MKNPRDANNF DAEFTKEDPV 600
    LTPIGNEVVR CINQDEFAGF SFVNPKFGPE RKVY 634
    Length:634
    Mass (Da):71,157
    Last modified:April 1, 1990 - v1
    Checksum:i3AE3A3D6B7A276BA
    GO

    Sequence cautioni

    The sequence AAF56846.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04848 mRNA. Translation: AAA28818.1.
    AE014297 Genomic DNA. Translation: AAF56846.1. Different initiation.
    PIRiB32392.
    RefSeqiNP_524545.2. NM_079821.3.
    UniGeneiDm.4053.

    Genome annotation databases

    GeneIDi43428.
    KEGGidme:Dmel_CG1954.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04848 mRNA. Translation: AAA28818.1 .
    AE014297 Genomic DNA. Translation: AAF56846.1 . Different initiation.
    PIRi B32392.
    RefSeqi NP_524545.2. NM_079821.3.
    UniGenei Dm.4053.

    3D structure databases

    ProteinModelPortali P13678.
    SMRi P13678. Positions 70-196, 302-625.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68299. 16 interactions.
    IntActi P13678. 1 interaction.
    MINTi MINT-155042.

    Proteomic databases

    PaxDbi P13678.
    PRIDEi P13678.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 43428.
    KEGGi dme:Dmel_CG1954.

    Organism-specific databases

    CTDi 43428.
    FlyBasei FBgn0003093. Pkc98E.

    Phylogenomic databases

    eggNOGi COG0515.
    InParanoidi P13678.
    KOi K18050.
    OrthoDBi EOG77M8QM.
    PhylomeDBi P13678.

    Enzyme and pathway databases

    BRENDAi 2.7.11.13. 1994.
    Reactomei REACT_181716. Role of phospholipids in phagocytosis.
    REACT_209941. DAG and IP3 signaling.
    SignaLinki P13678.

    Miscellaneous databases

    ChiTaRSi Pkc98E. drosophila.
    GenomeRNAii 43428.
    NextBioi 833872.

    Gene expression databases

    Bgeei P13678.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR014376. Prot_kin_PKC_delta.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00130. C1_1. 2 hits.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000551. PKC_delta. 1 hit.
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 2 hits.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS00479. ZF_DAG_PE_1. 2 hits.
    PS50081. ZF_DAG_PE_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of two new Drosophila protein kinase C genes, including one specifically expressed in photoreceptor cells."
      Schaeffer E., Smith D., Mardon G., Quinn W., Zuker C.
      Cell 57:403-412(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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.

    Entry informationi

    Entry nameiKPC3_DROME
    AccessioniPrimary (citable) accession number: P13678
    Secondary accession number(s): Q9VAQ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 145 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Miscellaneous

    This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme.

    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