ID   KPC3_DROME              Reviewed;         739 AA.
AC   P13678; A0A0B4LHW0; Q9VAQ6;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 2.
DT   24-JAN-2024, entry version 209.
DE   RecName: Full=Protein kinase C;
DE            Short=PKC;
DE            EC=2.7.11.13;
DE   AltName: Full=dPKC98F;
GN   Name=Pkc98E; Synonyms=Pkc3; ORFNames=CG1954;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2720775; DOI=10.1016/0092-8674(89)90915-x;
RA   Schaeffer E., Smith D., Mardon G., Quinn W., Zuker C.;
RT   "Isolation and characterization of two new Drosophila protein kinase C
RT   genes, including one specifically expressed in photoreceptor cells.";
RL   Cell 57:403-412(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
CC   -!- FUNCTION: PKC is activated by diacylglycerol which in turn
CC       phosphorylates a range of cellular proteins. PKC also serves as the
CC       receptor for phorbol esters, a class of tumor promoters.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.13;
CC   -!- MISCELLANEOUS: This is a calcium-activated, phospholipid-dependent,
CC       serine- and threonine-specific enzyme.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA28818.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; J04848; AAA28818.1; ALT_FRAME; mRNA.
DR   EMBL; AE014297; AAF56846.1; -; Genomic_DNA.
DR   EMBL; AE014297; AHN57576.1; -; Genomic_DNA.
DR   PIR; B32392; B32392.
DR   RefSeq; NP_001287577.1; NM_001300648.1.
DR   RefSeq; NP_524545.2; NM_079821.4.
DR   AlphaFoldDB; P13678; -.
DR   SMR; P13678; -.
DR   BioGRID; 68299; 17.
DR   IntAct; P13678; 1.
DR   STRING; 7227.FBpp0084728; -.
DR   BindingDB; P13678; -.
DR   PaxDb; 7227-FBpp0084728; -.
DR   DNASU; 43428; -.
DR   EnsemblMetazoa; FBtr0085359; FBpp0084728; FBgn0003093.
DR   EnsemblMetazoa; FBtr0339150; FBpp0308295; FBgn0003093.
DR   GeneID; 43428; -.
DR   KEGG; dme:Dmel_CG1954; -.
DR   AGR; FB:FBgn0003093; -.
DR   CTD; 43428; -.
DR   FlyBase; FBgn0003093; Pkc98E.
DR   VEuPathDB; VectorBase:FBgn0003093; -.
DR   eggNOG; KOG0694; Eukaryota.
DR   GeneTree; ENSGT00940000168328; -.
DR   InParanoid; P13678; -.
DR   OMA; VARICTC; -.
DR   OrthoDB; 841660at2759; -.
DR   PhylomeDB; P13678; -.
DR   BRENDA; 2.7.11.13; 1994.
DR   Reactome; R-DME-114508; Effects of PIP2 hydrolysis.
DR   Reactome; R-DME-1250196; SHC1 events in ERBB2 signaling.
DR   Reactome; R-DME-1489509; DAG and IP3 signaling.
DR   Reactome; R-DME-2029485; Role of phospholipids in phagocytosis.
DR   SignaLink; P13678; -.
DR   BioGRID-ORCS; 43428; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Pkc98E; fly.
DR   GenomeRNAi; 43428; -.
DR   PRO; PR:P13678; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0003093; Expressed in brain and 26 other cell types or tissues.
DR   ExpressionAtlas; P13678; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; ISS:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IMP:FlyBase.
DR   GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0034389; P:lipid droplet organization; IMP:FlyBase.
DR   GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:FlyBase.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:FlyBase.
DR   GO; GO:0045471; P:response to ethanol; IDA:FlyBase.
DR   CDD; cd20835; C1_nPKC_epsilon-like_rpt1; 1.
DR   CDD; cd20838; C1_nPKC_epsilon-like_rpt2; 1.
DR   CDD; cd04014; C2_PKC_epsilon; 1.
DR   CDD; cd05591; STKc_nPKC_epsilon; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR034669; nPKC_epsilon.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR014376; Prot_kin_PKC_delta.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF201; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000551; PKC_delta; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
DR   Genevisible; P13678; DM.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Kinase; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..739
FT                   /note="Protein kinase C"
FT                   /id="PRO_0000055732"
FT   DOMAIN          1..117
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          408..665
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          666..737
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   ZN_FING         176..226
FT                   /note="Phorbol-ester/DAG-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   ZN_FING         251..301
FT                   /note="Phorbol-ester/DAG-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   ACT_SITE        532
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         414..422
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         437
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   739 AA;  83107 MW;  FB3322575FCE5BC5 CRC64;
     MFTGKLQIKV CEASGLRPTD FQKRHNLTFG KLADEQLIDP YVSIDVDESH FDRATTRPKT
     FDPVWNEQFV HDVTNVSNIN LTVFHDAALP PDDFVANCII SFEDLMQSET AVQDLWVNLE
     PQGKIHVIIE LKNRTDKAKA EAVVEHTVAV NKEFKERAGF NRRRGAMRRR VHQVNGHKFM
     ATFLRQPTFC SHCREFIWGI GKQGYQCQVC TLVVHKKCHL SVVSKCPGMR DEQPAKVEMV
     PAGQRFNVNL PHRFVVHSYK RFTFCDHCGS LLYGLIKQGL QCETCGMNVH KRCQKNVANT
     CGINTKQMAE ILSSLGISPD KQQPRRSKYL NQQGGEDNYG ASLGADGDGA PGQSFRSCAL
     SVDSLATSTT TMTSGYNSSS CMSLAVTGSG GVGATGETRP GKCSLLDFNF IKVLGKGSFG
     KVMLAEKKGT DEIYAIKVLK KDAIIQDDDV DCTMTEKRIL ALAANHPFLT ALHSCFQTPD
     RLFFVMEYVN GGDLMFQIQK ARRFEASRAA FYAAEVTLAL QFLHTHGVIY RDLKLDNILL
     DQEGHCKLAD FGMCKEGIMN GMLTTTFCGT PDYIAPEILK EQEYGASVDW WALGVLMYEM
     MAGQPPFEAD NEDELFDSIM HDDVLYPVWL SREAVSILKG FLTKNPEQRL GCTGDENEIR
     KHPFFAKLDW KELEKRNIKP PFRPKMKNPR DANNFDAEFT KEDPVLTPIG NEVVRCINQD
     EFAGFSFVNP KFGPERKVY
//