KPC3_DROME
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 03-AUG-2022, entry version 204.
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; P13678; -.
DR PRIDE; P13678; -.
DR DNASU; 43428; -.
DR EnsemblMetazoa; FBtr0085359; FBpp0084728; FBgn0003093.
DR EnsemblMetazoa; FBtr0339150; FBpp0308295; FBgn0003093.
DR GeneID; 43428; -.
DR KEGG; dme:Dmel_CG1954; -.
DR CTD; 43428; -.
DR FlyBase; FBgn0003093; Pkc98E.
DR VEuPathDB; VectorBase:FBgn0003093; -.
DR eggNOG; KOG0694; Eukaryota.
DR GeneTree; ENSGT00940000168328; -.
DR InParanoid; P13678; -.
DR OrthoDB; 222529at2759; -.
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 tissues.
DR ExpressionAtlas; P13678; baseline and differential.
DR Genevisible; P13678; DM.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004697; F:protein kinase C activity; ISS:FlyBase.
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:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:FlyBase.
DR GO; GO:0045471; P:response to ethanol; IDA:FlyBase.
DR CDD; cd00029; C1; 2.
DR CDD; cd05591; STKc_nPKC_epsilon; 1.
DR Gene3D; 2.60.40.150; -; 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 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; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
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.
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
