ID   KPC4_DROME              Reviewed;         671 AA.
AC   P83099; Q5BIE9; Q9VYN2;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 3.
DT   02-SEP-2026, entry version 200.
DE   RecName: Full=Putative protein kinase C delta type homolog {ECO:0000312|FlyBase:FBgn0287828};
DE            EC=2.7.11.13;
GN   Name=Pkcdelta {ECO:0000312|FlyBase:FBgn0287828};
GN   ORFNames=CG10524 {ECO:0000312|FlyBase:FBgn0287828};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
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   [2]
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily. {ECO:0000305}.
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DR   EMBL; AE014298; AAF48160.3; -; Genomic_DNA.
DR   EMBL; BT021275; AAX33423.1; -; mRNA.
DR   RefSeq; NP_001138191.1; NM_001144719.2.
DR   RefSeq; NP_511171.3; NM_078616.4.
DR   AlphaFoldDB; P83099; -.
DR   SMR; P83099; -.
DR   BioGRID; 58590; 3.
DR   DIP; DIP-18369N; -.
DR   FunCoup; P83099; 117.
DR   IntAct; P83099; 3.
DR   STRING; 7227.FBpp0309085; -.
DR   PaxDb; 7227-FBpp0309085; -.
DR   PeptideAtlas; P83099; -.
DR   EnsemblMetazoa; FBtr0299936; FBpp0289213; FBgn0287828.
DR   EnsemblMetazoa; FBtr0299937; FBpp0289214; FBgn0287828.
DR   GeneID; 32191; -.
DR   KEGG; dme:Dmel_CG42349; -.
DR   AGR; FB:FBgn0287828; -.
DR   CTD; 32191; -.
DR   FlyBase; FBgn0287828; Pkcdelta.
DR   VEuPathDB; VectorBase:FBgn0287828; -.
DR   eggNOG; KOG0694; Eukaryota.
DR   HOGENOM; CLU_000288_54_4_1; -.
DR   InParanoid; P83099; -.
DR   OrthoDB; 10047816at2759; -.
DR   PhylomeDB; P83099; -.
DR   Reactome; R-DME-111465; Apoptotic cleavage of cellular proteins.
DR   Reactome; R-DME-111933; Calmodulin induced events.
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-202424; Downstream TCR signaling.
DR   Reactome; R-DME-2029485; Role of phospholipids in phagocytosis.
DR   Reactome; R-DME-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-DME-373752; Netrin-1 signaling.
DR   Reactome; R-DME-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR   Reactome; R-DME-5218921; VEGFR2 mediated cell proliferation.
DR   Reactome; R-DME-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-9648002; RAS processing.
DR   BioGRID-ORCS; 32191; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 32191; -.
DR   PRO; PR:P83099; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0259680; Expressed in muscle cell in body wall and 66 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004699; F:diacylglycerol-dependent, calcium-independent serine/threonine kinase activity; ISS:FlyBase.
DR   GO; GO:0004687; F:myosin light chain kinase activity; IMP: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:0060361; P:flight; IMP:FlyBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   CDD; cd20834; C1_nPKC_theta-like_rpt1; 1.
DR   CDD; cd20837; C1_nPKC_theta-like_rpt2; 1.
DR   CDD; cd05592; STKc_nPKC_theta_like; 1.
DR   FunFam; 1.10.510.10:FF:000023; Protein kinase C; 1.
DR   FunFam; 3.30.60.20:FF:000003; Protein kinase C delta; 1.
DR   FunFam; 3.30.60.20:FF:000008; Protein kinase C theta; 1.
DR   FunFam; 3.30.200.20:FF:000020; Protein kinase C, alpha; 1.
DR   Gene3D; 3.30.60.20; -; 2.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 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; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PKC_DAG/PE.
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; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00130; C1_1; 2.
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; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 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; 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; Kinase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..671
FT                   /note="Putative protein kinase C delta type homolog"
FT                   /id="PRO_0000055733"
FT   DOMAIN          343..601
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          602..671
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   ZN_FING         144..194
FT                   /note="Phorbol-ester/DAG-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   ZN_FING         216..266
FT                   /note="Phorbol-ester/DAG-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          1..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..27
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..116
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        467
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         349..357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         372
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   671 AA;  76333 MW;  552783774078196C CRC64;
     MMFTRAQVRK QKTSNSSSQR PRSSGGSTRH ETRYKQSSTS SSGAGSGLSG ASGASGARRD
     QYRDRDHYGK HSFELPRQHS KEEAYHRDRE SSAGGVDRGE RSGIGGNGGG VTGGGVYVDR
     RTRPRSITNR RGAIKHQKTH DINGHRFVAK FFRQPTFCAF CNLFLWGFGK QGYQCIICQT
     VVHKKCHDKL LGKCSGSVFT SASTILLRER FKIDMPHRFK PHTFMSPTFC DHCGSLMGGF
     FIQGLKCEEC DVNCHKKCER LTANLCGVNQ KLIVEALNHV KRGAREARDS PSTPPSLNPA
     YKIEASEEHD ETSYTYSQFQ KSGRFTAPAT VIPRFKNYSV DDFHFLAVLG KGSFGKVLLA
     ELRDTTYYYA IKCLKKDVVL EDDDVDSTLI ERKVLALGTK HPYLCHLFCT FQTESHLFFV
     MEYLNGGDLM FHIQESGRFS EERARFYGAE IISGLKFLHK KGIIYRDLKL DNVLLDYEGH
     VRIADFGMCK LQIYLDKTAD SFCGTPDYMA PEIIKGEKYN QNVDWWSFGV LLYEMLIGQS
     PFSGCDEDEL FWSICNEIPW FPVYISAEAT GILKGLLEKD YTKRIGSQYS PAGDIADHIF
     FRPIDWGLLE KRQIEPPFKP QVKHPLDTQY FDRVFTRERV RLTPIDKEIL ASMDQKQFHG
     FTYTNPHITL D
//