KPC1_DROME
ID KPC1_DROME Reviewed; 679 AA.
AC P05130; Q9V7V6; Q9V7V7;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Protein kinase C, brain isozyme;
DE Short=PKC;
DE EC=2.7.11.13;
DE AltName: Full=dPKC53E(BR);
GN Name=Pkc53E; Synonyms=PKC1; ORFNames=CG6622;
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 [GENOMIC DNA / MRNA] (ISOFORM SHORT).
RC STRAIN=Canton-S, and Oregon-R;
RX PubMed=3107983; DOI=10.1002/j.1460-2075.1987.tb04773.x;
RA Rosenthal A., Rhee L., Yadegari R., Paro R., Ullrich A., Goeddel D.V.;
RT "Structure and nucleotide sequence of a Drosophila melanogaster protein
RT kinase C gene.";
RL EMBO J. 6:433-441(1987).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=Berkeley; TISSUE=Ovary;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND INDUCTION BY BACTERIAL URACIL.
RX PubMed=25639794; DOI=10.1016/j.chom.2014.12.012;
RA Lee K.A., Kim B., Bhin J., Kim D.H., You H., Kim E.K., Kim S.H., Ryu J.H.,
RA Hwang D., Lee W.J.;
RT "Bacterial uracil modulates Drosophila DUOX-dependent gut immunity via
RT Hedgehog-induced signaling endosomes.";
RL Cell Host Microbe 17:191-204(2015).
CC -!- FUNCTION: PKC is activated by diacylglycerol which in turn
CC phosphorylates a range of cellular proteins (By similarity). PKC also
CC serves as the receptor for phorbol esters, a class of tumor promoters
CC (By similarity). Acts in a hh-signaling pathway which regulates the
CC Duox-dependent gut immune response to bacterial uracil; required for
CC the activation of Cad99C and consequently Cad99C-dependent endosome
CC formation, which is essential for the Duox-dependent production of
CC reactive oxygen species (ROS) in response to intestinal bacterial
CC infection (PubMed:25639794). {ECO:0000250|UniProtKB:P34885,
CC ECO:0000269|PubMed:25639794}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P05130-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P05130-2; Sequence=VSP_004743;
CC -!- TISSUE SPECIFICITY: Head neural tissue.
CC -!- INDUCTION: Up-regulated in the midgut epithelium in response to
CC bacterial uracil. {ECO:0000269|PubMed:25639794}.
CC -!- MISCELLANEOUS: This is a calcium-activated, phospholipid-dependent,
CC serine- and threonine-specific enzyme.
CC -!- MISCELLANEOUS: The sequence shown is that of Oregon-R.
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; X05076; CAA28736.1; -; mRNA.
DR EMBL; X05279; CAA28890.2; -; Genomic_DNA.
DR EMBL; X05280; CAA28890.2; JOINED; Genomic_DNA.
DR EMBL; X05281; CAA28890.2; JOINED; Genomic_DNA.
DR EMBL; X05282; CAA28890.2; JOINED; Genomic_DNA.
DR EMBL; X05283; CAA28890.2; JOINED; Genomic_DNA.
DR EMBL; AE013599; AAF57932.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57933.1; -; Genomic_DNA.
DR EMBL; AY095003; AAM11331.1; -; mRNA.
DR PIR; A32545; A32545.
DR RefSeq; NP_001261035.1; NM_001274106.1. [P05130-2]
DR RefSeq; NP_476682.1; NM_057334.3. [P05130-2]
DR RefSeq; NP_725626.1; NM_166201.3. [P05130-1]
DR AlphaFoldDB; P05130; -.
DR SMR; P05130; -.
DR BioGRID; 71309; 4.
DR IntAct; P05130; 5.
DR STRING; 7227.FBpp0086197; -.
DR PaxDb; P05130; -.
DR EnsemblMetazoa; FBtr0087048; FBpp0086197; FBgn0003091. [P05130-1]
DR EnsemblMetazoa; FBtr0087049; FBpp0086198; FBgn0003091. [P05130-2]
DR EnsemblMetazoa; FBtr0331960; FBpp0304291; FBgn0003091. [P05130-2]
DR GeneID; 48311; -.
DR KEGG; dme:Dmel_CG6622; -.
DR CTD; 48311; -.
DR FlyBase; FBgn0003091; Pkc53E.
DR VEuPathDB; VectorBase:FBgn0003091; -.
DR eggNOG; KOG0696; Eukaryota.
DR GeneTree; ENSGT00940000167637; -.
DR InParanoid; P05130; -.
DR PhylomeDB; P05130; -.
DR BRENDA; 2.7.11.13; 1994.
DR Reactome; R-DME-111933; Calmodulin induced events.
DR Reactome; R-DME-114516; Disinhibition of SNARE formation.
DR Reactome; R-DME-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-DME-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-DME-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-DME-3000170; Syndecan interactions.
DR Reactome; R-DME-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-DME-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-DME-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-DME-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-DME-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-DME-76005; Response to elevated platelet cytosolic Ca2+.
DR SignaLink; P05130; -.
DR BioGRID-ORCS; 48311; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 48311; -.
DR PRO; PR:P05130; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0003091; Expressed in oviduct (Drosophila) and 16 other tissues.
DR ExpressionAtlas; P05130; baseline and differential.
DR Genevisible; P05130; 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: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; IDA:FlyBase.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IMP:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IGI:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
DR CDD; cd00029; C1; 2.
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; IPR002219; PE/DAG-bd.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014375; Protein_kinase_C_a/b/g.
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; PIRSF000550; PKC_alpha; 1.
DR PRINTS; PR00360; C2DOMAIN.
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; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Calcium; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..679
FT /note="Protein kinase C, brain isozyme"
FT /id="PRO_0000055730"
FT DOMAIN 176..293
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 350..608
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 609..679
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 45..104
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 119..169
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 474
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 356..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 67..77
FT /note="CGYQSGYAWMG -> WG (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:3107983"
FT /id="VSP_004743"
FT VARIANT 437
FT /note="M -> I"
FT CONFLICT 608
FT /note="F -> S (in Ref. 1; CAA28736/CAA28890)"
FT /evidence="ECO:0000305"
FT CONFLICT 634..648
FT /note="DVSNFDKQFTSEKTD -> MCPTLTSSSHQRKQT (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 649..679
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 679 AA; 77695 MW; 3C69AD351E36B7DC CRC64;
MSEGSDNNGD PQQQGAEGEA VGENKMKSRL RKGALKKKNV FNVKDHCFIA RFFKQPTFCS
HCKDFICGYQ SGYAWMGFGK QGFQCQVCSY VVHKRCHEYV TFICPGKDKG IDSDSPKTQH
NFEPFTYAGP TFCDHCGSLL YGIYHQGLKC SACDMNVHAR CKENVPSLCG CDHTERRGRI
YLEINVKENL LTVQIKEGRN LIPMDPNGLS DPYVKVKLIP DDKDQSKKKT RTIKACLNPV
WNETLTYDLK PEDKDRRILI EVWDWDRTSR NDFMGALSFG ISEIIKNPTN GWFKLLTQDE
GEYYNVPCAD DEQDLLKLKQ KPSQKKPMVM RSDTNTHTSS KKDMIRATDF NFIKVLGKGS
FGKVLLAERK GSEELYAIKI LKKDVIIQDD DVECTMIEKR VLALGEKPPF LVQLHSCFQT
MDRLFFVMEY VNGGDLMFQI QQFGKFKEPV AVFYAAEIAA GLFFLHTKGI LYRDLKLDNV
LLDADGHVKI ADFGMCKENI VGDKTTKTFC GTPDYIAPEI ILYQPYGKSV DWWAYGVLLY
EMLVGQPPFD GEDEEELFAA ITDHNVSYPK SLSKEAKEAC KGFLTKQPNK RLGCGSSGEE
DVRLHPFFRR IDWEKIENRE VQPPFKPKIK HRKDVSNFDK QFTSEKTDLT PTDKVFMMNL
DQSEFVGFSY MNPEYVFSP
