APKC_DROME
ID APKC_DROME Reviewed; 606 AA.
AC A1Z9X0; Q0E971; Q0E972; Q0E973; Q0E974; Q8MT38; Q9GSZ3;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Atypical protein kinase C {ECO:0000312|EMBL:AAF58177.2};
DE EC=2.7.11.13;
GN Name=aPKC {ECO:0000312|EMBL:AAF58177.2, ECO:0000312|FlyBase:FBgn0261854};
GN ORFNames=CG30475;
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] {ECO:0000305, ECO:0000312|EMBL:AAG01528.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH BAZ,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10995441; DOI=10.1083/jcb.150.6.1361;
RA Wodarz A., Ramrath A., Grimm A., Knust E.;
RT "Drosophila atypical protein kinase C associates with Bazooka and controls
RT polarity of epithelia and neuroblasts.";
RL J. Cell Biol. 150:1361-1374(2000).
RN [2]
RP ERRATUM OF PUBMED:10995441.
RA Wodarz A., Ramrath A., Grimm A., Knust E.;
RL J. Cell Biol. 165:591-591(2004).
RN [3] {ECO:0000312|EMBL:AAF58177.2}
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 [4] {ECO:0000312|EMBL:AAF58177.2}
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAM48431.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6] {ECO:0000305, ECO:0000312|EMBL:ACL68694.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11734648; DOI=10.1073/pnas.261565198;
RA Cox D.N., Seyfried S.A., Jan L.Y., Jan Y.N.;
RT "Bazooka and atypical protein kinase C are required to regulate oocyte
RT differentiation in the Drosophila ovary.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14475-14480(2001).
RN [8] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH REF(2)P.
RX PubMed=12446795; DOI=10.1128/mcb.22.24.8787-8795.2002;
RA Avila A., Silverman N., Diaz-Meco M.T., Moscat J.;
RT "The Drosophila atypical protein kinase C-ref(2)p complex constitutes a
RT conserved module for signaling in the toll pathway.";
RL Mol. Cell. Biol. 22:8787-8795(2002).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=11914720; DOI=10.1038/nn820;
RA Drier E.A., Tello M.K., Cowan M., Wu P., Blace N., Sacktor T.C., Yin J.C.;
RT "Memory enhancement and formation by atypical PKM activity in Drosophila
RT melanogaster.";
RL Nat. Neurosci. 5:316-324(2002).
RN [10] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14657233; DOI=10.1083/jcb.200306079;
RA Rolls M.M., Albertson R., Shih H.P., Lee C.Y., Doe C.Q.;
RT "Drosophila aPKC regulates cell polarity and cell proliferation in
RT neuroblasts and epithelia.";
RL J. Cell Biol. 163:1089-1098(2003).
RN [11] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CRB AND PATJ, AND SUBCELLULAR LOCATION.
RX PubMed=15302858; DOI=10.1083/jcb.200311031;
RA Sotillos S., Diaz-Meco M.T., Caminero E., Moscat J., Campuzano S.;
RT "DaPKC-dependent phosphorylation of Crumbs is required for epithelial cell
RT polarity in Drosophila.";
RL J. Cell Biol. 166:549-557(2004).
RN [12] {ECO:0000305}
RP FUNCTION.
RX PubMed=15907474; DOI=10.1016/j.cell.2005.03.014;
RA Djiane A., Yogev S., Mlodzik M.;
RT "The apical determinants aPKC and dPatj regulate Frizzled-dependent planar
RT cell polarity in the Drosophila eye.";
RL Cell 121:621-631(2005).
RN [13] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17488624; DOI=10.1016/j.devcel.2007.02.011;
RA Harris T.J., Peifer M.;
RT "aPKC controls microtubule organization to balance adherens junction
RT symmetry and planar polarity during development.";
RL Dev. Cell 12:727-738(2007).
RN [14] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH L(2)GL.
RX PubMed=18094021; DOI=10.1242/dev.016253;
RA Tian A.G., Deng W.M.;
RT "Lgl and its phosphorylation by aPKC regulate oocyte polarity formation in
RT Drosophila.";
RL Development 135:463-471(2008).
RN [15] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DAP160, AND SUBCELLULAR LOCATION.
RX PubMed=18614576; DOI=10.1242/dev.024059;
RA Chabu C., Doe C.Q.;
RT "Dap160/intersectin binds and activates aPKC to regulate cell polarity and
RT cell cycle progression.";
RL Development 135:2739-2746(2008).
RN [16] {ECO:0000305}
RP FUNCTION.
RX PubMed=19472188; DOI=10.1002/dneu.20728;
RA Ramachandran P., Barria R., Ashley J., Budnik V.;
RT "A critical step for postsynaptic F-actin organization: regulation of
RT Baz/Par-3 localization by aPKC and PTEN.";
RL Dev. Neurobiol. 69:583-602(2009).
RN [17] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20434988; DOI=10.1016/j.cell.2010.02.040;
RA Morais-de-Sa E., Mirouse V., St Johnston D.;
RT "aPKC phosphorylation of Bazooka defines the apical/lateral border in
RT Drosophila epithelial cells.";
RL Cell 141:509-523(2010).
RN [18] {ECO:0000305}
RP FUNCTION.
RX PubMed=22223679; DOI=10.1242/dev.071027;
RA Guilgur L.G., Prudencio P., Ferreira T., Pimenta-Marques A.R.,
RA Martinho R.G.;
RT "Drosophila aPKC is required for mitotic spindle orientation during
RT symmetric division of epithelial cells.";
RL Development 139:503-513(2012).
RN [19] {ECO:0000305}
RP FUNCTION, INTERACTION WITH YRT, AND DISRUPTION PHENOTYPE.
RX PubMed=24515345; DOI=10.1083/jcb.201308032;
RA Gamblin C.L., Hardy E.J., Chartier F.J., Bisson N., Laprise P.;
RT "A bidirectional antagonism between aPKC and Yurt regulates epithelial cell
RT polarity.";
RL J. Cell Biol. 204:487-495(2014).
RN [20] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24830287; DOI=10.1371/journal.pgen.1004380;
RA Xu S., Tyagi S., Schedl P.;
RT "Spermatid cyst polarization in Drosophila depends upon apkc and the CPEB
RT family translational regulator orb2.";
RL PLoS Genet. 10:E1004380-E1004380(2014).
CC -!- FUNCTION: Serine/threonine protein kinase which is required for apico-
CC basal cell polarity in the germ line as well as in epithelial and
CC neural precursor cells, for epithelial planar cell polarity and for
CC cell proliferation. During oocyte development, required for the
CC posterior translocation of oocyte specification factors and for the
CC posterior establishment of the microtubule organizing center within the
CC presumptive oocyte. Phosphorylates l(2)gl which restricts l(2)gl
CC activity to the oocyte posterior and regulates posterior enrichment of
CC par-1, leading to establishment of correct oocyte polarity. Essential
CC for apical localization of l(2)gl and par-6 in neuroblasts and for
CC exclusion of mira from the apical cortex. Phosphorylates baz which is
CC required for targeting of baz to the postsynaptic region where it is
CC involved in actin organization, and for apical exclusion of baz which
CC is necessary for establishment of the apical/lateral border in
CC epithelial cells. Phosphorylates yrt which prevents its premature
CC apical localization and is necessary for correct epithelial cell
CC polarization. Required for the establishment of mitotic spindle
CC orientation during symmetric division of epithelial cells and for
CC apical exclusion of raps/Pins. Involved in symmetric adherens junction
CC positioning during embryogenesis. Required for polarization of the
CC spermatid cyst which is necessary for sperm differentiation. Required
CC for stimulation of the Toll signaling pathway which activates Dif and
CC dl and plays a role in innate immunity. Plays a role in memory
CC enhancement. {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:11734648,
CC ECO:0000269|PubMed:11914720, ECO:0000269|PubMed:12446795,
CC ECO:0000269|PubMed:14657233, ECO:0000269|PubMed:15302858,
CC ECO:0000269|PubMed:15907474, ECO:0000269|PubMed:17488624,
CC ECO:0000269|PubMed:18094021, ECO:0000269|PubMed:18614576,
CC ECO:0000269|PubMed:19472188, ECO:0000269|PubMed:20434988,
CC ECO:0000269|PubMed:22223679, ECO:0000269|PubMed:24515345,
CC ECO:0000269|PubMed:24830287}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with baz; the interaction is required for apical
CC localization of aPKC in neuroblasts and epithelial cells. Interacts
CC with Dap160; the interaction promotes aPKC apical localization and
CC kinase activity. Interacts with and phosphorylates l(2)gl and yrt.
CC Interacts with crb and ref(2)P. Forms a complex with baz, fz and Patj.
CC {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:12446795,
CC ECO:0000269|PubMed:15302858, ECO:0000269|PubMed:18094021,
CC ECO:0000269|PubMed:18614576, ECO:0000269|PubMed:24515345}.
CC -!- INTERACTION:
CC A1Z9X0; O96782: baz; NbExp=2; IntAct=EBI-160861, EBI-867941;
CC A1Z9X0; Q9VX75: baz; NbExp=3; IntAct=EBI-160861, EBI-2295779;
CC A1Z9X0; P10040: crb; NbExp=3; IntAct=EBI-160861, EBI-672928;
CC A1Z9X0; O97111: par-6; NbExp=6; IntAct=EBI-160861, EBI-186645;
CC A1Z9X0; Q9NB04: Patj; NbExp=2; IntAct=EBI-160861, EBI-442573;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:11734648,
CC ECO:0000269|PubMed:15302858, ECO:0000269|PubMed:18614576,
CC ECO:0000269|PubMed:20434988, ECO:0000269|PubMed:24830287}. Apicolateral
CC cell membrane {ECO:0000269|PubMed:10995441,
CC ECO:0000269|PubMed:11734648, ECO:0000269|PubMed:15302858,
CC ECO:0000269|PubMed:18614576, ECO:0000269|PubMed:20434988,
CC ECO:0000269|PubMed:24830287}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:11734648,
CC ECO:0000269|PubMed:15302858, ECO:0000269|PubMed:18614576,
CC ECO:0000269|PubMed:20434988, ECO:0000269|PubMed:24830287}.
CC Note=Cytoplasmic at interphase but localizes to the apical cell cortex
CC during mitosis. {ECO:0000269|PubMed:10995441,
CC ECO:0000269|PubMed:11734648, ECO:0000269|PubMed:15302858,
CC ECO:0000269|PubMed:18614576, ECO:0000269|PubMed:20434988,
CC ECO:0000269|PubMed:24830287}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=A {ECO:0000269|PubMed:10995441}; Synonyms=C
CC {ECO:0000312|FlyBase:FBgn0261854};
CC IsoId=A1Z9X0-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:12537572};
CC IsoId=A1Z9X0-2; Sequence=VSP_056765, VSP_056766, VSP_056768;
CC Name=D {ECO:0000269|PubMed:12537572};
CC IsoId=A1Z9X0-3; Sequence=VSP_056768;
CC Name=E {ECO:0000269|PubMed:12537572};
CC IsoId=A1Z9X0-4; Sequence=VSP_056765, VSP_056766;
CC Name=F {ECO:0000269|PubMed:12537572};
CC IsoId=A1Z9X0-5; Sequence=VSP_056764, VSP_056767;
CC -!- TISSUE SPECIFICITY: Expressed in the testis. In spermatid cysts,
CC localizes near the tips of spermatid flagellar axonemes (at protein
CC level). Detectable in freshly laid eggs before onset of zygotic
CC transcription so is deposited in the egg during oogenesis. At the
CC cellular blastoderm stage, present in all cells except the pole cells.
CC During gastrulation, strongly expressed in tissues undergoing
CC morphogenetic movements such as invaginating mesoderm, proctodeum and
CC cephalic furrow. Strongly expressed in neuroblasts.
CC {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:24830287}.
CC -!- DISRUPTION PHENOTYPE: Zygotes survive to mid-larval stages where they
CC exhibit defects in neuroblast and epithelial cell polarity. Mutant
CC neuroblasts lack apical localization of l(2)gl and par-6, and fail to
CC exclude mira from the apical cortex. Oocytes do not differentiate and
CC display failure of BicD and ORB to translocate from the anterior to the
CC posterior crescent, accumulation of Dhc64C in the two posterior-most
CC presumptive pre-oocytes instead of in a single cell as normal, and
CC defective posterior assembly of the microtubule organizing center.
CC Adherens junctions form atypical planar-polarized puncta at
CC gastrulation. Reduced yrt phosphorylation.
CC {ECO:0000269|PubMed:11734648, ECO:0000269|PubMed:14657233,
CC ECO:0000269|PubMed:17488624, ECO:0000269|PubMed:24515345}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000255}.
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DR EMBL; AF288482; AAG01528.1; -; mRNA.
DR EMBL; AE013599; AAF58177.2; -; Genomic_DNA.
DR EMBL; AE013599; ABI31090.1; -; Genomic_DNA.
DR EMBL; AE013599; ABI31091.1; -; Genomic_DNA.
DR EMBL; AE013599; ABI31092.1; -; Genomic_DNA.
DR EMBL; AE013599; ABI31093.1; -; Genomic_DNA.
DR EMBL; AE013599; ABI31094.1; -; Genomic_DNA.
DR EMBL; AY118402; AAM48431.1; -; mRNA.
DR EMBL; BT056247; ACL68694.1; -; mRNA.
DR RefSeq; NP_001036541.1; NM_001043076.3. [A1Z9X0-1]
DR RefSeq; NP_001036542.1; NM_001043077.3. [A1Z9X0-5]
DR RefSeq; NP_001036543.1; NM_001043078.2. [A1Z9X0-4]
DR RefSeq; NP_001036544.1; NM_001043079.2. [A1Z9X0-2]
DR RefSeq; NP_001036545.1; NM_001043080.3. [A1Z9X0-3]
DR RefSeq; NP_524892.2; NM_080153.5. [A1Z9X0-1]
DR AlphaFoldDB; A1Z9X0; -.
DR SMR; A1Z9X0; -.
DR BioGRID; 70851; 56.
DR IntAct; A1Z9X0; 10.
DR STRING; 7227.FBpp0302921; -.
DR iPTMnet; A1Z9X0; -.
DR PaxDb; A1Z9X0; -.
DR PRIDE; A1Z9X0; -.
DR EnsemblMetazoa; FBtr0303429; FBpp0292486; FBgn0261854. [A1Z9X0-2]
DR EnsemblMetazoa; FBtr0303430; FBpp0292487; FBgn0261854. [A1Z9X0-1]
DR EnsemblMetazoa; FBtr0303431; FBpp0292488; FBgn0261854. [A1Z9X0-3]
DR EnsemblMetazoa; FBtr0303432; FBpp0292489; FBgn0261854. [A1Z9X0-4]
DR EnsemblMetazoa; FBtr0303433; FBpp0292490; FBgn0261854. [A1Z9X0-5]
DR EnsemblMetazoa; FBtr0303434; FBpp0292491; FBgn0261854. [A1Z9X0-1]
DR GeneID; 47594; -.
DR KEGG; dme:Dmel_CG42783; -.
DR UCSC; CG10261-RA; d. melanogaster. [A1Z9X0-1]
DR UCSC; CG10261-RB; d. melanogaster.
DR UCSC; CG10261-RD; d. melanogaster.
DR UCSC; CG10261-RE; d. melanogaster.
DR UCSC; CG10261-RF; d. melanogaster.
DR CTD; 47594; -.
DR FlyBase; FBgn0261854; aPKC.
DR VEuPathDB; VectorBase:FBgn0261854; -.
DR eggNOG; KOG0695; Eukaryota.
DR GeneTree; ENSGT00940000169305; -.
DR OMA; RIQCFIC; -.
DR PhylomeDB; A1Z9X0; -.
DR Reactome; R-DME-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-DME-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-DME-9634635; Estrogen-stimulated signaling through PRKCZ.
DR SignaLink; A1Z9X0; -.
DR BioGRID-ORCS; 47594; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 47594; -.
DR PRO; PR:A1Z9X0; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0261854; Expressed in wing disc and 30 other tissues.
DR ExpressionAtlas; A1Z9X0; baseline and differential.
DR Genevisible; A1Z9X0; DM.
DR GO; GO:0045179; C:apical cortex; IDA:FlyBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005938; C:cell cortex; TAS:FlyBase.
DR GO; GO:0035003; C:subapical complex; TAS: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:0017022; F:myosin binding; IPI:FlyBase.
DR GO; GO:0004697; F:protein kinase C activity; IDA:UniProtKB.
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:0034332; P:adherens junction organization; IMP:UniProtKB.
DR GO; GO:0045176; P:apical protein localization; NAS:FlyBase.
DR GO; GO:0055059; P:asymmetric neuroblast division; IGI:FlyBase.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IPI:FlyBase.
DR GO; GO:0060446; P:branching involved in open tracheal system development; IMP:FlyBase.
DR GO; GO:0007043; P:cell-cell junction assembly; NAS:FlyBase.
DR GO; GO:0046667; P:compound eye retinal cell programmed cell death; IDA:FlyBase.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:FlyBase.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IGI:FlyBase.
DR GO; GO:0090163; P:establishment of epithelial cell planar polarity; IMP:FlyBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:FlyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:FlyBase.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:FlyBase.
DR GO; GO:0045196; P:establishment or maintenance of neuroblast polarity; IMP:FlyBase.
DR GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:FlyBase.
DR GO; GO:0016334; P:establishment or maintenance of polarity of follicular epithelium; IMP:FlyBase.
DR GO; GO:0051601; P:exocyst localization; IMP:FlyBase.
DR GO; GO:0007294; P:germarium-derived oocyte fate determination; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:FlyBase.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0007613; P:memory; IMP:FlyBase.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; TAS:FlyBase.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0140591; P:nuclear envelope budding; IMP:FlyBase.
DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; IGI:FlyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:FlyBase.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:FlyBase.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:1904580; P:regulation of intracellular mRNA localization; IMP:FlyBase.
DR GO; GO:0030860; P:regulation of polarized epithelial cell differentiation; IMP:FlyBase.
DR GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0007416; P:synapse assembly; IMP:FlyBase.
DR GO; GO:0007430; P:terminal branching, open tracheal system; IMP:FlyBase.
DR GO; GO:0045186; P:zonula adherens assembly; TAS:FlyBase.
DR CDD; cd00029; C1; 1.
DR CDD; cd06404; PB1_aPKC; 1.
DR CDD; cd05588; STKc_aPKC; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR034659; Atypical_PKC.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR034877; PB1_aPKC.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR012233; PKC.
DR InterPro; IPR017892; Pkinase_C.
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; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000554; PKC_zeta; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS51745; PB1; 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; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Kinase;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..606
FT /note="Atypical protein kinase C"
FT /id="PRO_0000430488"
FT DOMAIN 30..113
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 264..532
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 533..604
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 145..195
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 270..278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 293
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000303|PubMed:12537572"
FT /id="VSP_056764"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform B and isoform E)"
FT /evidence="ECO:0000303|PubMed:12537572"
FT /id="VSP_056765"
FT VAR_SEQ 83..110
FT /note="CTISTKMELDEAIRLYEMNFDSQLVIHV -> MIIWSGFCEAAQIYSTQTAT
FT FMSGGASL (in isoform B and isoform E)"
FT /evidence="ECO:0000303|PubMed:12537572"
FT /id="VSP_056766"
FT VAR_SEQ 104..110
FT /note="SQLVIHV -> MGKLACL (in isoform F)"
FT /evidence="ECO:0000303|PubMed:12537572"
FT /id="VSP_056767"
FT VAR_SEQ 540..578
FT /note="LERKQVTPPFKPRLDSDRDLANFPPEFTGEAVQLTPDDD -> IAQKEVQPP
FT YIPNIDTGDPYVTSNFDVQFTQEPAVLTPDDP (in isoform B and isoform
FT D)"
FT /evidence="ECO:0000303|PubMed:12537572"
FT /id="VSP_056768"
FT CONFLICT 16
FT /note="S -> T (in Ref. 1; AAG01528)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="N -> S (in Ref. 1; AAG01528)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="N -> K (in Ref. 5; AAM48431)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 606 AA; 69556 MW; 5C2E3046DBA61AEA CRC64;
MQKMPSQILN DGSSVSLNSA SMNMANTPNS ITVKTAYNGQ IIITTINKNI SYEELCYEIR
NICRFPLDQP FTIKWVDEEN DPCTISTKME LDEAIRLYEM NFDSQLVIHV FPNVPQAPGL
SCDGEDRSIY RRGARRWRKL YRVNGHIFQA KRFNRRAFCA YCQDRIWGLG RQGFKCIQCK
LLVHKKCHKL VQKHCTDQPE PLVKERAEES SDPIPVPLPP LPYEAMSGGA EACETHDHAH
IVAPPPPEDP LEPGTQRQYS LNDFELIRVI GRGSYAKVLM VELRRTRRIY AMKVIKKALV
TDDEDIDWVQ TEKHVFETAS NHPFLVGLHS CFQTPSRLFF VIEFVRGGDL MYHMQRQRRL
PEEHARFYAA EISLALNFLH EKGIIYRDLK LDNVLLDHEG HIKLTDYGMC KEGIRPGDTT
STFCGTPNYI APEILRGEDY GFSVDWWALG VLLYEMLAGR SPFDLAGASE NPDQNTEDYL
FQVILEKTIR IPRSLSVRAA SVLKGFLNKN PADRLGCHRE SAFMDIVSHP FFKNMDWELL
ERKQVTPPFK PRLDSDRDLA NFPPEFTGEA VQLTPDDDHV IDNIDQSEFE GFEYVNPLLM
SLEDCV
