ID Q4QQA3_DROME Unreviewed; 554 AA. AC Q4QQA3; DT 19-JUL-2005, integrated into UniProtKB/TrEMBL. DT 19-JUL-2005, sequence version 1. DT 23-MAY-2018, entry version 131. DE RecName: Full=Protein kinase C {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00929532}; DE EC=2.7.11.13 {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00929532}; GN Name=Pkc98E {ECO:0000313|EMBL:ACZ95061.1, GN ECO:0000313|FlyBase:FBgn0003093}; GN Synonyms=98F {ECO:0000313|EMBL:ACZ95061.1}, Dmel\CG1954 GN {ECO:0000313|EMBL:ACZ95061.1}, Dpkc3 {ECO:0000313|EMBL:ACZ95061.1}, GN dPKC98F {ECO:0000313|EMBL:ACZ95061.1}, Nc98F GN {ECO:0000313|EMBL:ACZ95061.1}, nPKC {ECO:0000313|EMBL:ACZ95061.1}, GN PK-C {ECO:0000313|EMBL:ACZ95061.1}, PKC {ECO:0000313|EMBL:ACZ95061.1}, GN PKC 98F {ECO:0000313|EMBL:ACZ95061.1}, PKC d98F GN {ECO:0000313|EMBL:ACZ95061.1}, PKC-98F {ECO:0000313|EMBL:ACZ95061.1}, GN Pkc3 {ECO:0000313|EMBL:ACZ95061.1}, PKC98C GN {ECO:0000313|EMBL:ACZ95061.1}, PKC98E {ECO:0000313|EMBL:ACZ95061.1}; GN ORFNames=CG1954 {ECO:0000313|EMBL:ACZ95061.1, GN ECO:0000313|FlyBase:FBgn0003093}, Dmel_CG1954 GN {ECO:0000313|EMBL:ACZ95061.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAY84913.1}; RN [1] {ECO:0000313|EMBL:ACZ95061.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., RA Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., RA Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., RA Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:ACZ95061.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:ACZ95061.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; 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., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:ACZ95061.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:ACZ95061.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:ACZ95061.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AAY84913.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berkeley {ECO:0000313|EMBL:AAY84913.1}; RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J., RA Park S., Wan K., Yu C., Celniker S.; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:ACZ95061.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., RA Yu C., Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:ACZ95061.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:ACZ95061.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [11] {ECO:0000313|EMBL:ACZ95061.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [12] {ECO:0000313|EMBL:ACZ95061.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00935732}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. PKC subfamily. CC {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00929254}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BT023513; AAY84913.1; -; mRNA. DR EMBL; AE014297; ACZ95061.1; -; Genomic_DNA. DR RefSeq; NP_001163767.1; NM_001170296.2. DR UniGene; Dm.4053; -. DR SMR; Q4QQA3; -. DR PRIDE; Q4QQA3; -. DR EnsemblMetazoa; FBtr0301516; FBpp0290731; FBgn0003093. DR GeneID; 43428; -. DR CTD; 43428; -. DR FlyBase; FBgn0003093; Pkc98E. DR eggNOG; KOG0694; Eukaryota. DR eggNOG; ENOG410XNPH; LUCA. DR GeneTree; ENSGT00820000126964; -. DR OrthoDB; EOG091G0QRS; -. DR ChiTaRS; Pkc98E; fly. DR GenomeRNAi; 43428; -. DR Proteomes; UP000000803; Chromosome 3R. DR Bgee; FBgn0003093; -. DR ExpressionAtlas; Q4QQA3; baseline and differential. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004697; F:protein kinase C activity; IEA:UniProtKB-EC. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR CDD; cd00029; C1; 1. DR CDD; cd05591; STKc_nPKC_epsilon; 1. DR InterPro; IPR000961; AGC-kinase_C. 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; 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; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 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; 1. DR PROSITE; PS50081; ZF_DAG_PE_2; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|PIRNR:PIRNR000551, KW ECO:0000256|PIRSR:PIRSR000551-51, ECO:0000256|SAAS:SAAS00593399}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Kinase {ECO:0000256|PIRNR:PIRNR000551, ECO:0000256|SAAS:SAAS00593820, KW ECO:0000313|EMBL:ACZ95061.1}; KW Metal-binding {ECO:0000256|SAAS:SAAS00515414}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000551, KW ECO:0000256|PIRSR:PIRSR000551-51, ECO:0000256|SAAS:SAAS00593601}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000551, KW ECO:0000256|SAAS:SAAS00593706}; KW Transferase {ECO:0000256|PIRNR:PIRNR000551, KW ECO:0000256|SAAS:SAAS00592725, ECO:0000313|EMBL:ACZ95061.1}; KW Zinc {ECO:0000256|SAAS:SAAS00515409}; KW Zinc-finger {ECO:0000256|SAAS:SAAS00732991}. FT DOMAIN 66 116 Phorbol-ester/DAG-type. FT {ECO:0000259|PROSITE:PS50081}. FT DOMAIN 223 480 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT DOMAIN 481 552 AGC-kinase C-terminal. FT {ECO:0000259|PROSITE:PS51285}. FT NP_BIND 229 237 ATP. {ECO:0000256|PIRSR:PIRSR000551-51}. FT ACT_SITE 347 347 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000551-50}. FT BINDING 252 252 ATP. {ECO:0000256|PIRSR:PIRSR000551-51}. SQ SEQUENCE 554 AA; 61583 MW; 3C0FBC95992E43F4 CRC64; MGTSSWPRFC VNPPSVRIAG SLSVCTLVVH KKCHLSVVSK CPGMRDEQPA KVEMVPAGQR FNVNLPHRFV VHSYKRFTFC DHCGSLLYGL IKQGLQCETC GMNVHKRCQK NVANTCGINT KQMAEILSSL GISPDKQQPR RSKYLNQQGG EDNYGASLGA DGDGAPGQSF RSCALSVDSL ATSTTTMTSG YNSSSCMSLA VTGSGGVGAT GETRPGKCSL LDFNFIKVLG KGSFGKVMLA EKKGTDEIYA IKVLKKDAII QDDDVDCTMT EKRILALAAN HPFLTALHSC FQTPDRLFFV MEYVNGGDLM FQIQKARRFE ASRAAFYAAE VTLALQFLHT HGVIYRDLKL DNILLDQEGH CKLADFGMCK EGIMNGMLTT TFCGTPDYIA PEILKEQEYG ASVDWWALGV LMYEMMAGQP PFEADNEDEL FDSIMHDDVL YPVWLSREAV SILKGFLTKN PEQRLGCTGD ENEIRKHPFF AKLDWKELEK RNIKPPFRPK MKNPRDANNF DAEFTKEDPV LTPIGNEVVR CINQDEFAGF SFVNPKFGPE RKVY //