ID KAPC_DROME STANDARD; PRT; 352 AA. AC P12370; Q9VL99; DT 01-OCT-1989 (Rel. 12, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT (EC 2.7.1.37) (PKA C). GN PKA-C1 OR CDKA OR DC0 OR CG4379. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88115281; PubMed=2828348; RA Foster J.L., Higgins G.C., Jackson R.F.; RT "Cloning, sequence, and expression of the Drosophila cAMP-dependent RT protein kinase catalytic subunit gene."; RL J. Biol. Chem. 263:1676-1681(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CANTON-S; RX MEDLINE=89107990; PubMed=3215511; RA Kalderon D., Rubin G.M.; RT "Isolation and characterization of Drosophila cAMP-dependent protein RT kinase genes."; RL Genes Dev. 2:1539-1556(1988). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; 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.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., 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.C., 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., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., 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). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- ENZYME REGULATION: THIS ENZYME IS ACTIVATED BY CAMP. CC -!- SUBUNIT: COMPOSED OF TWO REGULATORY CHAINS AND TWO CATALYTIC CC CHAINS. CC -!- TISSUE SPECIFICITY: MORE ABUNDANT IN ADULT HEAD THAN ADULT BODY. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CAMP SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M18655; AAA28412.1; -. DR EMBL; X16969; CAA34840.1; -. DR EMBL; AE003625; AAF52797.1; -. DR PIR; A28269; A28269. DR PIR; C31751; C31751. DR HSSP; P05132; 2CPK. DR FLYBASE; FBgn0000273; Pka-C1. DR INTERPRO; IPR000719; -. DR INTERPRO; IPR000961; -. DR INTERPRO; IPR002290; -. DR PFAM; PF00069; pkinase; 1. DR PFAM; PF00433; pkinase_C; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; cAMP; KW Phosphorylation; Myristate. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT DOMAIN 45 299 PROTEIN KINASE. FT NP_BIND 51 59 ATP (BY SIMILARITY). FT BINDING 74 74 ATP (BY SIMILARITY). FT ACT_SITE 168 168 BY SIMILARITY. SQ SEQUENCE 352 AA; 40707 MW; 88E42BCFA95E9640 CRC64; GNNATTSNKK VDAAETVKEF LEQAKEEFED KWRRNPTNTA ALDDFERIKT LGTGSFGRVM IVQHKPTKDY YAMKILDKQK VVKLKQVEHT LNEKRILQAI QFPFLVSLRY HFKDNSNLYM VLEYVPGGEM FSHLRKVGRF SEPHSRFYAA QIVLAFEYLH YLDLIYRDLK PENLLIDSQG YLKVTDFGFA KRVKGRTWTL CGTPEYLAPE IILSKGYNKA VDWWALGVLV YEMAAGYPPF FADQPIQIYE KIVSGKVRFP SHFGSDLKDL LRNLLQVDLT KRYGNLKAGV NDIKNQKWFA STDWIAIFQK KIEAPFIPRC KGPGDTSNFD DYEEEALRIS STEKCAKEFA EF //