P12370 (KAPC_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
cAMP-dependent protein kinase catalytic subunit
Short name=PKA C
EC=2.7.11.11

Gene names

Name:	Pka-C1
Synonyms:	CdkA, DC0
ORF Names:	CG4379

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by cAMP.
Subunit structure	Composed of two regulatory chains and two catalytic chains.
Tissue specificity	More abundant in adult head than adult body.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. cAMP subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding cAMP
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anesthesia-resistant memory Inferred from mutant phenotype PubMed 19075226. Source: FlyBase anterior/posterior pattern specification, imaginal disc Inferred from mutant phenotype PubMed 7867062. Source: FlyBase behavioral response to ethanol Non-traceable author statement PubMed 11715043. Source: FlyBase cAMP-mediated signaling Non-traceable author statement PubMed 11462211PubMed 11741030PubMed 14515157. Source: FlyBase compound eye development Non-traceable author statement PubMed 11715043. Source: FlyBase imaginal disc-derived leg morphogenesis Non-traceable author statement PubMed 11715043. Source: FlyBase imaginal disc-derived wing morphogenesis Inferred from mutant phenotype PubMed 7867062. Source: FlyBase locomotor rhythm Non-traceable author statement PubMed 11715043. Source: FlyBase negative regulation of smoothened signaling pathway Inferred from genetic interaction PubMed 9874371. Source: FlyBase olfactory learning Non-traceable author statement PubMed 11462211. Source: FlyBase oocyte anterior/posterior axis specification Inferred from mutant phenotype PubMed 16291786PubMed 7528157. Source: FlyBase oocyte microtubule cytoskeleton polarization Inferred from mutant phenotype PubMed 7528157. Source: FlyBase positive regulation of hh target transcription factor activity Inferred from mutant phenotype PubMed 10862750. Source: FlyBase regulation of bicoid mRNA localization Inferred from mutant phenotype PubMed 7528157. Source: FlyBase regulation of circadian sleep/wake cycle, sleep Inferred from mutant phenotype PubMed 16753559. Source: FlyBase regulation of pole plasm oskar mRNA localization Inferred from mutant phenotype PubMed 7528157. Source: FlyBase regulation of synaptic transmission Inferred from mutant phenotype PubMed 11287463. Source: FlyBase
Cellular_component	cAMP-dependent protein kinase complex Inferred from sequence or structural similarity Ref.2. Source: FlyBase plasma membrane Inferred from direct assay PubMed 20462449PubMed 7734392. Source: FlyBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cAMP-dependent protein kinase activity Inferred from sequence or structural similarity Ref.2. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
slo	Q03720	5	EBI-82224,EBI-426805

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 353	352	cAMP-dependent protein kinase catalytic subunit		PRO_0000086069
Regions
	Domain	46 – 300	255	Protein kinase
	Domain	301 – 353	53	AGC-kinase C-terminal
	Nucleotide binding	52 – 60	9	ATP By similarity
Sites
	Active site	169	1	Proton acceptor By similarity
	Binding site	75	1	ATP By similarity
Amino acid modifications
	Lipidation	2	1	N-myristoyl glycine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P12370 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 9611D1001C791874	FASTA	353	40,839
	10 20 30 40 50 60 MGNNATTSNK KVDAAETVKE FLEQAKEEFE DKWRRNPTNT AALDDFERIK TLGTGSFGRV 70 80 90 100 110 120 MIVQHKPTKD YYAMKILDKQ KVVKLKQVEH TLNEKRILQA IQFPFLVSLR YHFKDNSNLY 130 140 150 160 170 180 MVLEYVPGGE MFSHLRKVGR FSEPHSRFYA AQIVLAFEYL HYLDLIYRDL KPENLLIDSQ 190 200 210 220 230 240 GYLKVTDFGF AKRVKGRTWT LCGTPEYLAP EIILSKGYNK AVDWWALGVL VYEMAAGYPP 250 260 270 280 290 300 FFADQPIQIY EKIVSGKVRF PSHFGSDLKD LLRNLLQVDL TKRYGNLKAG VNDIKNQKWF 310 320 330 340 350 ASTDWIAIFQ KKIEAPFIPR CKGPGDTSNF DDYEEEALRI SSTEKCAKEF AEF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, sequence, and expression of the Drosophila cAMP-dependent protein kinase catalytic subunit gene." Foster J.L., Higgins G.C., Jackson R.F. J. Biol. Chem. 263:1676-1681(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Isolation and characterization of Drosophila cAMP-dependent protein kinase genes." Kalderon D., Rubin G.M. Genes Dev. 2:1539-1556(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Canton-S.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M18655 Genomic DNA. Translation: AAA28412.1. X16969 Genomic DNA. Translation: CAA34840.1. AE014134 Genomic DNA. Translation: AAF52797.1. AE014134 Genomic DNA. Translation: AAN10703.1. AE014134 Genomic DNA. Translation: AAS64669.1. AY069425 mRNA. Translation: AAL39570.1.
PIR	C31751.
RefSeq	NP_476977.1. NM_057629.4. NP_723479.1. NM_164866.3. NP_995672.1. NM_205950.3.
UniGene	Dm.2136.
3D structure databases
ProteinModelPortal	P12370.
SMR	P12370. Positions 18-353.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-23727N.
IntAct	P12370. 3 interactions.
MINT	MINT-1019424.
STRING	7227.FBpp0079447.
Proteomic databases
PaxDb	P12370.
PRIDE	P12370.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0079851; FBpp0079448; FBgn0000273. FBtr0079852; FBpp0089382; FBgn0000273.
GeneID	34284.
KEGG	dme:Dmel_CG4379.
UCSC	CG4379-RB. d. melanogaster.
Organism-specific databases
CTD	34284.
FlyBase	FBgn0000273. Pka-C1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00550000074358.
InParanoid	P12370.
KO	K04345.
OMA	LENESHH.
OrthoDB	EOG469P9J.
PhylomeDB	P12370.
Enzyme and pathway databases
BRENDA	2.7.11.11. 1994.
SignaLink	P12370.
Gene expression databases
Bgee	P12370.
GermOnline	CG4379. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	34284.
NextBio	787747.

Entry information

Entry name

KAPC_DROME

Accession

Primary (citable) accession number: P12370
Secondary accession number(s): A4V0I0, Q9VL99

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project