KAPC3_DROME
ID KAPC3_DROME Reviewed; 583 AA.
AC P16912; Q86BP5; Q8MSN9; Q9VUV5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=cAMP-dependent protein kinase catalytic subunit 3 {ECO:0000305};
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase DC2 {ECO:0000303|PubMed:3215511};
GN Name=Pka-C3; Synonyms=DC2; ORFNames=CG6117;
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 [MRNA] (ISOFORM A).
RC STRAIN=Canton-S;
RX PubMed=3215511; DOI=10.1101/gad.2.12a.1539;
RA Kalderon D., Rubin G.M.;
RT "Isolation and characterization of Drosophila cAMP-dependent protein kinase
RT genes.";
RL Genes Dev. 2:1539-1556(1988).
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, AND ALTERNATIVE SPLICING.
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 B).
RC STRAIN=Berkeley; TISSUE=Testis;
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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8601490; DOI=10.1093/genetics/141.4.1507;
RA Melendez A., Li W., Kalderon D.;
RT "Activity, expression and function of a second Drosophila protein kinase A
RT catalytic subunit gene.";
RL Genetics 141:1507-1520(1995).
CC -!- FUNCTION: Does not have an essential role in development.
CC {ECO:0000269|PubMed:8601490}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=P16912-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P16912-2; Sequence=VSP_015105;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic mesoderm, and the optic
CC lamina, wing disk and leg disks of third instar larvae. More abundant
CC in adult head than adult body. {ECO:0000269|PubMed:8601490}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR EMBL; AE014296; AAF49568.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN11771.2; -; Genomic_DNA.
DR EMBL; AY118681; AAM50541.1; -; mRNA.
DR RefSeq; NP_524097.2; NM_079373.4. [P16912-2]
DR RefSeq; NP_730083.2; NM_168638.3. [P16912-1]
DR AlphaFoldDB; P16912; -.
DR SMR; P16912; -.
DR BioGRID; 65045; 6.
DR IntAct; P16912; 2.
DR STRING; 7227.FBpp0075283; -.
DR PaxDb; P16912; -.
DR EnsemblMetazoa; FBtr0075528; FBpp0075283; FBgn0000489. [P16912-1]
DR EnsemblMetazoa; FBtr0075529; FBpp0075284; FBgn0000489. [P16912-2]
DR GeneID; 39733; -.
DR KEGG; dme:Dmel_CG6117; -.
DR CTD; 39733; -.
DR FlyBase; FBgn0000489; Pka-C3.
DR VEuPathDB; VectorBase:FBgn0000489; -.
DR eggNOG; KOG0616; Eukaryota.
DR GeneTree; ENSGT00940000159832; -.
DR InParanoid; P16912; -.
DR OMA; LSDMWSA; -.
DR PhylomeDB; P16912; -.
DR BRENDA; 2.7.11.1; 1994.
DR SignaLink; P16912; -.
DR BioGRID-ORCS; 39733; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Pka-C3; fly.
DR GenomeRNAi; 39733; -.
DR PRO; PR:P16912; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000489; Expressed in adult hindgut (Drosophila) and 33 other tissues.
DR ExpressionAtlas; P16912; baseline and differential.
DR Genevisible; P16912; DM.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 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.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..583
FT /note="cAMP-dependent protein kinase catalytic subunit 3"
FT /id="PRO_0000086112"
FT DOMAIN 274..528
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 529..583
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 51..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..222
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 397
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 280..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:3215511"
FT /id="VSP_015105"
FT CONFLICT 122
FT /note="K -> KKK (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="N -> K (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="N -> D (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 65407 MW; DC52142F06F2625B CRC64;
MDLWHIFLER ILVACRVSAS VFANFGCGLY SSWKLICGDH DSASGLRAGL ATPTQRGKAT
GDNGTTGTPA RTIGKPQARI ATAMSTATCA RFCTPLSSGT AGSTSKLTTG NGSGNTMTSA
YKIPSNNSTT ANDSSNTETT FTFKLGRSNG RSSSNVASSE SSDPLESDYS EEDPEQEQQR
PDPATNSRSS STATTTTTSS ADHDNDVDEE DEEDDENEGE GNGRDADDAT HDSSESIEED
DGNETDDEED DDESEESSSV QTAKGVRKYH LDDYQIIKTV GTGTFGRVCL CRDRISEKYC
AMKILAMTEV IRLKQIEHVK NERNILREIR HPFVISLEWS TKDDSNLYMI FDYVCGGELF
TYLRNAGKFT SQTSNFYAAE IVSALEYLHS LQIVYRDLKP ENLLINRDGH LKITDFGFAK
KLRDRTWTLC GTPEYIAPEI IQSKGHNKAV DWWALGVLIY EMLVGYPPFY DEQPFGIYEK
ILSGKIEWER HMDPIAKDLI KKLLVNDRTK RLGNMKNGAD DVKRHRWFKH LNWNDVYSKK
LKPPILPDVH HDGDTKNFDD YPEKDWKPAK AVDQRDLQYF NDF
