KAPC2_DROME
ID KAPC2_DROME Reviewed; 354 AA.
AC P16911; P16910; Q53XD8; Q8IMH7;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=cAMP-dependent protein kinase catalytic subunit 2 {ECO:0000305};
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase DC1 {ECO:0000303|PubMed:3215511};
GN Name=Pka-C2; Synonyms=DC1; ORFNames=CG12066;
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 [GENOMIC DNA].
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.
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].
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- TISSUE SPECIFICITY: More abundant in adult body than adult head.
CC -!- DEVELOPMENTAL STAGE: In embryos, pupae and adults.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA34834.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X16960; CAA34833.1; -; Genomic_DNA.
DR EMBL; X16960; CAA34834.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014297; AAN14254.2; -; Genomic_DNA.
DR EMBL; BT012339; AAS77464.1; -; mRNA.
DR PIR; D31751; D31751.
DR RefSeq; NP_733397.2; NM_170518.4.
DR AlphaFoldDB; P16911; -.
DR SMR; P16911; -.
DR BioGRID; 68495; 1.
DR STRING; 7227.FBpp0085089; -.
DR PaxDb; P16911; -.
DR PRIDE; P16911; -.
DR DNASU; 43644; -.
DR EnsemblMetazoa; FBtr0085727; FBpp0085089; FBgn0000274.
DR GeneID; 43644; -.
DR KEGG; dme:Dmel_CG12066; -.
DR CTD; 43644; -.
DR FlyBase; FBgn0000274; Pka-C2.
DR VEuPathDB; VectorBase:FBgn0000274; -.
DR eggNOG; KOG0616; Eukaryota.
DR GeneTree; ENSGT00940000172108; -.
DR InParanoid; P16911; -.
DR OMA; KGHPWFQ; -.
DR OrthoDB; 963519at2759; -.
DR PhylomeDB; P16911; -.
DR BRENDA; 2.7.11.1; 1994.
DR Reactome; R-DME-163615; PKA activation.
DR Reactome; R-DME-164378; PKA activation in glucagon signalling.
DR Reactome; R-DME-180024; DARPP-32 events.
DR Reactome; R-DME-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-DME-392517; Rap1 signalling.
DR Reactome; R-DME-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-DME-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-DME-5610787; Hedgehog 'off' state.
DR Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DME-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DME-9634597; GPER1 signaling.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 43644; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43644; -.
DR PRO; PR:P16911; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0000274; Expressed in testis and 10 other tissues.
DR ExpressionAtlas; P16911; baseline and differential.
DR Genevisible; Q53XD8; DM.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISS:FlyBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; ISS:FlyBase.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISS:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:FlyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:FlyBase.
DR GO; GO:0010737; P:protein kinase A signaling; 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 ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..354
FT /note="cAMP-dependent protein kinase catalytic subunit 2"
FT /id="PRO_0000086111"
FT DOMAIN 45..301
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 302..354
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 51..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 354 AA; 41468 MW; 4E7AEF98C7C662D9 CRC64;
MSQHTSQYVF NSKEDYNVIL DNMSREFEER WNHQTQSPYT NLENYITRAV LGNGSFGTVM
LVREKSGKNY YAAKMMSKED LVRLKQVAHV HNEKHVLNAA RFPFLIYLVD STKCFDYLYL
ILPLVNGGEL FSYHRRVRKF NEKHARFYAA QVALALEYMH KMHLMYRDLK PENILLDQRG
YIKITDFGFT KRVDGRTSTL CGTPEYLAPE IVQLRPYNKS VDWWAFGILV YEFVAGRSPF
AIHNRDVILM YSKICICDYK MPSYFTSQLR SLVESLMQVD TSKRLGNSND GSSDVKSHPW
FQGVDWFGIL NQEVTAPYQP TISGAEDLSN FENFEFKDRY KSRINRHPEL FANF
