ID KAPR1_DROME Reviewed; 376 AA.
AC P16905; A4V272; A4V277; Q59E10; Q8IGP3; Q8IPU2; Q8MR47; Q95TK7; Q9VPA6;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 27-MAR-2024, entry version 212.
DE RecName: Full=cAMP-dependent protein kinase type I regulatory subunit;
DE Short=DRI class I to class IV;
GN Name=Pka-R1; Synonyms=CdkR; ORFNames=CG3263;
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], AND ALTERNATIVE SPLICING (ISOFORMS 1; 2
RP AND 3).
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=Berkeley; TISSUE=Embryo, and Head;
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).
CC -!- SUBUNIT: Tetramer, composed of 2 regulatory (R) and 2 catalytic (C)
CC subunits. In the presence of cAMP it dissociates into 2 active
CC monomeric C subunits and an R dimer.
CC -!- INTERACTION:
CC P16905; Q9VRY7: Rsph3; NbExp=4; IntAct=EBI-263057, EBI-15108291;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=DRI-1, A, C, G, H, I, J;
CC IsoId=P16905-1; Sequence=Displayed;
CC Name=2; Synonyms=DRI-2, D;
CC IsoId=P16905-2; Sequence=VSP_002795;
CC Name=3; Synonyms=DRI-3-4, B, F;
CC IsoId=P16905-3; Sequence=VSP_002796;
CC Name=E;
CC IsoId=P16905-4; Sequence=VSP_036066;
CC -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC region of the catalytic chain but is not phosphorylated. The
CC physiological significance of phosphorylations by other kinases is
CC unclear.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN71433.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X16963; CAA34837.1; -; Genomic_DNA.
DR EMBL; X16964; CAA34837.1; JOINED; Genomic_DNA.
DR EMBL; X16970; CAA34841.1; -; Genomic_DNA.
DR EMBL; X16971; CAA34841.1; JOINED; Genomic_DNA.
DR EMBL; X16966; CAA34838.1; -; Genomic_DNA.
DR EMBL; X16968; CAA34839.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51649.3; -; Genomic_DNA.
DR EMBL; AE014296; AAG22179.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN12146.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN12147.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52761.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52762.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52763.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52764.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52765.1; -; Genomic_DNA.
DR EMBL; AE014296; AAX52766.1; -; Genomic_DNA.
DR EMBL; AY058709; AAL13938.1; -; mRNA.
DR EMBL; AY122131; AAM52643.1; -; mRNA.
DR EMBL; BT001678; AAN71433.1; ALT_FRAME; mRNA.
DR PIR; A31751; OKFF1R.
DR RefSeq; NP_001014593.1; NM_001014593.3. [P16905-1]
DR RefSeq; NP_001014594.1; NM_001014594.3. [P16905-1]
DR RefSeq; NP_001014595.1; NM_001014595.3. [P16905-1]
DR RefSeq; NP_001014596.1; NM_001014596.3. [P16905-1]
DR RefSeq; NP_001014597.1; NM_001014597.2. [P16905-3]
DR RefSeq; NP_001014598.1; NM_001014598.2. [P16905-4]
DR RefSeq; NP_001189145.1; NM_001202216.1.
DR RefSeq; NP_001189146.1; NM_001202217.1.
DR RefSeq; NP_001189147.1; NM_001202218.2.
DR RefSeq; NP_001189148.1; NM_001202219.2.
DR RefSeq; NP_001189149.1; NM_001202220.2.
DR RefSeq; NP_524189.2; NM_079465.4. [P16905-3]
DR RefSeq; NP_730573.2; NM_168875.4. [P16905-1]
DR RefSeq; NP_730574.2; NM_168876.6. [P16905-1]
DR RefSeq; NP_730576.1; NM_168877.2. [P16905-2]
DR AlphaFoldDB; P16905; -.
DR SMR; P16905; -.
DR BioGRID; 65562; 11.
DR DIP; DIP-23282N; -.
DR IntAct; P16905; 13.
DR STRING; 7227.FBpp0291777; -.
DR PaxDb; 7227-FBpp0291777; -.
DR DNASU; 40305; -.
DR EnsemblMetazoa; FBtr0299891; FBpp0289169; FBgn0259243. [P16905-1]
DR EnsemblMetazoa; FBtr0299892; FBpp0289170; FBgn0259243. [P16905-1]
DR EnsemblMetazoa; FBtr0300528; FBpp0289755; FBgn0259243. [P16905-1]
DR EnsemblMetazoa; FBtr0300529; FBpp0289756; FBgn0259243. [P16905-3]
DR EnsemblMetazoa; FBtr0300530; FBpp0289757; FBgn0259243. [P16905-1]
DR EnsemblMetazoa; FBtr0300531; FBpp0289758; FBgn0259243. [P16905-2]
DR EnsemblMetazoa; FBtr0300532; FBpp0289759; FBgn0259243. [P16905-4]
DR EnsemblMetazoa; FBtr0300533; FBpp0289760; FBgn0259243. [P16905-3]
DR EnsemblMetazoa; FBtr0300534; FBpp0289761; FBgn0259243. [P16905-1]
DR EnsemblMetazoa; FBtr0300535; FBpp0289762; FBgn0259243. [P16905-1]
DR GeneID; 40305; -.
DR KEGG; dme:Dmel_CG42341; -.
DR AGR; FB:FBgn0259243; -.
DR CTD; 40305; -.
DR FlyBase; FBgn0259243; Pka-R1.
DR VEuPathDB; VectorBase:FBgn0259243; -.
DR eggNOG; KOG1113; Eukaryota.
DR GeneTree; ENSGT00940000157513; -.
DR InParanoid; P16905; -.
DR OrthoDB; 55978at2759; -.
DR PhylomeDB; P16905; -.
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-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-5610787; Hedgehog 'off' state.
DR Reactome; R-DME-9634597; GPER1 signaling.
DR Reactome; R-DME-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 40305; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Pka-R1; fly.
DR GenomeRNAi; 40305; -.
DR PRO; PR:P16905; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0259243; Expressed in brain and 30 other cell types or tissues.
DR ExpressionAtlas; P16905; baseline and differential.
DR Genevisible; P16905; DM.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IMP:FlyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
DR GO; GO:0019933; P:cAMP-mediated signaling; NAS:FlyBase.
DR GO; GO:0007591; P:molting cycle, chitin-based cuticle; IMP:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
DR GO; GO:2000253; P:positive regulation of feeding behavior; IMP:FlyBase.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:FlyBase.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR GO; GO:0045471; P:response to ethanol; IDA:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; HMP:FlyBase.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd12097; DD_RI_PKA; 1.
DR Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR PANTHER; PTHR11635:SF126; CAMP-DEPENDENT PROTEIN KINASE TYPE I-BETA REGULATORY SUBUNIT; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 1.
DR PIRSF; PIRSF000548; PK_regulatory; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; cAMP; cAMP-binding; Disulfide bond;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..376
FT /note="cAMP-dependent protein kinase type I regulatory
FT subunit"
FT /id="PRO_0000205396"
FT REGION 1..131
FT /note="Dimerization and phosphorylation"
FT REGION 72..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 91..95
FT /note="Pseudophosphorylation motif"
FT BINDING 132..247
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 197
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 206
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 250..371
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 321
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 330
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT DISULFID 17
FT /note="Interchain (with C-38)"
FT /evidence="ECO:0000250"
FT DISULFID 38
FT /note="Interchain (with C-17)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_002796"
FT VAR_SEQ 1..58
FT /note="MSYMMAKTLEEQSLRECEHYIQTHGIQRVLKDCIVQLCVCRPENPVQFLRQY
FT FQKLER -> MPK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_002795"
FT VAR_SEQ 2..58
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_036066"
FT CONFLICT 303
FT /note="E -> EQ (in Ref. 1; CAA34837/CAA34838/CAA34839/
FT CAA34841)"
FT /evidence="ECO:0000305"
FT CONFLICT P16905-2:1..3
FT /note="MPK -> M (in Ref. 1; CAA34837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 42239 MW; F7B89D9C3EC313A5 CRC64;
MSYMMAKTLE EQSLRECEHY IQTHGIQRVL KDCIVQLCVC RPENPVQFLR QYFQKLEREQ
VKLDASRQVI SPDDCEDLSP MPQTAAPPVR RRGGISAEPV TEEDATNYVK KVVPKDYKTM
NALSKAIAKN VLFAHLDESE RSDIFDAMFP VNHIAGENII QQGDEGDNFY VIDVGEVDVF
VNSELVTTIS EGGSFGELAL IYGTPRAATV RAKTDVKLWG IDRDSYRRIL MGSTIRKRKM
YEEFLSRVSI LESLDKWERL TVADSLETCS FDDGETIVKQ GAAGDDFYII LEGCAVVLQQ
RSEGEDPAEV GRLGSSDYFG EIALLLDRPR AATVVARGPL KCVKLDRARF ERVLGPCADI
LKRNITQYNS FVSLSV
//
