KGP24_DROME
ID KGP24_DROME Reviewed; 1088 AA.
AC Q03043; A4V042; Q24304; Q9I7Q1; Q9VQT2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=cGMP-dependent protein kinase, isozyme 2 forms cD4/T1/T3A/T3B;
DE Short=cGK;
DE EC=2.7.11.12;
DE AltName: Full=Foraging protein;
GN Name=for; Synonyms=DG2, PGK2, Pkg24A; ORFNames=CG10033;
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 / MRNA] (ISOFORMS T1 AND T3B), AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Imaginal disk;
RX PubMed=2732245; DOI=10.1016/s0021-9258(18)81684-2;
RA Kalderon D., Rubin G.M.;
RT "cGMP-dependent protein kinase genes in Drosophila.";
RL J. Biol. Chem. 264:10738-10748(1989).
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] (ISOFORM T1).
RC STRAIN=Berkeley; TISSUE=Embryo;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-934 AND THR-938, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
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=2.7.11.12;
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=2.7.11.12;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=T1; Synonyms=A, H;
CC IsoId=Q03043-1; Sequence=Displayed;
CC Name=cD4;
CC IsoId=Q03043-4; Sequence=VSP_004763;
CC Name=T3A;
CC IsoId=Q03043-2; Sequence=VSP_004761;
CC Name=T3B; Synonyms=B;
CC IsoId=Q03043-3; Sequence=VSP_004762;
CC Name=cD5; Synonyms=E, J;
CC IsoId=P32023-1; Sequence=External;
CC Name=T2; Synonyms=C, D, G, T2a, T2b;
CC IsoId=P32023-2; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, high during
CC embryonic and adult stages. Isoform T1 is predominantly expressed
CC during embryo and adult stages. {ECO:0000269|PubMed:2732245}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cGMP subfamily. {ECO:0000305}.
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DR EMBL; M27120; AAA28455.1; -; Genomic_DNA.
DR EMBL; M27117; AAA28455.1; JOINED; Genomic_DNA.
DR EMBL; M27118; AAA28455.1; JOINED; Genomic_DNA.
DR EMBL; M27119; AAA28455.1; JOINED; Genomic_DNA.
DR EMBL; M30413; AAA28459.1; -; mRNA.
DR EMBL; AE014134; AAF51082.2; -; Genomic_DNA.
DR EMBL; AE014134; AAS64613.1; -; Genomic_DNA.
DR EMBL; AE014134; AAS64614.1; -; Genomic_DNA.
DR EMBL; AY061514; AAL29062.1; -; mRNA.
DR PIR; B34106; B34106.
DR RefSeq; NP_477487.1; NM_058139.4. [Q03043-1]
DR RefSeq; NP_995626.1; NM_205904.2. [Q03043-1]
DR RefSeq; NP_995628.1; NM_205906.2. [Q03043-1]
DR AlphaFoldDB; Q03043; -.
DR SMR; Q03043; -.
DR BioGRID; 69303; 13.
DR STRING; 7227.FBpp0088350; -.
DR iPTMnet; Q03043; -.
DR PaxDb; Q03043; -.
DR PRIDE; Q03043; -.
DR DNASU; 44817; -.
DR EnsemblMetazoa; FBtr0089304; FBpp0088350; FBgn0000721. [Q03043-1]
DR EnsemblMetazoa; FBtr0089310; FBpp0088922; FBgn0000721. [Q03043-1]
DR EnsemblMetazoa; FBtr0089312; FBpp0088923; FBgn0000721. [Q03043-1]
DR EnsemblMetazoa; FBtr0446099; FBpp0402801; FBgn0000721. [Q03043-3]
DR EnsemblMetazoa; FBtr0473363; FBpp0422967; FBgn0000721. [Q03043-4]
DR EnsemblMetazoa; FBtr0473364; FBpp0422968; FBgn0000721. [Q03043-4]
DR GeneID; 44817; -.
DR UCSC; CG10033-RA; d. melanogaster. [Q03043-1]
DR CTD; 44817; -.
DR FlyBase; FBgn0000721; for.
DR VEuPathDB; VectorBase:FBgn0000721; -.
DR eggNOG; KOG0614; Eukaryota.
DR eggNOG; KOG0616; Eukaryota.
DR HOGENOM; CLU_000288_73_6_1; -.
DR InParanoid; Q03043; -.
DR PhylomeDB; Q03043; -.
DR BRENDA; 2.7.11.12; 1994.
DR Reactome; R-DME-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-DME-392517; Rap1 signalling.
DR Reactome; R-DME-9648002; RAS processing.
DR BioGRID-ORCS; 44817; 0 hits in 3 CRISPR screens.
DR ChiTaRS; for; fly.
DR GenomeRNAi; 44817; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000721; Expressed in spermathecum and 64 other tissues.
DR ExpressionAtlas; Q03043; baseline and differential.
DR Genevisible; Q03043; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0007631; P:feeding behavior; TAS:FlyBase.
DR GO; GO:0046959; P:habituation; IMP:FlyBase.
DR GO; GO:0030536; P:larval feeding behavior; IMP:UniProtKB.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:FlyBase.
DR GO; GO:0032095; P:regulation of response to food; IMP:FlyBase.
DR GO; GO:0009744; P:response to sucrose; IDA:FlyBase.
DR GO; GO:0007614; P:short-term memory; IMP:FlyBase.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd05572; STKc_cGK; 1.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR002374; cGMP_dep_kinase.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR031831; PKcGMP_CC.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035014; STKc_cGK.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF16808; PKcGMP_CC; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00104; CGMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; cGMP; cGMP-binding; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1088
FT /note="cGMP-dependent protein kinase, isozyme 2 forms
FT cD4/T1/T3A/T3B"
FT /id="PRO_0000086121"
FT DOMAIN 777..1036
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1037..1088
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..69
FT /note="Dimerization"
FT /evidence="ECO:0000250"
FT REGION 15..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..528
FT /note="Regulatory"
FT /evidence="ECO:0000250"
FT REGION 128..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 901
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 584..587
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 594..595
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 699
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 708..711
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 718..719
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 783..791
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 807
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 934
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 938
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..520
FT /note="Missing (in isoform cD4)"
FT /evidence="ECO:0000305"
FT /id="VSP_004763"
FT VAR_SEQ 1..346
FT /note="Missing (in isoform T3B)"
FT /evidence="ECO:0000303|PubMed:2732245"
FT /id="VSP_004762"
FT VAR_SEQ 1..169
FT /note="Missing (in isoform T3A)"
FT /evidence="ECO:0000305"
FT /id="VSP_004761"
FT CONFLICT 49
FT /note="P -> T (in Ref. 1; AAA28455)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="S -> T (in Ref. 1; AAA28455)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="Y -> H (in Ref. 1; AAA28455/AAA28459)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="T -> R (in Ref. 1; AAA28455/AAA28459)"
FT /evidence="ECO:0000305"
FT CONFLICT 915
FT /note="V -> G (in Ref. 1; AAA28455/AAA28459)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1088 AA; 121341 MW; A9450E31FF7AB8BD CRC64;
MRFCFDRLCF ATKRPAQNSN SNAPHSSTTV DAPPRPADVD VATVPVATPA PPPQQPVSNL
FYADYQKLQP AIIDRDWERD RDTDTDTRSE AKPPDIVEHI EPVEEQRQIH TQIQSPAEIQ
IQIPPTPPAP SIQIQIQQRY RRHSSAEDRN LNTRRNDSNI TEALRKAASM QQEPNANYQF
PTDLGLVSIV NNNNNTNTHP SGSNSGSNNN SNINNNLVGG IVTLPAAGGL IGLEHTASGL
RLIPAPPTHS DVLTHTLIYG TPPSGAQQLN QDPRSLLHQQ ELQLQQRYQQ LQQLQAQTQG
LYTSQGSPVL YHQPSPGSSQ PVAIPGATCH SPTQLQPPNT LNLQQQMQSL RISGCTPSGT
GGSATPSPVG LVDPNFIVSN YVAASPQEER FIQIIQAKEL KIQEMQRALQ FKDNEIAELK
SHLDKFQSVF PFSRGSAAGC AGTGGASGSG AGGSGGSGPG TATGATRKSG QNFQRQRALG
ISAEPQSESS LLLEHVSFPK YDKDERSREL IKAAILDNDF MKNLDLTQIR EIVDCMYPVK
YPAKNLIIKE GDVGSIVYVM EDGRVEVSRE GKYLSTLSGA KVLGELAILY NCQRTATITA
ITECNLWAIE RQCFQTIMMR TGLIRQAEYS DFLKSVPIFK DLAEDTLIKI SDVLEETHYQ
RGDYIVRQGA RGDTFFIISK GKVRVTIKQQ DTQEEKFIRM LGKGDFFGEK ALQGDDLRTA
NIICESADGV SCLVIDRETF NQLISNLDEI KHRYDDEGAM ERRKINEEFR DINLTDLRVI
ATLGVGGFGR VELVQTNGDS SRSFALKQMK KSQIVETRQQ QHIMSEKEIM GEANCQFIVK
LFKTFKDKKY LYMLMESCLG GELWTILRDK GNFDDSTTRF YTACVVEAFD YLHSRNIIYR
DLKPENLLLN ERGYVKLVDF GFAKKLQTGR KTWTFCGTPE YVAPEVILNR GHDISADYWS
LGVLMFELLT GTPPFTGSDP MRTYNIILKG IDAIEFPRNI TRNASNLIKK LCRDNPAERL
GYQRGGISEI QKHKWFDGFY WWGLQNCTLE PPIKPAVKSV VDTTNFDDYP PDPEGPPPDD
VTGWDKDF
