ID   KGP25_DROME             Reviewed;         934 AA.
AC   P32023; A4V044; A4V046; Q0E8U1; Q24302; Q24303; Q9I7Q0; Q9I7Q2;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 3.
DT   02-SEP-2026, entry version 208.
DE   RecName: Full=cGMP-dependent protein kinase, isozyme 2 forms cD5/T2;
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; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS CD5 AND T2), 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 T2).
RC   STRAIN=Berkeley; TISSUE=Embryo, and Head;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.12;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=cD5; Synonyms=E, J;
CC         IsoId=P32023-1; Sequence=Displayed;
CC       Name=T2; Synonyms=C, D, G, T2a, T2b;
CC         IsoId=P32023-2; Sequence=VSP_004764;
CC       Name=cD4;
CC         IsoId=Q03043-4; Sequence=External;
CC       Name=T1; Synonyms=A, H;
CC         IsoId=Q03043-1; Sequence=External;
CC       Name=T3A;
CC         IsoId=Q03043-2; Sequence=External;
CC       Name=T3B; Synonyms=B;
CC         IsoId=Q03043-3; Sequence=External;
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development, high during
CC       embryonic and adult stages. Isoform T2 is predominantly expressed
CC       during larval 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M27124; AAA28457.1; -; Genomic_DNA.
DR   EMBL; M27122; AAA28457.1; JOINED; Genomic_DNA.
DR   EMBL; M27123; AAA28457.1; JOINED; Genomic_DNA.
DR   EMBL; M30147; AAA28456.1; -; mRNA.
DR   EMBL; M30148; AAA28458.1; -; mRNA.
DR   EMBL; M30149; AAA28454.1; -; mRNA.
DR   EMBL; AE014134; AAG22252.2; -; Genomic_DNA.
DR   EMBL; AE014134; AAG22254.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAS64616.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAX52650.1; -; Genomic_DNA.
DR   EMBL; AF132175; AAD34763.2; -; mRNA.
DR   EMBL; BT004881; AAO45237.1; -; mRNA.
DR   PIR; C34106; C34106.
DR   PIR; D34106; D34106.
DR   PIR; T08418; T08418.
DR   RefSeq; NP_001014464.1; NM_001014464.2. [P32023-1]
DR   RefSeq; NP_001162858.1; NM_001169387.2. [P32023-2]
DR   RefSeq; NP_477489.1; NM_058141.4. [P32023-2]
DR   RefSeq; NP_477490.1; NM_058142.4. [P32023-1]
DR   RefSeq; NP_599146.1; NM_134319.4. [P32023-2]
DR   RefSeq; NP_995629.1; NM_205907.2. [P32023-2]
DR   AlphaFoldDB; P32023; -.
DR   SMR; P32023; -.
DR   BioGRID; 69303; 14.
DR   DNASU; 44817; -.
DR   EnsemblMetazoa; FBtr0089306; FBpp0088352; FBgn0000721.
DR   EnsemblMetazoa; FBtr0100363; FBpp0099769; FBgn0000721.
DR   GeneID; 44817; -.
DR   KEGG; dme:Dmel_CG10033; -.
DR   UCSC; CG10033-RA; d. melanogaster. [P32023-1]
DR   AGR; FB:FBgn0000721; -.
DR   CTD; 44817; -.
DR   FlyBase; FBgn0000721; for.
DR   VEuPathDB; VectorBase:FBgn0000721; -.
DR   HOGENOM; CLU_013232_0_0_1; -.
DR   OrthoDB; 63267at2759; -.
DR   BRENDA; 2.7.11.12; 1994.
DR   BioGRID-ORCS; 44817; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 44817; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0000721; Expressed in spermathecum and 220 other cell types or tissues.
DR   ExpressionAtlas; P32023; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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: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   FunFam; 1.10.510.10:FF:000096; cGMP-dependent protein kinase; 1.
DR   FunFam; 2.60.120.10:FF:000064; cGMP-dependent protein kinase, isozyme; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR002374; cGMP_dep_kinase.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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   PANTHER; PTHR24353:SF111; -; 1.
DR   PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00104; CGMPKINASE.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
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   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; cGMP; cGMP-binding; Kinase;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..934
FT                   /note="cGMP-dependent protein kinase, isozyme 2 forms
FT                   cD5/T2"
FT                   /id="PRO_0000086122"
FT   DOMAIN          623..882
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          883..934
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   REGION          121..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          910..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..131
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..213
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        747
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         430..433
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13976"
FT   BINDING         440..441
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13976"
FT   BINDING         545
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13976"
FT   BINDING         554..557
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13976"
FT   BINDING         564..565
FT                   /ligand="3',5'-cyclic GMP"
FT                   /ligand_id="ChEBI:CHEBI:57746"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13976"
FT   BINDING         629..637
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         653
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   VAR_SEQ         368..407
FT                   /note="Missing (in isoform T2)"
FT                   /evidence="ECO:0000303|PubMed:2732245, ECO:0000303|Ref.4"
FT                   /id="VSP_004764"
FT   CONFLICT        66
FT                   /note="A -> V (in Ref. 1; AAA28454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        219
FT                   /note="Q -> H (in Ref. 1; AAA28456/AAA28457/AAA28458)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393
FT                   /note="N -> H (in Ref. 1; AAA28454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401
FT                   /note="N -> D (in Ref. 1; AAA28454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        404..406
FT                   /note="IFS -> NFF (in Ref. 1; AAA28454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464
FT                   /note="M -> L (in Ref. 1; AAA28454)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        510
FT                   /note="Y -> H (in Ref. 1; AAA28456/AAA28458)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        761
FT                   /note="V -> G (in Ref. 1;
FT                   AAA28454/AAA28456/AAA28457/AAA28458)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   934 AA;  105907 MW;  5087411147CD5CCA CRC64;
     MKIKHYPGKA VDASLSLEGS SAMGALYEAN WLRAANQPAA PATTGTKLSR QSSSAGSSFL
     IEGISALSKY QMTLENIRQL ELQSRDKRIA STIKELSGYR PSALQHHQQQ QMHNVWVAED
     QDQEHEELED ASEGKEKLAS IQEPPAVNHY VLDPTERPRV PRPRQQFSVK PPSLRRSQTM
     SQPPSYATLR SPPKIKENLS KSSSAYSTFS SAAEDSQDQV VICQQPQRLM APPPREPPPE
     PPKRVSKPLS RSQTSVQRYA TVRMPNQTTS FSRSVVRSRD STASQRRLSL EQAIEGLKLE
     GEKAVRQKSP QISPAASSNG SSKDLNGEGF CIPRPRLIVP VHTYARRRRT GNLKEQSSGG
     QEEEAEKGKG WKDFYVLSQD RHSSFYINRI GQNYDYDYPI NFNIFSPDGR VEVSREGKYL
     STLSGAKVLG ELAILYNCQR TATITAITEC NLWAIERQCF QTIMMRTGLI RQAEYSDFLK
     SVPIFKDLAE DTLIKISDVL EETHYQRGDY IVRQGARGDT FFIISKGKVR VTIKQQDTQE
     EKFIRMLGKG DFFGEKALQG DDLRTANIIC ESADGVSCLV IDRETFNQLI SNLDEIKHRY
     DDEGAMERRK INEEFRDINL TDLRVIATLG VGGFGRVELV QTNGDSSRSF ALKQMKKSQI
     VETRQQQHIM SEKEIMGEAN CQFIVKLFKT FKDKKYLYML MESCLGGELW TILRDKGNFD
     DSTTRFYTAC VVEAFDYLHS RNIIYRDLKP ENLLLNERGY VKLVDFGFAK KLQTGRKTWT
     FCGTPEYVAP EVILNRGHDI SADYWSLGVL MFELLTGTPP FTGSDPMRTY NIILKGIDAI
     EFPRNITRNA SNLIKKLCRD NPAERLGYQR GGISEIQKHK WFDGFYWWGL QNCTLEPPIK
     PAVKSVVDTT NFDDYPPDPE GPPPDDVTGW DKDF
//