KGP25_DROME
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 03-AUG-2022, entry version 195.
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; 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 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=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=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}.
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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; 13.
DR DNASU; 44817; -.
DR EnsemblMetazoa; FBtr0089306; FBpp0088352; FBgn0000721. [P32023-1]
DR EnsemblMetazoa; FBtr0089307; FBpp0088353; FBgn0000721. [P32023-2]
DR EnsemblMetazoa; FBtr0089308; FBpp0088354; FBgn0000721. [P32023-2]
DR EnsemblMetazoa; FBtr0089309; FBpp0088924; FBgn0000721. [P32023-2]
DR EnsemblMetazoa; FBtr0100363; FBpp0099769; FBgn0000721. [P32023-1]
DR EnsemblMetazoa; FBtr0301399; FBpp0290613; FBgn0000721. [P32023-2]
DR GeneID; 44817; -.
DR KEGG; dme:Dmel_CG10033; -.
DR UCSC; CG10033-RA; d. melanogaster. [P32023-1]
DR CTD; 44817; -.
DR FlyBase; FBgn0000721; for.
DR VEuPathDB; VectorBase:FBgn0000721; -.
DR HOGENOM; CLU_013232_0_0_1; -.
DR OMA; MHNGWVA; -.
DR BRENDA; 2.7.11.12; 1994.
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; P32023; baseline and differential.
DR Genevisible; P32023; DM.
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: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; 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; 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; SSF51206; 2.
DR SUPFAM; SSF56112; SSF56112; 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 170..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..325
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; AAA28454/AAA28456/AAA28457/
FT 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
