KGP1_DROME
ID KGP1_DROME Reviewed; 768 AA.
AC Q03042; Q24566; Q9V403;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=cGMP-dependent protein kinase, isozyme 1;
DE Short=cGK;
DE EC=2.7.11.12;
GN Name=Pkg21D; Synonyms=DG1; ORFNames=CG3324;
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 DEVELOPMENTAL STAGE.
RC TISSUE=Larva;
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 [MRNA], FUNCTION, SUBUNIT, AUTOPHOSPHORYLATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8798533; DOI=10.1074/jbc.271.38.23322;
RA Foster J.L., Higgins G.C., Jackson F.R.;
RT "Biochemical properties and cellular localization of the Drosophila DG1
RT cGMP-dependent protein kinase.";
RL J. Biol. Chem. 271:23322-23328(1996).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=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).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 172-644.
RX PubMed=2828348; DOI=10.1016/s0021-9258(19)77929-0;
RA Foster J.L., Higgins G.C., Jackson R.F.;
RT "Cloning, sequence, and expression of the Drosophila cAMP-dependent protein
RT kinase catalytic subunit gene.";
RL J. Biol. Chem. 263:1676-1681(1988).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Binding of cGMP results in enzyme activation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8798533}.
CC -!- TISSUE SPECIFICITY: In embryo stage 13, expression is seen in a few
CC large, irregular cells having the appearance of hemocytes or
CC macrophages. In adults, expression is seen in optic lamina and weakly
CC in testis. {ECO:0000269|PubMed:8798533}.
CC -!- DEVELOPMENTAL STAGE: Highest expression is in embryos, low level
CC expression is seen through rest of development.
CC {ECO:0000269|PubMed:2732245, ECO:0000269|PubMed:8798533}.
CC -!- PTM: Autophosphorylated.
CC -!- MISCELLANEOUS: cGMP-dependent protein kinase 1 consists of 3 types of
CC domains: the regulatory domain, two cGMP-binding regions and the
CC catalytic domain. {ECO:0000250}.
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; M27114; AAA28453.1; -; Genomic_DNA.
DR EMBL; M27113; AAA28453.1; JOINED; Genomic_DNA.
DR EMBL; U59901; AAB03405.1; -; mRNA.
DR EMBL; AE014134; AAF51459.1; -; Genomic_DNA.
DR EMBL; AY058288; AAL13517.1; -; mRNA.
DR PIR; A34106; A34106.
DR RefSeq; NP_477213.1; NM_057865.4.
DR AlphaFoldDB; Q03042; -.
DR SMR; Q03042; -.
DR IntAct; Q03042; 2.
DR STRING; 7227.FBpp0077706; -.
DR PaxDb; Q03042; -.
DR PRIDE; Q03042; -.
DR EnsemblMetazoa; FBtr0078042; FBpp0077706; FBgn0000442.
DR GeneID; 33253; -.
DR KEGG; dme:Dmel_CG3324; -.
DR CTD; 33253; -.
DR FlyBase; FBgn0000442; Pkg21D.
DR VEuPathDB; VectorBase:FBgn0000442; -.
DR eggNOG; KOG0614; Eukaryota.
DR GeneTree; ENSGT00940000166710; -.
DR HOGENOM; CLU_000288_73_2_1; -.
DR InParanoid; Q03042; -.
DR OMA; WIVKLYK; -.
DR OrthoDB; 401933at2759; -.
DR PhylomeDB; Q03042; -.
DR BRENDA; 2.7.11.12; 1994.
DR BioGRID-ORCS; 33253; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33253; -.
DR PRO; PR:Q03042; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0000442; Expressed in adult Malpighian tubule (Drosophila) and 14 other tissues.
DR Genevisible; Q03042; DM.
DR GO; GO:0005737; C:cytoplasm; 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:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA: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 PIRSF; PIRSF000559; cGMP-dep_kinase; 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; 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 1: Evidence at protein level;
KW ATP-binding; cGMP; cGMP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..768
FT /note="cGMP-dependent protein kinase, isozyme 1"
FT /id="PRO_0000086120"
FT DOMAIN 457..717
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 718..768
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..192
FT /note="Regulatory"
FT /evidence="ECO:0000250"
FT REGION 114..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 582
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 249..252
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 259..260
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 366
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 375..378
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 385..386
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 421
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13976"
FT BINDING 463..471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 235
FT /note="Q -> H (in Ref. 2; AAB03405)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="Q -> R (in Ref. 2; AAB03405)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="R -> Q (in Ref. 2; AAB03405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 768 AA; 86759 MW; 36A97452319BE63C CRC64;
MAAGMLTDRE REAIVSNLTK DVQALREMVR SRESELVKLH REIHKLKSVL QQTTNNLNVT
RNEKAKKKLY SLPEQCGEQE SRNQNPHLCS SCGMVLPTSP EFALEALSLG PLSPLASTSS
ASPSGRTSAD EVRPKAMPAA IKKQGVSAES CVQSMQQSYS IPIPKYEKDF SDKQQIKDAI
MDNDFLKNID ASQVRELVDS MYSKSIAAGE FVIREGEVGA HLYVSAAGEF AVMQQGKVLD
KMGAGKAFGE LAILYNCTRT ASIRVLSEAA RVWVLDRRVF QQIMMCTGLQ RIENSVNFLR
SVPLLMNLSE ELLAKIADVL ELEFYAAGTY IIRQGTAGDS FFLISQGNVR VTQKLTPTSP
EETELRTLSR GDYFGEQALI NEDKRTANII ALSPGVECLT LDRDSFKRLI GDLCELKEKD
YGDESRKLAM KQAQESCRDE PKEQLQQEFP DLKLTDLEVV STLGIGGFGR VELVKAHHQD
RVDIFALKCL KKRHIVDTKQ EEHIFSERHI MLSSRSPFIC RLYRTFRDEK YVYMLLEACM
GGEIWTMLRD RGSFEDNAAQ FIIGCVLQAF EYLHARGIIY RDLKPENLML DERGYVKIVD
FGFAKQIGTS SKTWTFCGTP EYVAPEIILN KGHDRAVDYW ALGILIHELL NGTPPFSAPD
PMQTYNLILK GIDMIAFPKH ISRWAVQLIK RLCRDVPSER LGYQTGGIQD IKKHKWFLGF
DWDGLASQLL IPPFVRPIAH PTDVRYFDRF PCDLNEPPDE LSGWDADF
