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cGMP-dependent protein kinase, isozyme 1 (cGK) (EC 2.7.11.12)

 KGP1_DROME              Reviewed;         768 AA.
Q03042; Q24566; Q9V403;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
02-NOV-2001, sequence version 2.
28-FEB-2018, entry version 164.
RecName: Full=cGMP-dependent protein kinase, isozyme 1;
Short=cGK;
EC=2.7.11.12;
Name=Pkg21D; Synonyms=DG1; ORFNames=CG3324;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
TISSUE=Larva;
PubMed=2732245;
Kalderon D., Rubin G.M.;
"cGMP-dependent protein kinase genes in Drosophila.";
J. Biol. Chem. 264:10738-10748(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AUTOPHOSPHORYLATION,
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=8798533; DOI=10.1074/jbc.271.38.23322;
Foster J.L., Higgins G.C., Jackson F.R.;
"Biochemical properties and cellular localization of the Drosophila
DG1 cGMP-dependent protein kinase.";
J. Biol. Chem. 271:23322-23328(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
NUCLEOTIDE SEQUENCE OF 172-644.
PubMed=2828348;
Foster J.L., Higgins G.C., Jackson R.F.;
"Cloning, sequence, and expression of the Drosophila cAMP-dependent
protein kinase catalytic subunit gene.";
J. Biol. Chem. 263:1676-1681(1988).
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Binding of cGMP results in enzyme activation.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8798533}.
-!- TISSUE SPECIFICITY: In embryo stage 13, expression is seen in a
few large, irregular cells having the appearance of hemocytes or
macrophages. In adults, expression is seen in optic lamina and
weakly in testis. {ECO:0000269|PubMed:8798533}.
-!- DEVELOPMENTAL STAGE: Highest expression is in embryos, low level
expression is seen through rest of development.
{ECO:0000269|PubMed:2732245, ECO:0000269|PubMed:8798533}.
-!- PTM: Autophosphorylated.
-!- MISCELLANEOUS: cGMP-dependent protein kinase 1 consists of 3 types
of domains: the regulatory domain, two cGMP-binding regions and
the catalytic domain. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. cGMP subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M27114; AAA28453.1; -; Genomic_DNA.
EMBL; M27113; AAA28453.1; JOINED; Genomic_DNA.
EMBL; U59901; AAB03405.1; -; mRNA.
EMBL; AE014134; AAF51459.1; -; Genomic_DNA.
EMBL; AY058288; AAL13517.1; -; mRNA.
PIR; A34106; A34106.
RefSeq; NP_477213.1; NM_057865.4.
UniGene; Dm.4323; -.
ProteinModelPortal; Q03042; -.
SMR; Q03042; -.
IntAct; Q03042; 2.
STRING; 7227.FBpp0077706; -.
PaxDb; Q03042; -.
PRIDE; Q03042; -.
EnsemblMetazoa; FBtr0078042; FBpp0077706; FBgn0000442.
GeneID; 33253; -.
KEGG; dme:Dmel_CG3324; -.
CTD; 33253; -.
FlyBase; FBgn0000442; Pkg21D.
eggNOG; KOG0616; Eukaryota.
eggNOG; ENOG410XPQQ; LUCA.
GeneTree; ENSGT00810000125385; -.
HOGENOM; HOG000264194; -.
InParanoid; Q03042; -.
KO; K07376; -.
OMA; RQQEHIF; -.
OrthoDB; EOG091G0S9R; -.
PhylomeDB; Q03042; -.
BRENDA; 2.7.11.12; 1994.
Reactome; R-DME-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
SignaLink; Q03042; -.
GenomeRNAi; 33253; -.
PRO; PR:Q03042; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0000442; -.
Genevisible; Q03042; DM.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
GO; GO:0004692; F:cGMP-dependent protein kinase activity; IDA:FlyBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; NAS:FlyBase.
GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
CDD; cd00038; CAP_ED; 2.
CDD; cd05572; STKc_cGK; 1.
Gene3D; 2.60.120.10; -; 2.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR002374; cGMP_dep_kinase.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR018488; cNMP-bd_CS.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR035014; STKc_cGK.
Pfam; PF00027; cNMP_binding; 2.
Pfam; PF00069; Pkinase; 1.
PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
PRINTS; PR00104; CGMPKINASE.
SMART; SM00100; cNMP; 2.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF51206; SSF51206; 2.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00888; CNMP_BINDING_1; 1.
PROSITE; PS00889; CNMP_BINDING_2; 2.
PROSITE; PS50042; CNMP_BINDING_3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; cGMP; cGMP-binding; Complete proteome; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 768 cGMP-dependent protein kinase, isozyme 1.
/FTId=PRO_0000086120.
DOMAIN 457 717 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 718 768 AGC-kinase C-terminal.
NP_BIND 249 252 cAMP or cGMP 1.
{ECO:0000250|UniProtKB:Q13976}.
NP_BIND 259 260 cAMP or cGMP 1.
{ECO:0000250|UniProtKB:Q13976}.
NP_BIND 375 378 cAMP or cGMP 2.
{ECO:0000250|UniProtKB:Q13976}.
NP_BIND 385 386 cAMP or cGMP 2.
{ECO:0000250|UniProtKB:Q13976}.
NP_BIND 463 471 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 192 Regulatory. {ECO:0000250}.
ACT_SITE 582 582 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 366 366 cGMP 2. {ECO:0000250|UniProtKB:Q13976}.
BINDING 421 421 cAMP or cGMP 2.
{ECO:0000250|UniProtKB:Q13976}.
BINDING 488 488 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CONFLICT 235 235 Q -> H (in Ref. 2; AAB03405).
{ECO:0000305}.
CONFLICT 434 434 Q -> R (in Ref. 2; AAB03405).
{ECO:0000305}.
CONFLICT 438 438 R -> Q (in Ref. 2; AAB03405).
{ECO:0000305}.
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


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