Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

cGMP-dependent protein kinase, isozyme 1

Gene

Pkg21D

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Binding of cGMP results in enzyme activation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei488 – 4881ATPPROSITE-ProRule annotation
Active sitei582 – 5821Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 301117cGMP 1Add
BLAST
Nucleotide bindingi304 – 427124cGMP 2Add
BLAST
Nucleotide bindingi463 – 4719ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cGMP binding Source: UniProtKB-KW
  • cGMP-dependent protein kinase activity Source: FlyBase
  • cyclic nucleotide binding Source: FlyBase
  • protein serine/threonine kinase activity Source: FlyBase

GO - Biological processi

  • larval somatic muscle development Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, cGMP, cGMP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.12. 1994.
ReactomeiR-DME-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
SignaLinkiQ03042.

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-dependent protein kinase, isozyme 1 (EC:2.7.11.12)
Short name:
cGK
Gene namesi
Name:Pkg21D
Synonyms:DG1
ORF Names:CG3324
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000442. Pkg21D.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 768768cGMP-dependent protein kinase, isozyme 1PRO_0000086120Add
BLAST

Post-translational modificationi

Autophosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ03042.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

Highest expression is in embryos, low level expression is seen through rest of development.2 Publications

Gene expression databases

BgeeiQ03042.
GenevisibleiQ03042. DM.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiQ03042. 2 interactions.
STRINGi7227.FBpp0077706.

Structurei

3D structure databases

ProteinModelPortaliQ03042.
SMRiQ03042. Positions 9-50, 142-750.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini457 – 717261Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini718 – 76851AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 192192RegulatoryBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0616. Eukaryota.
ENOG410XPQQ. LUCA.
GeneTreeiENSGT00810000125385.
HOGENOMiHOG000264194.
InParanoidiQ03042.
KOiK07376.
OMAiWIVKLYK.
OrthoDBiEOG75B84Q.
PhylomeDBiQ03042.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR002374. cGMP_dep_kinase.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014710. RmlC-like_jellyroll.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000559. cGMP-dep_kinase. 1 hit.
PRINTSiPR00104. CGMPKINASE.
SMARTiSM00100. cNMP. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03042-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGMLTDRE REAIVSNLTK DVQALREMVR SRESELVKLH REIHKLKSVL
60 70 80 90 100
QQTTNNLNVT RNEKAKKKLY SLPEQCGEQE SRNQNPHLCS SCGMVLPTSP
110 120 130 140 150
EFALEALSLG PLSPLASTSS ASPSGRTSAD EVRPKAMPAA IKKQGVSAES
160 170 180 190 200
CVQSMQQSYS IPIPKYEKDF SDKQQIKDAI MDNDFLKNID ASQVRELVDS
210 220 230 240 250
MYSKSIAAGE FVIREGEVGA HLYVSAAGEF AVMQQGKVLD KMGAGKAFGE
260 270 280 290 300
LAILYNCTRT ASIRVLSEAA RVWVLDRRVF QQIMMCTGLQ RIENSVNFLR
310 320 330 340 350
SVPLLMNLSE ELLAKIADVL ELEFYAAGTY IIRQGTAGDS FFLISQGNVR
360 370 380 390 400
VTQKLTPTSP EETELRTLSR GDYFGEQALI NEDKRTANII ALSPGVECLT
410 420 430 440 450
LDRDSFKRLI GDLCELKEKD YGDESRKLAM KQAQESCRDE PKEQLQQEFP
460 470 480 490 500
DLKLTDLEVV STLGIGGFGR VELVKAHHQD RVDIFALKCL KKRHIVDTKQ
510 520 530 540 550
EEHIFSERHI MLSSRSPFIC RLYRTFRDEK YVYMLLEACM GGEIWTMLRD
560 570 580 590 600
RGSFEDNAAQ FIIGCVLQAF EYLHARGIIY RDLKPENLML DERGYVKIVD
610 620 630 640 650
FGFAKQIGTS SKTWTFCGTP EYVAPEIILN KGHDRAVDYW ALGILIHELL
660 670 680 690 700
NGTPPFSAPD PMQTYNLILK GIDMIAFPKH ISRWAVQLIK RLCRDVPSER
710 720 730 740 750
LGYQTGGIQD IKKHKWFLGF DWDGLASQLL IPPFVRPIAH PTDVRYFDRF
760
PCDLNEPPDE LSGWDADF
Length:768
Mass (Da):86,759
Last modified:November 2, 2001 - v2
Checksum:i36A97452319BE63C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2351Q → H in AAB03405 (PubMed:8798533).Curated
Sequence conflicti434 – 4341Q → R in AAB03405 (PubMed:8798533).Curated
Sequence conflicti438 – 4381R → Q in AAB03405 (PubMed:8798533).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27114, M27113 Genomic DNA. Translation: AAA28453.1.
U59901 mRNA. Translation: AAB03405.1.
AE014134 Genomic DNA. Translation: AAF51459.1.
AY058288 mRNA. Translation: AAL13517.1.
PIRiA34106.
RefSeqiNP_477213.1. NM_057865.4.
UniGeneiDm.4323.

Genome annotation databases

EnsemblMetazoaiFBtr0078042; FBpp0077706; FBgn0000442.
GeneIDi33253.
KEGGidme:Dmel_CG3324.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27114, M27113 Genomic DNA. Translation: AAA28453.1.
U59901 mRNA. Translation: AAB03405.1.
AE014134 Genomic DNA. Translation: AAF51459.1.
AY058288 mRNA. Translation: AAL13517.1.
PIRiA34106.
RefSeqiNP_477213.1. NM_057865.4.
UniGeneiDm.4323.

3D structure databases

ProteinModelPortaliQ03042.
SMRiQ03042. Positions 9-50, 142-750.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ03042. 2 interactions.
STRINGi7227.FBpp0077706.

Proteomic databases

PaxDbiQ03042.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078042; FBpp0077706; FBgn0000442.
GeneIDi33253.
KEGGidme:Dmel_CG3324.

Organism-specific databases

CTDi33253.
FlyBaseiFBgn0000442. Pkg21D.

Phylogenomic databases

eggNOGiKOG0616. Eukaryota.
ENOG410XPQQ. LUCA.
GeneTreeiENSGT00810000125385.
HOGENOMiHOG000264194.
InParanoidiQ03042.
KOiK07376.
OMAiWIVKLYK.
OrthoDBiEOG75B84Q.
PhylomeDBiQ03042.

Enzyme and pathway databases

BRENDAi2.7.11.12. 1994.
ReactomeiR-DME-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
SignaLinkiQ03042.

Miscellaneous databases

GenomeRNAii33253.
PROiQ03042.

Gene expression databases

BgeeiQ03042.
GenevisibleiQ03042. DM.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR002374. cGMP_dep_kinase.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014710. RmlC-like_jellyroll.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000559. cGMP-dep_kinase. 1 hit.
PRINTSiPR00104. CGMPKINASE.
SMARTiSM00100. cNMP. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00888. CNMP_BINDING_1. 1 hit.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cGMP-dependent protein kinase genes in Drosophila."
    Kalderon D., Rubin G.M.
    J. Biol. Chem. 264:10738-10748(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE.
    Tissue: Larva.
  2. "Biochemical properties and cellular localization of the Drosophila DG1 cGMP-dependent protein kinase."
    Foster J.L., Higgins G.C., Jackson F.R.
    J. Biol. Chem. 271:23322-23328(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    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.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  6. "Cloning, sequence, and expression of the Drosophila cAMP-dependent protein kinase catalytic subunit gene."
    Foster J.L., Higgins G.C., Jackson R.F.
    J. Biol. Chem. 263:1676-1681(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 172-644.

Entry informationi

Entry nameiKGP1_DROME
AccessioniPrimary (citable) accession number: Q03042
Secondary accession number(s): Q24566, Q9V403
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 2, 2001
Last modified: June 8, 2016
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

cGMP-dependent protein kinase 1 consists of 3 types of domains: the regulatory domain, two cGMP-binding regions and the catalytic domain.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.