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P13678 (KPC3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein kinase C

Short name=PKC
EC=2.7.11.13
Alternative name(s):
dPKC98F
Gene names
Name:Pkc98E
Synonyms:Pkc3
ORF Names:CG1954
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length634 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Miscellaneous

This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.

Contains 1 AGC-kinase C-terminal domain.

Contains 2 phorbol-ester/DAG-type zinc fingers.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAF56846.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 634634Protein kinase C
PRO_0000055732

Regions

Domain303 – 560258Protein kinase
Domain561 – 63272AGC-kinase C-terminal
Zinc finger71 – 12151Phorbol-ester/DAG-type 1
Zinc finger146 – 19651Phorbol-ester/DAG-type 2
Nucleotide binding309 – 3179ATP By similarity

Sites

Active site4271Proton acceptor By similarity
Binding site3321ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P13678 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 3AE3A3D6B7A276BA

FASTA63471,157
        10         20         30         40         50         60 
MQSETAVQDL WVNLEPQGKI HVIIELKNRT DKAKAEAVVE HTVAVNKEFK ERAGFNRRRG 

        70         80         90        100        110        120 
AMRRRVHQVN GHKFMATFLR QPTFCSHCRE FIWGIGKQGY QCQVCTLVVH KKCHLSVVSK 

       130        140        150        160        170        180 
CPGMRDEQPA KVEMVPAGQR FNVNLPHRFV VHSYKRFTFC DHCGSLLYGL IKQGLQCETC 

       190        200        210        220        230        240 
GMNVHKRCQK NVANTCGINT KQMAEILSSL GISPDKQQPR RSKYLNQQGG EDNYGASLGA 

       250        260        270        280        290        300 
DGDGAPGQSF RSCALSVDSL ATSTTTMTSG YNSSSCMSLA VTGSGGVGAT GETRPGKCSL 

       310        320        330        340        350        360 
LDFNFIKVLG KGSFGKVMLA EKKGTDEIYA IKVLKKDAII QDDDVDCTMT EKRILALAAN 

       370        380        390        400        410        420 
HPFLTALHSC FQTPDRLFFV MEYVNGGDLM FQIQKARRFE ASRAAFYAAE VTLALQFLHT 

       430        440        450        460        470        480 
HGVIYRDLKL DNILLDQEGH CKLADFGMCK EGIMNGMLTT TFCGTPDYIA PEILKEQEYG 

       490        500        510        520        530        540 
ASVDWWALGV LMYEMMAGQP PFEADNEDEL FDSIMHDDVL YPVWLSREAV SILKGFLTKN 

       550        560        570        580        590        600 
PEQRLGCTGD ENEIRKHPFF AKLDWKELEK RNIKPPFRPK MKNPRDANNF DAEFTKEDPV 

       610        620        630 
LTPIGNEVVR CINQDEFAGF SFVNPKFGPE RKVY 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of two new Drosophila protein kinase C genes, including one specifically expressed in photoreceptor cells."
Schaeffer E., Smith D., Mardon G., Quinn W., Zuker C.
Cell 57:403-412(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04848 mRNA. Translation: AAA28818.1.
AE014297 Genomic DNA. Translation: AAF56846.1. Different initiation.
PIRB32392.
RefSeqNP_524545.2. NM_079821.3.
UniGeneDm.4053.

3D structure databases

ProteinModelPortalP13678.
SMRP13678. Positions 70-196, 302-625.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid68299. 16 interactions.
IntActP13678. 1 interaction.
MINTMINT-155042.

Proteomic databases

PaxDbP13678.
PRIDEP13678.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID43428.
KEGGdme:Dmel_CG1954.

Organism-specific databases

CTD43428.
FlyBaseFBgn0003093. Pkc98E.

Phylogenomic databases

eggNOGCOG0515.
InParanoidP13678.
KOK18050.
OrthoDBEOG77M8QM.
PhylomeDBP13678.

Enzyme and pathway databases

BRENDA2.7.11.13. 1994.
SignaLinkP13678.

Gene expression databases

BgeeP13678.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR020454. DAG/PE-bd.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR014376. Prot_kin_PKC_delta.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00130. C1_1. 2 hits.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000551. PKC_delta. 1 hit.
PRINTSPR00008. DAGPEDOMAIN.
SMARTSM00109. C1. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPkc98E. drosophila.
GenomeRNAi43428.
NextBio833872.

Entry information

Entry nameKPC3_DROME
AccessionPrimary (citable) accession number: P13678
Secondary accession number(s): Q9VAQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase