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Reviewed, UniProtKB/Swiss-Prot P05130 (KPC1_DROME)

Last modified June 16, 2009. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein kinase C, brain isozyme
      Short name=PKC
    EC=2.7.11.13
Alternative name(s):
    dPKC53E(BR)
Gene names
Name: Pkc53E
Synonyms: PKC1
ORF Names: CG6622
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length679 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Tissue specificity

Head neural tissue.

Miscellaneous

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

The sequence shown is that of Oregon-R.

Sequence similarities

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

Contains 1 AGC-kinase C-terminal domain.

Contains 1 C2 domain.

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

Contains 1 protein kinase domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P05130-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: P05130-2)

The sequence of this isoform differs from the canonical sequence as follows:
     67-77: CGYQSGYAWMG → WG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 679679Protein kinase C, brain isozyme
PRO_0000055730

Regions

Domain191 – 27888C2
Domain350 – 608259Protein kinase
Domain609 – 67971AGC-kinase C-terminal
Zinc finger45 – 10460Phorbol-ester/DAG-type 1
Zinc finger119 – 16951Phorbol-ester/DAG-type 2
Nucleotide binding356 – 3649ATP By similarity

Sites

Active site4741Proton acceptor By similarity
Binding site3791ATP By similarity

Natural variations

Alternative sequence67 – 7711CGYQSGYAWMG → WG in isoform Short.
VSP_004743
Natural variant4371M → I

Experimental info

Sequence conflict6081F → S in CAA28736. Ref.1
Sequence conflict6081F → S in CAA28890. Ref.1
Sequence conflict634 – 64815DVSNF…SEKTD → MCPTLTSSSHQRKQT Ref.1
Sequence conflict649 – 67931Missing Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: 3C69AD351E36B7DC

FASTA67977,695
        10         20         30         40         50         60 
MSEGSDNNGD PQQQGAEGEA VGENKMKSRL RKGALKKKNV FNVKDHCFIA RFFKQPTFCS 

        70         80         90        100        110        120 
HCKDFICGYQ SGYAWMGFGK QGFQCQVCSY VVHKRCHEYV TFICPGKDKG IDSDSPKTQH 

       130        140        150        160        170        180 
NFEPFTYAGP TFCDHCGSLL YGIYHQGLKC SACDMNVHAR CKENVPSLCG CDHTERRGRI 

       190        200        210        220        230        240 
YLEINVKENL LTVQIKEGRN LIPMDPNGLS DPYVKVKLIP DDKDQSKKKT RTIKACLNPV 

       250        260        270        280        290        300 
WNETLTYDLK PEDKDRRILI EVWDWDRTSR NDFMGALSFG ISEIIKNPTN GWFKLLTQDE 

       310        320        330        340        350        360 
GEYYNVPCAD DEQDLLKLKQ KPSQKKPMVM RSDTNTHTSS KKDMIRATDF NFIKVLGKGS 

       370        380        390        400        410        420 
FGKVLLAERK GSEELYAIKI LKKDVIIQDD DVECTMIEKR VLALGEKPPF LVQLHSCFQT 

       430        440        450        460        470        480 
MDRLFFVMEY VNGGDLMFQI QQFGKFKEPV AVFYAAEIAA GLFFLHTKGI LYRDLKLDNV 

       490        500        510        520        530        540 
LLDADGHVKI ADFGMCKENI VGDKTTKTFC GTPDYIAPEI ILYQPYGKSV DWWAYGVLLY 

       550        560        570        580        590        600 
EMLVGQPPFD GEDEEELFAA ITDHNVSYPK SLSKEAKEAC KGFLTKQPNK RLGCGSSGEE 

       610        620        630        640        650        660 
DVRLHPFFRR IDWEKIENRE VQPPFKPKIK HRKDVSNFDK QFTSEKTDLT PTDKVFMMNL 

       670 
DQSEFVGFSY MNPEYVFSP 

« Hide

Isoform Short.

Checksum: 588F5194A212BEAF
Show »

FASTA67076,734

References

« Hide 'large scale' references
[1]"Structure and nucleotide sequence of a Drosophila melanogaster protein kinase C gene."
Rosenthal A., Rhee L., Yadegari R., Paro R., Ullrich A., Goeddel D.V.
EMBO J. 6:433-441(1987) [PubMed: 3107983] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM SHORT).
Strain: Canton-S and Oregon-R.
[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: 10731132] [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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
Strain: Berkeley.
Tissue: Ovary.

Cross-references

Sequence databases

X05076 mRNA. Translation: CAA28736.1.
X05279 expand/collapse EMBL AC list , X05280, X05281, X05282, X05283 Genomic DNA. Translation: CAA28890.2.
AE013599 Genomic DNA. Translation: AAF57932.1.
AE013599 Genomic DNA. Translation: AAF57933.1.
AY095003 mRNA. Translation: AAM11331.1.
PIRA32545.
RefSeqNP_476682.1.
NP_725626.1.
UniGeneDm.3632

3D structure databases

HSSPHSSP built from PDB template 1DSY based on UniProtKB P05696.
ModBaseSearch...

Protein-protein interaction databases

IntActP05130. 2 interactions.

Genome annotation databases

EnsemblFBgn0003091. Drosophila melanogaster. [Contig view]
GeneID48311.

Organism-specific databases

FlyBaseFBgn0003091. Pkc53E.

Phylogenomic databases

HOGENOMP05130.
OMAP05130. EEGEFYN.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-005054-MON.
BRENDA2.7.11.13. 48.

Gene expression databases

ArrayExpressP05130.
GermOnlineCG6622. Drosophila melanogaster.

Family and domain databases

InterProIPR000961. AGC-kinase_C.
IPR000008. C2_Ca-dep.
IPR018029. C2_membr_targeting.
IPR002219. DAG_PE_bd.
IPR015745. PKC.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR014375. Protein_kinase_C_a/b/g.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PANTHERPTHR22985:SF86. PKC. 1 hit.
PfamPF00130. C1_1. 2 hits.
PF00168. C2. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
PIRSFPIRSF000550. PKC_alpha. 1 hit.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00109. C1. 2 hits.
SM00239. C2. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS50004. C2. 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. 1 hit.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio839293.

Entry information

Entry nameKPC1_DROME
AccessionPrimary (citable) accession number: P05130
Secondary accession number(s): Q9V7V6, Q9V7V7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 28, 2002
Last modified: June 16, 2009
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents