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Reviewed, UniProtKB/Swiss-Prot P05128 (KPCG_BOVIN)

Last modified June 16, 2009. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein kinase C gamma type
      Short name=PKC-gamma
    EC=2.7.11.13
Gene names
Name: PRKCG
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length682 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

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

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.

Cofactor

Binds 3 calcium ions per subunit. The ions are bound to the C2 domain By similarity.

Subunit structure

Interacts with CDCP1 By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 682›682Protein kinase C gamma type
PRO_0000055688

Regions

Domain155 – 24591C2
Domain336 – 599264Protein kinase
Domain600 – 67071AGC-kinase C-terminal
Zinc finger20 – 7051Phorbol-ester/DAG-type 1
Zinc finger85 – 13551Phorbol-ester/DAG-type 2
Nucleotide binding342 – 3509ATP By similarity

Sites

Active site4651Proton acceptor By similarity
Metal binding1711Calcium 1; via carbonyl oxygen By similarity
Metal binding1721Calcium 1 By similarity
Metal binding1721Calcium 2 By similarity
Metal binding1781Calcium 2 By similarity
Metal binding2311Calcium 1 By similarity
Metal binding2311Calcium 2 By similarity
Metal binding2321Calcium 2; via carbonyl oxygen By similarity
Metal binding2331Calcium 1 By similarity
Metal binding2331Calcium 2 By similarity
Metal binding2331Calcium 3 By similarity
Metal binding2361Calcium 3 By similarity
Metal binding2371Calcium 3; via carbonyl oxygen By similarity
Metal binding2391Calcium 1 By similarity
Metal binding2391Calcium 3 By similarity
Binding site3651ATP By similarity

Amino acid modifications

Modified residue1801Phosphotyrosine By similarity
Modified residue2971Phosphotyrosine By similarity
Modified residue3071Phosphoserine By similarity
Modified residue3151Phosphoserine By similarity
Modified residue4991Phosphothreonine By similarity
Modified residue5031Phosphothreonine By similarity
Modified residue6331Phosphothreonine; by autocatalysis Potential
Modified residue6401Phosphothreonine; by autocatalysis Potential
Modified residue6721Phosphoserine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P05128-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 20392D11188C731C

FASTA68277,156
        10         20         30         40         50         60 
RPLFCRKGAL RQKVVHEVKS HKFTARFFKQ PTFCSHCTDF IWGIGKQGLQ CQVCSFVVHR 

        70         80         90        100        110        120 
RCHEFVTFEC PGAGKGPQTD DPRNKHKFRL HSYSSPTFCD HCGSLLYGLV HQGMKCSCCE 

       130        140        150        160        170        180 
MNVHRRCVRS VPSLCGVDHT ERRGRLQLEI RAPTSDEIHV TVGEARNLIP MDPNGLSDPY 

       190        200        210        220        230        240 
VKLKLIPDPR NLTKQKTRTV KATLNPVWNE TFVFNLKPGD VERRLSVEVW DWDRTSRNDF 

       250        260        270        280        290        300 
MGAMSFGVSE LLKAPVDGWY KLLNQEEGEY YNVPVADADN CNLLQKFEAC NYPLELYERV 

       310        320        330        340        350        360 
RTGPSSSPIP SPSPSPTDSK RCFFGASPGR LHISDFSFLM VLGKGSFGKV MLAERRGSDE 

       370        380        390        400        410        420 
LYAIKILKKD VIVQDDDVDC TLVEKRVLAL GGRGPGGRPH FLTQLHSTFQ TPDRLYFVME 

       430        440        450        460        470        480 
YVTGGDLMYH IQQLGKFKEP HAAFYAAEIA IGLFFLHNQG IIYRDLKLDN VMLDAEGHIK 

       490        500        510        520        530        540 
ITDFGMCKEN VFPGSTTRTF CGTPDYIAPE IIAYQPYGKS VDWWSFGVLL YEMLAGQPPF 

       550        560        570        580        590        600 
DGEDEEELFQ AIMEQTVTYP KSLSREAVAI CKGFLTKHPA KRLGSGPDGE PTIRAHGFFR 

       610        620        630        640        650        660 
WIDWDRLERL EIAPPFRPRP CGRSGENFDK FFTRAAPALT PPDRLVLASI DQAEFQGFTY 

       670        680 
VNPDFVHPDA RSPISPTPVP VM 

« Hide

References

[1]"Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways."
Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E., Waterfield M.D., Francke U., Ullrich A.
Science 233:859-866(1986) [PubMed: 3755548] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The molecular heterogeneity of protein kinase C and its implications for cellular regulation."
Nishizuka Y.
Nature 334:661-665(1988) [PubMed: 3045562] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

M13976 mRNA. Translation: AAA30704.1.
IPIIPI00685679.
PIRKIBOGC. C24664.
UniGeneBt.12762

3D structure databases

HSSPHSSP built from PDB template 1TBN based on UniProtKB P05697.
SMRP05128. Positions 78-143, 333-668.
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000013550. Bos taurus. [Contig view]

Phylogenomic databases

HOVERGENP05128.

Enzyme and pathway databases

BRENDA2.7.11.13. 251.

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. 2 hits.
PS50081. ZF_DAG_PE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKPCG_BOVIN
AccessionPrimary (citable) accession number: P05128
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 16, 2009
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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