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Reviewed, UniProtKB/Swiss-Prot O02697 (PK3CG_PIG)

Last modified September 1, 2009. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
    EC=2.7.1.153
Alternative name(s):
    PI3-kinase p110 subunit gamma
    PtdIns-3-kinase subunit p110
    PI3Kgamma
      Short name=PI3K
    p120-PI3K
Gene names
Name: PIK3CG
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length1102 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

3-phosphorylates the cellular phosphoinositide PtdIns-4,5-biphosphate (PtdIns(4,5)P2) to produce PtdIns-3, 4,5-triiphosphate (PtdIns(3,4,5)P3). Links G-protein coupled receptor activation to the secondary messenger PtdIns(3,4,5)P3 production.

Catalytic activity

ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate.

Enzyme regulation

Activated by both the alpha and the beta-gamma G proteins. When bound to PIK3R5 the PI3K activity of PIK3CG could be activated greater than 100-fold by the beta-gamma G proteins.

Pathway

Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis.

Subunit structure

Heterodimer of a catalytic subunit (PIK3CG/p120) and a regulatory (PIK3R5a/p101) subunit.

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 PI3K/PI4K domain.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11021102Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
PRO_0000088794

Regions

Domain828 – 1073246PI3K/PI4K
Compositional bias17 – 226Poly-Arg

Secondary structure

1 ................................................................................................................................. 1102
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O02697-1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 9E7D4211FD626DFC

FASTA1,102126,658
        10         20         30         40         50         60 
MELENYEQPV VLREDNRRRR RRMKPRSTAA SLSSMELIPI EFVLPTSQRN TKTPETALLH 

        70         80         90        100        110        120 
VAGHGNVEQM KAQVWLRALE TSVSADFYHR LGPDHFLLLY QKKGQWYEIY DKYQVVQTLD 

       130        140        150        160        170        180 
CLRYWKVLHR SPGQIHVVQR HAPSEETLAF QRQLNALIGY DVTDVSNVHD DELEFTRRRL 

       190        200        210        220        230        240 
VTPRMAEVAG RDPKLYAMHP WVTSKPLPEY LLKKITNNCV FIVIHRSTTS QTIKVSADDT 

       250        260        270        280        290        300 
PGTILQSFFT KMAKKKSLMD IPESQNERDF VLRVCGRDEY LVGETPIKNF QWVRQCLKNG 

       310        320        330        340        350        360 
EEIHLVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF TVSLWDCDRK 

       370        380        390        400        410        420 
FRVKIRGIDI PVLPRTADLT VFVEANIQYG QQVLCQRRTS PKPFTEEVLW NVWLEFSIKI 

       430        440        450        460        470        480 
KDLPKGALLN LQIYCGKAPA LSGKTSAEMP SPESKGKAQL LYYVNLLLID HRFLLRHGEY 

       490        500        510        520        530        540 
VLHMWQLSGK GEDQGSFNAD KLTSRTNPDK ENSMSISILL DNYCHPIALP KHRPTPDPEG 

       550        560        570        580        590        600 
DRVRAEMPNQ LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKDPKAYP KLFSSVKWGQ 

       610        620        630        640        650        660 
QEIVAKTYQL LAKREVWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES LEDDDVLHYL 

       670        680        690        700        710        720 
LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR SEIAQSRHYQ QRFAVILEAY 

       730        740        750        760        770        780 
LRGCGTAMLH DFTQQVQVID MLQKVTIDIK SLSAEKYDVS SQVISQLKQK LENLQNLNLP 

       790        800        810        820        830        840 
QSFRVPYDPG LKAGALVIEK CKVMASKKKP LWLEFKCADP TALSNETIGI IFKHGDDLRQ 

       850        860        870        880        890        900 
DMLILQILRI MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAK IQQSTVGNTG 

       910        920        930        940        950        960 
AFKDEVLSHW LKEKCPIEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND NIMISETGNL 

       970        980        990       1000       1010       1020 
FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGTSGK KTSLHFQKFQ DVCVKAYLAL 

      1030       1040       1050       1060       1070       1080 
RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY IRDALTVGKS EEDAKKYFLD QIEVCRDKGW 

      1090       1100 
TVQFNWFLHL VLGIKQGEKH SA

« Hide

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References

[1]"The G beta gamma sensitivity of a PI3K is dependent upon a tightly associated adaptor, p101."
Stephens L.R., Eguinoa A., Erdjument-Bromage H., Lui M., Cooke F., Coadwell J., Smrcka A.S., Thelen M., Cadwallader K., Tempst P., Hawkins P.T.
Cell 89:105-114(1997) [PubMed: 9094719] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH PIK3R5.
Tissue: Neutrophil.
[2]Stephens L.R.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

Y10743 mRNA. Translation: CAA71731.1.
RefSeqNP_999104.1.
UniGeneSsc.11109

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1E7UX-ray2.00A144-1102[»]
1E7VX-ray2.40A144-1102[»]
1E8WX-ray2.50A144-1102[»]
1E8XX-ray2.20A144-1102[»]
1E90X-ray2.70A144-1102[»]
ModBaseSearch...

Genome annotation databases

GeneID396979.
KEGGssc:396979.

Organism-specific databases

CTD396979.

Phylogenomic databases

HOVERGENO02697.

Enzyme and pathway databases

BRENDA2.7.1.137. 249.
2.7.1.153. 249.

Family and domain databases

InterProIPR000403. PI3/4_kinase_cat.
IPR018936. PI3/4_kinase_CS.
IPR002420. PI3K_C2.
IPR000341. PI3K_ras_bd.
IPR001263. PI3Ka.
IPR015433. PI_Kinase.
[Graphical view]
Gene3DG3DSA:1.10.1070.11. PI3/4_kinase_cat. 1 hit.
G3DSA:1.25.40.70. PI3Ka. 1 hit.
PANTHERPTHR10048. PI_Kinase. 1 hit.
PfamPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
SMARTSM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
PROSITEPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePK3CG_PIG
AccessionPrimary (citable) accession number: O02697
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 15, 1998
Last modified: September 1, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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