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O02697

- PK3CG_PIG

UniProt

O02697 - PK3CG_PIG

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Protein
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Gene
PIK3CG
Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Phosphoinositide-3-kinase (PI3K) that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Links G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses. Modulates leukocyte chemotaxis to inflammatory sites and in response to chemoattractant agents. May control leukocyte polarization and migration by regulating the spatial accumulation of PIP3 and by regulating the organization of F-actin formation and integrin-based adhesion at the leading edge. Controls motility of dendritic cells. Participates in T-lymphocyte migration. Regulates T-lymphocyte proliferation and cytokine production. Required for B-lymphocyte development and signaling. Together with other PI3Ks are involved in the oxidative burst produced by neutrophils in response to chemotactic agents. Together with PIK3CD regulate neutrophil extravasation. Together with PIK3CB promotes platelet aggregation and thrombosis. Regulates alpha-IIb/beta-3 integrins (ITGA2B/ ITGB3) adhesive function in platelets downstream of P2Y12 through a lipid kinase activity-independent mechanism. May have also a lipid kinase activity-dependent function in platelet aggregation. Involved in endothelial progenitor cell migration. Negative regulator of cardiac contractility. Modulates cardiac contractility by anchoring protein kinase A (PKA) and PDE3B activation, reducing cAMP levels. Regulates cardiac contractility also by promoting beta-adrenergic receptor internalization by binding to ADRBK1 and by non-muscle tropomyosin phosphorylation. Also has serine/threonine protein kinase activity: both lipid and protein kinase activities are required for beta-adrenergic receptor endocytosis. May also have a scaffolding role in modulating cardiac contractility. Contribute to cardiac hypertrophy under pathological stress. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which the PI3K gamma complex is activated by RAPGEF3 and which is involved in angiogenesis By similarity.

Catalytic activityi

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

Enzyme regulationi

Activated by both the alpha and the beta-gamma G proteins following stimulation of G protein-coupled receptors (GPCRs). Activation by GPCRs is assisted by the regulatory subunits (PIK3R5 or PIK3R6) leading to the translocation from the cytosol to the plasma membrane and to kinase activation. When bound to PIK3R5 the PI3K activity of PIK3CG could be activated greater than 100-fold by the beta-gamma G proteins.

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi829 – 83810ATP
Nucleotide bindingi864 – 8729ATP
Nucleotide bindingi961 – 9699ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: UniProtKB-EC
  3. protein serine/threonine kinase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. chemotaxis Source: UniProtKB-KW
  3. endocytosis Source: UniProtKB-KW
  4. immune system process Source: UniProtKB-KW
  5. inflammatory response Source: UniProtKB-KW
  6. phosphatidylinositol-mediated signaling Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Angiogenesis, Chemotaxis, Endocytosis, Immunity, Inflammatory response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.137. 6170.
ReactomeiREACT_208233. Synthesis of PIPs at the plasma membrane.
REACT_208923. G beta:gamma signalling through PI3Kgamma.
UniPathwayiUPA00220.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (EC:2.7.1.153)
Short name:
PI3-kinase subunit gamma
Short name:
PI3K-gamma
Short name:
PI3Kgamma
Short name:
PtdIns-3-kinase subunit gamma
Alternative name(s):
Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma
Short name:
PtdIns-3-kinase subunit p110-gamma
Short name:
p110gamma
Phosphoinositide-3-kinase catalytic gamma polypeptide
Serine/threonine protein kinase PIK3CG (EC:2.7.11.1)
p120-PI3K
Gene namesi
Name:PIK3CG
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227: Unplaced

Subcellular locationi

Cytoplasm By similarity. Cell membrane By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11021102Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
PRO_0000088794Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1024 – 10241Phosphothreonine; by PKA By similarity
Modified residuei1101 – 11011Phosphoserine; by autocatalysis By similarity

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit PIK3CG and a PIK3R5 or PIK3R6 regulatory subunit. Interacts with ADRBK1 through the PIK helical domain. Interaction with ADRBK1 is required for targeting to agonist-occupied receptor. Interacts with PDE3B. Interacts with TPM2. Interacts with EPHA8; regulates integrin-mediated cell adhesion to substrate. Interacts with HRAS; the interaction is required for membrane recruitment and beta-gamma G protein dimer-dependent activation of the PI3K gamma complex PIK3CG:PIK3R6 By similarity.1 Publication

Protein-protein interaction databases

IntActiO02697. 2 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi145 – 15814
Beta strandi169 – 1713
Helixi172 – 19019
Helixi193 – 1986
Helixi209 – 2124
Helixi213 – 2153
Beta strandi216 – 22813
Beta strandi230 – 2367
Helixi241 – 25111
Beta strandi271 – 2744
Beta strandi283 – 2853
Helixi287 – 2893
Helixi291 – 2999
Beta strandi303 – 3086
Helixi313 – 3164
Beta strandi359 – 36911
Beta strandi379 – 38911
Beta strandi392 – 3987
Beta strandi406 – 41914
Helixi420 – 4223
Beta strandi428 – 43710
Beta strandi460 – 46910
Beta strandi473 – 4753
Beta strandi478 – 4836
Helixi499 – 5024
Turni510 – 5123
Beta strandi515 – 5206
Helixi549 – 55911
Beta strandi563 – 5653
Helixi569 – 5779
Helixi579 – 5824
Helixi586 – 5883
Helixi589 – 5935
Helixi601 – 61212
Helixi615 – 6195
Helixi624 – 6296
Helixi638 – 64811
Helixi653 – 66614
Helixi667 – 6693
Beta strandi671 – 6744
Helixi676 – 68712
Helixi689 – 70517
Turni707 – 7093
Helixi710 – 72112
Helixi726 – 74823
Helixi750 – 7534
Beta strandi754 – 7563
Helixi761 – 77616
Beta strandi783 – 7853
Beta strandi788 – 7969
Helixi798 – 8003
Beta strandi805 – 8084
Beta strandi811 – 8188
Beta strandi828 – 8369
Helixi839 – 85719
Beta strandi869 – 8735
Beta strandi876 – 8805
Beta strandi883 – 8875
Helixi888 – 8958
Beta strandi898 – 9003
Helixi906 – 9149
Helixi918 – 94124
Helixi949 – 9513
Beta strandi952 – 9554
Beta strandi960 – 9623
Helixi989 – 9946
Beta strandi998 – 10014
Helixi1004 – 102118
Helixi1024 – 103714
Beta strandi1039 – 10413
Helixi1045 – 105410
Turni1055 – 10584
Helixi1061 – 107818
Helixi1081 – 109010

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E7UX-ray2.00A144-1102[»]
1E7VX-ray2.40A144-1102[»]
1E8WX-ray2.50A144-1102[»]
1E8XX-ray2.20A144-1094[»]
1E90X-ray2.70A144-1102[»]
ProteinModelPortaliO02697.
SMRiO02697. Positions 144-1094.

Miscellaneous databases

EvolutionaryTraceiO02697.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 141108PI3K-ABD
Add
BLAST
Domaini217 – 30993PI3K-RBD
Add
BLAST
Domaini357 – 521165C2 PI3K-type
Add
BLAST
Domaini541 – 723183PIK helical
Add
BLAST
Domaini828 – 1073246PI3K/PI4K
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi17 – 226Poly-Arg

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.
Contains 1 PI3K-ABD domain.
Contains 1 PI3K-RBD domain.
Contains 1 PI3K/PI4K domain.
Contains 1 PIK helical domain.

Phylogenomic databases

HOVERGENiHBG101026.
KOiK00922.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003113. PI3K_adapt-bd_dom.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10048. PTHR10048. 1 hit.
PfamiPF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view]
SMARTiSM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51544. PI3K_ABD. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O02697-1 [UniParc]FASTAAdd to Basket

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MELENYEQPV VLREDNRRRR RRMKPRSTAA SLSSMELIPI EFVLPTSQRN     50
TKTPETALLH VAGHGNVEQM KAQVWLRALE TSVSADFYHR LGPDHFLLLY 100
QKKGQWYEIY DKYQVVQTLD CLRYWKVLHR SPGQIHVVQR HAPSEETLAF 150
QRQLNALIGY DVTDVSNVHD DELEFTRRRL VTPRMAEVAG RDPKLYAMHP 200
WVTSKPLPEY LLKKITNNCV FIVIHRSTTS QTIKVSADDT PGTILQSFFT 250
KMAKKKSLMD IPESQNERDF VLRVCGRDEY LVGETPIKNF QWVRQCLKNG 300
EEIHLVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF 350
TVSLWDCDRK FRVKIRGIDI PVLPRTADLT VFVEANIQYG QQVLCQRRTS 400
PKPFTEEVLW NVWLEFSIKI KDLPKGALLN LQIYCGKAPA LSGKTSAEMP 450
SPESKGKAQL LYYVNLLLID HRFLLRHGEY VLHMWQLSGK GEDQGSFNAD 500
KLTSRTNPDK ENSMSISILL DNYCHPIALP KHRPTPDPEG DRVRAEMPNQ 550
LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKDPKAYP KLFSSVKWGQ 600
QEIVAKTYQL LAKREVWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES 650
LEDDDVLHYL LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR 700
SEIAQSRHYQ QRFAVILEAY LRGCGTAMLH DFTQQVQVID MLQKVTIDIK 750
SLSAEKYDVS SQVISQLKQK LENLQNLNLP QSFRVPYDPG LKAGALVIEK 800
CKVMASKKKP LWLEFKCADP TALSNETIGI IFKHGDDLRQ DMLILQILRI 850
MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAK IQQSTVGNTG 900
AFKDEVLSHW LKEKCPIEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND 950
NIMISETGNL FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGTSGK 1000
KTSLHFQKFQ DVCVKAYLAL RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY 1050
IRDALTVGKS EEDAKKYFLD QIEVCRDKGW TVQFNWFLHL VLGIKQGEKH 1100
SA 1102
Length:1,102
Mass (Da):126,658
Last modified:December 15, 1998 - v2
Checksum:i9E7D4211FD626DFC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10743 mRNA. Translation: CAA71731.1.
RefSeqiNP_999104.1. NM_213939.1.
UniGeneiSsc.82467.

Genome annotation databases

GeneIDi396979.
KEGGissc:396979.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10743 mRNA. Translation: CAA71731.1 .
RefSeqi NP_999104.1. NM_213939.1.
UniGenei Ssc.82467.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E7U X-ray 2.00 A 144-1102 [» ]
1E7V X-ray 2.40 A 144-1102 [» ]
1E8W X-ray 2.50 A 144-1102 [» ]
1E8X X-ray 2.20 A 144-1094 [» ]
1E90 X-ray 2.70 A 144-1102 [» ]
ProteinModelPortali O02697.
SMRi O02697. Positions 144-1094.
ModBasei Search...

Protein-protein interaction databases

IntActi O02697. 2 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396979.
KEGGi ssc:396979.

Organism-specific databases

CTDi 5294.

Phylogenomic databases

HOVERGENi HBG101026.
KOi K00922.

Enzyme and pathway databases

UniPathwayi UPA00220 .
BRENDAi 2.7.1.137. 6170.
Reactomei REACT_208233. Synthesis of PIPs at the plasma membrane.
REACT_208923. G beta:gamma signalling through PI3Kgamma.

Miscellaneous databases

EvolutionaryTracei O02697.

Family and domain databases

Gene3Di 1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
2.60.40.150. 1 hit.
InterProi IPR016024. ARM-type_fold.
IPR000008. C2_dom.
IPR011009. Kinase-like_dom.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR003113. PI3K_adapt-bd_dom.
IPR002420. PI3K_C2_dom.
IPR000341. PI3K_Ras-bd_dom.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
PANTHERi PTHR10048. PTHR10048. 1 hit.
Pfami PF00454. PI3_PI4_kinase. 1 hit.
PF00792. PI3K_C2. 1 hit.
PF00794. PI3K_rbd. 1 hit.
PF00613. PI3Ka. 1 hit.
[Graphical view ]
SMARTi SM00142. PI3K_C2. 1 hit.
SM00144. PI3K_rbd. 1 hit.
SM00145. PI3Ka. 1 hit.
SM00146. PI3Kc. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF54236. SSF54236. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51544. PI3K_ABD. 1 hit.
PS51547. PI3K_C2. 1 hit.
PS51546. PI3K_RBD. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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.
  3. "Structural determinants of phosphoinositide 3-kinase inhibition by wortmannin, LY294002, quercetin, myricetin, and staurosporine."
    Walker E.H., Pacold M.E., Perisic O., Stephens L., Hawkins P.T., Wymann M.P., Williams R.L.
    Mol. Cell 6:909-919(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-1102 IN COMPLEX WITH ATP AND INHIBITORS.

Entry informationi

Entry nameiPK3CG_PIG
AccessioniPrimary (citable) accession number: O02697
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 15, 1998
Last modified: September 3, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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