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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: 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 GRK2 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).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: phosphatidylinositol phosphate biosynthesis

This protein is involved in the pathway phosphatidylinositol phosphate biosynthesis, which is part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phosphatidylinositol phosphate biosynthesis and in Phospholipid metabolism.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi829 – 838ATP1 Publication10
Nucleotide bindingi864 – 872ATP1 Publication9
Nucleotide bindingi961 – 969ATP1 Publication9

GO - Molecular functioni

GO - Biological processi

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.
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
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000887941 – 1102Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoformAdd BLAST1102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1024Phosphothreonine; by PKABy similarity1
Modified residuei1101Phosphoserine; by autocatalysisBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO02697.

Expressioni

Gene expression databases

BgeeiENSSSCG00000027272.
GenevisibleiO02697. SS.

Interactioni

Subunit structurei

Heterodimer of a catalytic subunit PIK3CG and a PIK3R5 or PIK3R6 regulatory subunit. Interacts with GRK2 through the PIK helical domain. Interaction with GRK2 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).By similarity

Protein-protein interaction databases

IntActiO02697. 2 interactors.

Structurei

Secondary structure

11102
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi145 – 158Combined sources14
Beta strandi169 – 171Combined sources3
Helixi172 – 190Combined sources19
Helixi193 – 198Combined sources6
Helixi209 – 212Combined sources4
Helixi213 – 215Combined sources3
Beta strandi216 – 228Combined sources13
Beta strandi230 – 236Combined sources7
Helixi241 – 251Combined sources11
Beta strandi271 – 274Combined sources4
Beta strandi283 – 285Combined sources3
Helixi287 – 289Combined sources3
Helixi291 – 299Combined sources9
Beta strandi303 – 308Combined sources6
Helixi313 – 316Combined sources4
Beta strandi359 – 369Combined sources11
Beta strandi379 – 389Combined sources11
Beta strandi392 – 398Combined sources7
Beta strandi406 – 419Combined sources14
Helixi420 – 422Combined sources3
Beta strandi428 – 437Combined sources10
Beta strandi460 – 469Combined sources10
Beta strandi473 – 475Combined sources3
Beta strandi478 – 483Combined sources6
Helixi499 – 502Combined sources4
Turni510 – 512Combined sources3
Beta strandi515 – 520Combined sources6
Helixi549 – 559Combined sources11
Beta strandi563 – 565Combined sources3
Helixi569 – 577Combined sources9
Helixi579 – 582Combined sources4
Helixi586 – 588Combined sources3
Helixi589 – 593Combined sources5
Helixi601 – 612Combined sources12
Helixi615 – 619Combined sources5
Helixi624 – 629Combined sources6
Helixi638 – 648Combined sources11
Helixi653 – 666Combined sources14
Helixi667 – 669Combined sources3
Beta strandi671 – 674Combined sources4
Helixi676 – 687Combined sources12
Helixi689 – 705Combined sources17
Turni707 – 709Combined sources3
Helixi710 – 721Combined sources12
Helixi726 – 748Combined sources23
Helixi750 – 753Combined sources4
Beta strandi754 – 756Combined sources3
Helixi761 – 776Combined sources16
Beta strandi783 – 785Combined sources3
Beta strandi788 – 796Combined sources9
Helixi798 – 800Combined sources3
Beta strandi805 – 808Combined sources4
Beta strandi811 – 818Combined sources8
Beta strandi828 – 836Combined sources9
Helixi839 – 857Combined sources19
Beta strandi869 – 873Combined sources5
Beta strandi876 – 880Combined sources5
Beta strandi883 – 887Combined sources5
Helixi888 – 895Combined sources8
Beta strandi898 – 900Combined sources3
Helixi906 – 914Combined sources9
Helixi918 – 941Combined sources24
Helixi949 – 951Combined sources3
Beta strandi952 – 955Combined sources4
Beta strandi960 – 962Combined sources3
Helixi989 – 994Combined sources6
Beta strandi998 – 1001Combined sources4
Helixi1004 – 1021Combined sources18
Helixi1024 – 1037Combined sources14
Beta strandi1039 – 1041Combined sources3
Helixi1045 – 1054Combined sources10
Turni1055 – 1058Combined sources4
Helixi1061 – 1078Combined sources18
Helixi1081 – 1090Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO02697.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 141PI3K-ABDPROSITE-ProRule annotationAdd BLAST108
Domaini217 – 309PI3K-RBDPROSITE-ProRule annotationAdd BLAST93
Domaini357 – 521C2 PI3K-typePROSITE-ProRule annotationAdd BLAST165
Domaini541 – 723PIK helicalPROSITE-ProRule annotationAdd BLAST183
Domaini828 – 1073PI3K/PI4KPROSITE-ProRule annotationAdd BLAST246

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi17 – 22Poly-Arg6

Sequence similaritiesi

Belongs to the PI3/PI4-kinase family.PROSITE-ProRule annotation
Contains 1 C2 PI3K-type domain.PROSITE-ProRule annotation
Contains 1 PI3K-ABD domain.PROSITE-ProRule annotation
Contains 1 PI3K-RBD domain.PROSITE-ProRule annotation
Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 1 PIK helical domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG101026.
InParanoidiO02697.
KOiK00922.
OrthoDBiEOG091G027R.

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

« Hide

        10         20         30         40         50
MELENYEQPV VLREDNRRRR RRMKPRSTAA SLSSMELIPI EFVLPTSQRN
60 70 80 90 100
TKTPETALLH VAGHGNVEQM KAQVWLRALE TSVSADFYHR LGPDHFLLLY
110 120 130 140 150
QKKGQWYEIY DKYQVVQTLD CLRYWKVLHR SPGQIHVVQR HAPSEETLAF
160 170 180 190 200
QRQLNALIGY DVTDVSNVHD DELEFTRRRL VTPRMAEVAG RDPKLYAMHP
210 220 230 240 250
WVTSKPLPEY LLKKITNNCV FIVIHRSTTS QTIKVSADDT PGTILQSFFT
260 270 280 290 300
KMAKKKSLMD IPESQNERDF VLRVCGRDEY LVGETPIKNF QWVRQCLKNG
310 320 330 340 350
EEIHLVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF
360 370 380 390 400
TVSLWDCDRK FRVKIRGIDI PVLPRTADLT VFVEANIQYG QQVLCQRRTS
410 420 430 440 450
PKPFTEEVLW NVWLEFSIKI KDLPKGALLN LQIYCGKAPA LSGKTSAEMP
460 470 480 490 500
SPESKGKAQL LYYVNLLLID HRFLLRHGEY VLHMWQLSGK GEDQGSFNAD
510 520 530 540 550
KLTSRTNPDK ENSMSISILL DNYCHPIALP KHRPTPDPEG DRVRAEMPNQ
560 570 580 590 600
LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKDPKAYP KLFSSVKWGQ
610 620 630 640 650
QEIVAKTYQL LAKREVWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES
660 670 680 690 700
LEDDDVLHYL LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR
710 720 730 740 750
SEIAQSRHYQ QRFAVILEAY LRGCGTAMLH DFTQQVQVID MLQKVTIDIK
760 770 780 790 800
SLSAEKYDVS SQVISQLKQK LENLQNLNLP QSFRVPYDPG LKAGALVIEK
810 820 830 840 850
CKVMASKKKP LWLEFKCADP TALSNETIGI IFKHGDDLRQ DMLILQILRI
860 870 880 890 900
MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAK IQQSTVGNTG
910 920 930 940 950
AFKDEVLSHW LKEKCPIEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND
960 970 980 990 1000
NIMISETGNL FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGTSGK
1010 1020 1030 1040 1050
KTSLHFQKFQ DVCVKAYLAL RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY
1060 1070 1080 1090 1100
IRDALTVGKS EEDAKKYFLD QIEVCRDKGW TVQFNWFLHL VLGIKQGEKH

SA
Length:1,102
Mass (Da):126,658
Last modified:December 15, 1998 - v2
Checksum:i9E7D4211FD626DFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
Y10743 mRNA. Translation: CAA71731.1.
RefSeqiNP_999104.1. NM_213939.1.
UniGeneiSsc.82467.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO02697. 2 interactors.

Proteomic databases

PRIDEiO02697.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396979.
KEGGissc:396979.

Organism-specific databases

CTDi5294.

Phylogenomic databases

HOVERGENiHBG101026.
InParanoidiO02697.
KOiK00922.
OrthoDBiEOG091G027R.

Enzyme and pathway databases

UniPathwayiUPA00220.
BRENDAi2.7.1.137. 6170.

Miscellaneous databases

EvolutionaryTraceiO02697.

Gene expression databases

BgeeiENSSSCG00000027272.
GenevisibleiO02697. SS.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 126 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.