Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O02697

- PK3CG_PIG

UniProt

O02697 - PK3CG_PIG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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).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 – 83810ATP1 Publication
Nucleotide bindingi864 – 8729ATP1 Publication
Nucleotide bindingi961 – 9699ATP1 Publication

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

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-KW
  2. plasma membrane Source: UniProtKB-KW
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 isoformPRO_0000088794Add
BLAST

Amino acid modifications

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

Protein-protein interaction databases

IntActiO02697. 2 interactions.

Structurei

Secondary structure

1
1102
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi145 – 15814Combined sources
Beta strandi169 – 1713Combined sources
Helixi172 – 19019Combined sources
Helixi193 – 1986Combined sources
Helixi209 – 2124Combined sources
Helixi213 – 2153Combined sources
Beta strandi216 – 22813Combined sources
Beta strandi230 – 2367Combined sources
Helixi241 – 25111Combined sources
Beta strandi271 – 2744Combined sources
Beta strandi283 – 2853Combined sources
Helixi287 – 2893Combined sources
Helixi291 – 2999Combined sources
Beta strandi303 – 3086Combined sources
Helixi313 – 3164Combined sources
Beta strandi359 – 36911Combined sources
Beta strandi379 – 38911Combined sources
Beta strandi392 – 3987Combined sources
Beta strandi406 – 41914Combined sources
Helixi420 – 4223Combined sources
Beta strandi428 – 43710Combined sources
Beta strandi460 – 46910Combined sources
Beta strandi473 – 4753Combined sources
Beta strandi478 – 4836Combined sources
Helixi499 – 5024Combined sources
Turni510 – 5123Combined sources
Beta strandi515 – 5206Combined sources
Helixi549 – 55911Combined sources
Beta strandi563 – 5653Combined sources
Helixi569 – 5779Combined sources
Helixi579 – 5824Combined sources
Helixi586 – 5883Combined sources
Helixi589 – 5935Combined sources
Helixi601 – 61212Combined sources
Helixi615 – 6195Combined sources
Helixi624 – 6296Combined sources
Helixi638 – 64811Combined sources
Helixi653 – 66614Combined sources
Helixi667 – 6693Combined sources
Beta strandi671 – 6744Combined sources
Helixi676 – 68712Combined sources
Helixi689 – 70517Combined sources
Turni707 – 7093Combined sources
Helixi710 – 72112Combined sources
Helixi726 – 74823Combined sources
Helixi750 – 7534Combined sources
Beta strandi754 – 7563Combined sources
Helixi761 – 77616Combined sources
Beta strandi783 – 7853Combined sources
Beta strandi788 – 7969Combined sources
Helixi798 – 8003Combined sources
Beta strandi805 – 8084Combined sources
Beta strandi811 – 8188Combined sources
Beta strandi828 – 8369Combined sources
Helixi839 – 85719Combined sources
Beta strandi869 – 8735Combined sources
Beta strandi876 – 8805Combined sources
Beta strandi883 – 8875Combined sources
Helixi888 – 8958Combined sources
Beta strandi898 – 9003Combined sources
Helixi906 – 9149Combined sources
Helixi918 – 94124Combined sources
Helixi949 – 9513Combined sources
Beta strandi952 – 9554Combined sources
Beta strandi960 – 9623Combined sources
Helixi989 – 9946Combined sources
Beta strandi998 – 10014Combined sources
Helixi1004 – 102118Combined sources
Helixi1024 – 103714Combined sources
Beta strandi1039 – 10413Combined sources
Helixi1045 – 105410Combined sources
Turni1055 – 10584Combined sources
Helixi1061 – 107818Combined sources
Helixi1081 – 109010Combined sources

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO02697.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 141108PI3K-ABDPROSITE-ProRule annotationAdd
BLAST
Domaini217 – 30993PI3K-RBDPROSITE-ProRule annotationAdd
BLAST
Domaini357 – 521165C2 PI3K-typePROSITE-ProRule annotationAdd
BLAST
Domaini541 – 723183PIK helicalPROSITE-ProRule annotationAdd
BLAST
Domaini828 – 1073246PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST

Compositional bias

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

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.

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 [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:
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...
MobiDBi 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.
InParanoidi O02697.
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: October 29, 2014
This is version 112 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