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Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform (PI3-kinase subunit gamma) (PI3K-gamma) (PI3Kgamma) (PtdIns-3-kinase subunit gamma) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma) (PtdIns-3-kinase subunit p110-gamma) (p110gamma) (Phosphoinositide-3-kinase catalytic gamma polypeptide) (Serine/threonine protein kinase PIK3CG) (EC 2.7.11.1) (p120-PI3K)

 PK3CG_PIG               Reviewed;        1102 AA.
O02697;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
12-SEP-2018, entry version 138.
RecName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform;
Short=PI3-kinase subunit gamma;
Short=PI3K-gamma;
Short=PI3Kgamma;
Short=PtdIns-3-kinase subunit gamma;
EC=2.7.1.153;
AltName: Full=Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma;
Short=PtdIns-3-kinase subunit p110-gamma;
Short=p110gamma;
AltName: Full=Phosphoinositide-3-kinase catalytic gamma polypeptide;
AltName: Full=Serine/threonine protein kinase PIK3CG;
EC=2.7.11.1;
AltName: Full=p120-PI3K;
Name=PIK3CG;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND INTERACTION
WITH PIK3R5.
TISSUE=Neutrophil;
PubMed=9094719; DOI=10.1016/S0092-8674(00)80187-7;
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.;
"The G beta gamma sensitivity of a PI3K is dependent upon a tightly
associated adaptor, p101.";
Cell 89:105-114(1997).
[2]
SEQUENCE REVISION.
Stephens L.R.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[3]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 144-1102 IN COMPLEX WITH ATP
AND INHIBITORS.
PubMed=11090628; DOI=10.1016/S1097-2765(05)00089-4;
Walker E.H., Pacold M.E., Perisic O., Stephens L., Hawkins P.T.,
Wymann M.P., Williams R.L.;
"Structural determinants of phosphoinositide 3-kinase inhibition by
wortmannin, LY294002, quercetin, myricetin, and staurosporine.";
Mol. Cell 6:909-919(2000).
-!- FUNCTION: 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).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4,5-
bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-
trisphosphate.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ACTIVITY REGULATION: 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.
-!- PATHWAY: Phospholipid metabolism; phosphatidylinositol phosphate
biosynthesis.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
{ECO:0000255|PROSITE-ProRule:PRU00877, ECO:0000255|PROSITE-
ProRule:PRU00879, ECO:0000255|PROSITE-ProRule:PRU00880}.
-----------------------------------------------------------------------
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EMBL; Y10743; CAA71731.1; -; mRNA.
RefSeq; NP_999104.1; NM_213939.1.
UniGene; Ssc.82467; -.
PDB; 1E7U; X-ray; 2.00 A; A=144-1102.
PDB; 1E7V; X-ray; 2.40 A; A=144-1102.
PDB; 1E8W; X-ray; 2.50 A; A=144-1102.
PDB; 1E8X; X-ray; 2.20 A; A=144-1094.
PDB; 1E90; X-ray; 2.70 A; A=144-1102.
PDBsum; 1E7U; -.
PDBsum; 1E7V; -.
PDBsum; 1E8W; -.
PDBsum; 1E8X; -.
PDBsum; 1E90; -.
ProteinModelPortal; O02697; -.
SMR; O02697; -.
IntAct; O02697; 2.
STRING; 9823.ENSSSCP00000024176; -.
PaxDb; O02697; -.
PRIDE; O02697; -.
GeneID; 396979; -.
KEGG; ssc:396979; -.
CTD; 5294; -.
HOVERGEN; HBG101026; -.
InParanoid; O02697; -.
KO; K21289; -.
OrthoDB; EOG091G027R; -.
BRENDA; 2.7.1.137; 6170.
UniPathway; UPA00220; -.
EvolutionaryTrace; O02697; -.
Proteomes; UP000008227; Unplaced.
Genevisible; O02697; SS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005944; C:phosphatidylinositol 3-kinase complex, class IB; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IBA:GO_Central.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0002250; P:adaptive immune response; IBA:GO_Central.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0070527; P:platelet aggregation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
GO; GO:0010818; P:T cell chemotaxis; IBA:GO_Central.
Gene3D; 1.10.1070.11; -; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR036940; PI3/4_kinase_cat_sf.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR003113; PI3K_adapt-bd_dom.
InterPro; IPR002420; PI3K_C2_dom.
InterPro; IPR000341; PI3K_Ras-bd_dom.
InterPro; IPR008290; PI3K_Vps34.
InterPro; IPR015433; PI_Kinase.
InterPro; IPR001263; PInositide-3_kin_accessory_dom.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR10048; PTHR10048; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
Pfam; PF00792; PI3K_C2; 1.
Pfam; PF00794; PI3K_rbd; 1.
Pfam; PF00613; PI3Ka; 1.
PIRSF; PIRSF000587; PI3K_Vps34; 1.
SMART; SM00142; PI3K_C2; 1.
SMART; SM00144; PI3K_rbd; 1.
SMART; SM00145; PI3Ka; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00915; PI3_4_KINASE_1; 1.
PROSITE; PS00916; PI3_4_KINASE_2; 1.
PROSITE; PS50290; PI3_4_KINASE_3; 1.
PROSITE; PS51544; PI3K_ABD; 1.
PROSITE; PS51547; PI3K_C2; 1.
PROSITE; PS51546; PI3K_RBD; 1.
PROSITE; PS51545; PIK_HELICAL; 1.
1: Evidence at protein level;
3D-structure; Angiogenesis; ATP-binding; Cell membrane; Chemotaxis;
Complete proteome; Cytoplasm; Direct protein sequencing; Endocytosis;
Immunity; Inflammatory response; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase.
CHAIN 1 1102 Phosphatidylinositol 4,5-bisphosphate 3-
kinase catalytic subunit gamma isoform.
/FTId=PRO_0000088794.
DOMAIN 34 141 PI3K-ABD. {ECO:0000255|PROSITE-
ProRule:PRU00877}.
DOMAIN 217 309 PI3K-RBD. {ECO:0000255|PROSITE-
ProRule:PRU00879}.
DOMAIN 357 521 C2 PI3K-type. {ECO:0000255|PROSITE-
ProRule:PRU00880}.
DOMAIN 541 723 PIK helical. {ECO:0000255|PROSITE-
ProRule:PRU00878}.
DOMAIN 828 1073 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
NP_BIND 829 838 ATP. {ECO:0000269|PubMed:11090628}.
NP_BIND 864 872 ATP. {ECO:0000269|PubMed:11090628}.
NP_BIND 961 969 ATP. {ECO:0000269|PubMed:11090628}.
COMPBIAS 17 22 Poly-Arg.
MOD_RES 1024 1024 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:Q9JHG7}.
MOD_RES 1101 1101 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:P48736}.
HELIX 145 158 {ECO:0000244|PDB:1E7U}.
STRAND 169 171 {ECO:0000244|PDB:1E7U}.
HELIX 172 190 {ECO:0000244|PDB:1E7U}.
HELIX 193 198 {ECO:0000244|PDB:1E7U}.
HELIX 209 212 {ECO:0000244|PDB:1E7U}.
HELIX 213 215 {ECO:0000244|PDB:1E8X}.
STRAND 216 228 {ECO:0000244|PDB:1E7U}.
STRAND 230 236 {ECO:0000244|PDB:1E7U}.
HELIX 241 251 {ECO:0000244|PDB:1E7U}.
STRAND 271 274 {ECO:0000244|PDB:1E7U}.
STRAND 283 285 {ECO:0000244|PDB:1E7U}.
HELIX 287 289 {ECO:0000244|PDB:1E7U}.
HELIX 291 299 {ECO:0000244|PDB:1E7U}.
STRAND 303 308 {ECO:0000244|PDB:1E7U}.
HELIX 313 316 {ECO:0000244|PDB:1E7U}.
STRAND 359 369 {ECO:0000244|PDB:1E7U}.
STRAND 379 389 {ECO:0000244|PDB:1E7U}.
STRAND 392 398 {ECO:0000244|PDB:1E7U}.
STRAND 406 419 {ECO:0000244|PDB:1E7U}.
HELIX 420 422 {ECO:0000244|PDB:1E7U}.
STRAND 428 437 {ECO:0000244|PDB:1E7U}.
STRAND 460 469 {ECO:0000244|PDB:1E7U}.
STRAND 473 475 {ECO:0000244|PDB:1E7U}.
STRAND 478 483 {ECO:0000244|PDB:1E7U}.
HELIX 499 502 {ECO:0000244|PDB:1E7U}.
TURN 510 512 {ECO:0000244|PDB:1E7U}.
STRAND 515 520 {ECO:0000244|PDB:1E7U}.
HELIX 549 559 {ECO:0000244|PDB:1E7U}.
STRAND 563 565 {ECO:0000244|PDB:1E7V}.
HELIX 569 577 {ECO:0000244|PDB:1E7U}.
HELIX 579 582 {ECO:0000244|PDB:1E7U}.
HELIX 586 588 {ECO:0000244|PDB:1E7U}.
HELIX 589 593 {ECO:0000244|PDB:1E7U}.
HELIX 601 612 {ECO:0000244|PDB:1E7U}.
HELIX 615 619 {ECO:0000244|PDB:1E7U}.
HELIX 624 629 {ECO:0000244|PDB:1E7U}.
HELIX 638 648 {ECO:0000244|PDB:1E7U}.
HELIX 653 666 {ECO:0000244|PDB:1E7U}.
HELIX 667 669 {ECO:0000244|PDB:1E7U}.
STRAND 671 674 {ECO:0000244|PDB:1E7U}.
HELIX 676 687 {ECO:0000244|PDB:1E7U}.
HELIX 689 705 {ECO:0000244|PDB:1E7U}.
TURN 707 709 {ECO:0000244|PDB:1E7U}.
HELIX 710 721 {ECO:0000244|PDB:1E7U}.
HELIX 726 748 {ECO:0000244|PDB:1E7U}.
HELIX 750 753 {ECO:0000244|PDB:1E7U}.
STRAND 754 756 {ECO:0000244|PDB:1E8X}.
HELIX 761 776 {ECO:0000244|PDB:1E7U}.
STRAND 783 785 {ECO:0000244|PDB:1E7U}.
STRAND 788 796 {ECO:0000244|PDB:1E7U}.
HELIX 798 800 {ECO:0000244|PDB:1E7U}.
STRAND 805 808 {ECO:0000244|PDB:1E7V}.
STRAND 811 818 {ECO:0000244|PDB:1E7U}.
STRAND 828 836 {ECO:0000244|PDB:1E7U}.
HELIX 839 857 {ECO:0000244|PDB:1E7U}.
STRAND 869 873 {ECO:0000244|PDB:1E7U}.
STRAND 876 880 {ECO:0000244|PDB:1E7U}.
STRAND 883 887 {ECO:0000244|PDB:1E7U}.
HELIX 888 895 {ECO:0000244|PDB:1E7U}.
STRAND 898 900 {ECO:0000244|PDB:1E7U}.
HELIX 906 914 {ECO:0000244|PDB:1E7U}.
HELIX 918 941 {ECO:0000244|PDB:1E7U}.
HELIX 949 951 {ECO:0000244|PDB:1E7U}.
STRAND 952 955 {ECO:0000244|PDB:1E7U}.
STRAND 960 962 {ECO:0000244|PDB:1E7U}.
HELIX 989 994 {ECO:0000244|PDB:1E7U}.
STRAND 998 1001 {ECO:0000244|PDB:1E7V}.
HELIX 1004 1021 {ECO:0000244|PDB:1E7U}.
HELIX 1024 1037 {ECO:0000244|PDB:1E7U}.
STRAND 1039 1041 {ECO:0000244|PDB:1E8X}.
HELIX 1045 1054 {ECO:0000244|PDB:1E7U}.
TURN 1055 1058 {ECO:0000244|PDB:1E7U}.
HELIX 1061 1078 {ECO:0000244|PDB:1E7U}.
HELIX 1081 1090 {ECO:0000244|PDB:1E7U}.
SEQUENCE 1102 AA; 126658 MW; 9E7D4211FD626DFC CRC64;
MELENYEQPV VLREDNRRRR RRMKPRSTAA SLSSMELIPI EFVLPTSQRN TKTPETALLH
VAGHGNVEQM KAQVWLRALE TSVSADFYHR LGPDHFLLLY QKKGQWYEIY DKYQVVQTLD
CLRYWKVLHR SPGQIHVVQR HAPSEETLAF QRQLNALIGY DVTDVSNVHD DELEFTRRRL
VTPRMAEVAG RDPKLYAMHP WVTSKPLPEY LLKKITNNCV FIVIHRSTTS QTIKVSADDT
PGTILQSFFT KMAKKKSLMD IPESQNERDF VLRVCGRDEY LVGETPIKNF QWVRQCLKNG
EEIHLVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF TVSLWDCDRK
FRVKIRGIDI PVLPRTADLT VFVEANIQYG QQVLCQRRTS PKPFTEEVLW NVWLEFSIKI
KDLPKGALLN LQIYCGKAPA LSGKTSAEMP SPESKGKAQL LYYVNLLLID HRFLLRHGEY
VLHMWQLSGK GEDQGSFNAD KLTSRTNPDK ENSMSISILL DNYCHPIALP KHRPTPDPEG
DRVRAEMPNQ LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKDPKAYP KLFSSVKWGQ
QEIVAKTYQL LAKREVWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES LEDDDVLHYL
LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR SEIAQSRHYQ QRFAVILEAY
LRGCGTAMLH DFTQQVQVID MLQKVTIDIK SLSAEKYDVS SQVISQLKQK LENLQNLNLP
QSFRVPYDPG LKAGALVIEK CKVMASKKKP LWLEFKCADP TALSNETIGI IFKHGDDLRQ
DMLILQILRI MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAK IQQSTVGNTG
AFKDEVLSHW LKEKCPIEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND NIMISETGNL
FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGTSGK KTSLHFQKFQ DVCVKAYLAL
RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY IRDALTVGKS EEDAKKYFLD QIEVCRDKGW
TVQFNWFLHL VLGIKQGEKH SA


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