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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_MOUSE             Reviewed;        1102 AA.
Q9JHG7; Q80V09;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
30-AUG-2017, entry version 149.
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; Synonyms=Pi3kg1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ENZYME REGULATION.
PubMed=11054537; DOI=10.1016/S0378-1119(00)00328-0;
Hirsch E., Wymann M.P., Patrucco E., Tolosano E., Bulgarelli-Leva G.,
Marengo S., Rocchi M., Altruda F.;
"Analysis of the murine phosphoinositide 3-kinase gamma gene.";
Gene 256:69-81(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N-3; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 1060-1065, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[4]
FUNCTION ON INFLAMMATION AND CHEMOTACTIC RESPONSE, AND DISRUPTION
PHENOTYPE.
PubMed=10669416; DOI=10.1126/science.287.5455.1040;
Sasaki T., Irie-Sasaki J., Jones R.G., Oliveira-dos-Santos A.J.,
Stanford W.L., Bolon B., Wakeham A., Itie A., Bouchard D.,
Kozieradzki I., Joza N., Mak T.W., Ohashi P.S., Suzuki A.,
Penninger J.M.;
"Function of PI3Kgamma in thymocyte development, T cell activation,
and neutrophil migration.";
Science 287:1040-1046(2000).
[5]
FUNCTION ON INFLAMMATION AND CHEMOTACTIC RESPONSE, AND DISRUPTION
PHENOTYPE.
PubMed=10669418; DOI=10.1126/science.287.5455.1049;
Hirsch E., Katanaev V.L., Garlanda C., Azzolino O., Pirola L.,
Silengo L., Sozzani S., Mantovani A., Altruda F., Wymann M.P.;
"Central role for G protein-coupled phosphoinositide 3-kinase gamma in
inflammation.";
Science 287:1049-1053(2000).
[6]
INTERACTION WITH EPHA8.
PubMed=11416136; DOI=10.1128/MCB.21.14.4579-4597.2001;
Gu C., Park S.;
"The EphA8 receptor regulates integrin activity through p110gamma
phosphatidylinositol-3 kinase in a tyrosine kinase activity-
independent manner.";
Mol. Cell. Biol. 21:4579-4597(2001).
[7]
FUNCTION ON CARDIAC CONTRACTILITY, AND DISRUPTION PHENOTYPE.
PubMed=12297047; DOI=10.1016/S0092-8674(02)00969-8;
Crackower M.A., Oudit G.Y., Kozieradzki I., Sarao R., Sun H.,
Sasaki T., Hirsch E., Suzuki A., Shioi T., Irie-Sasaki J., Sah R.,
Cheng H.-Y.M., Rybin V.O., Lembo G., Fratta L.,
Oliveira-dos-Santos A.J., Benovic J.L., Kahn C.R., Izumo S.,
Steinberg S.F., Wymann M.P., Backx P.H., Penninger J.M.;
"Regulation of myocardial contractility and cell size by distinct
PI3K-PTEN signaling pathways.";
Cell 110:737-749(2002).
[8]
FUNCTION, INTERACTION WITH PDE3B, AND DISRUPTION PHENOTYPE.
PubMed=15294162; DOI=10.1016/j.cell.2004.07.017;
Patrucco E., Notte A., Barberis L., Selvetella G., Maffei A.,
Brancaccio M., Marengo S., Russo G., Azzolino O., Rybalkin S.D.,
Silengo L., Altruda F., Wetzker R., Wymann M.P., Lembo G., Hirsch E.;
"PI3Kgamma modulates the cardiac response to chronic pressure overload
by distinct kinase-dependent and -independent effects.";
Cell 118:375-387(2004).
[9]
FUNCTION ON IMMUNE RESPONSE, AND DISRUPTION PHENOTYPE.
PubMed=15318168; DOI=10.1038/sj.emboj.7600361;
Del Prete A., Vermi W., Dander E., Otero K., Barberis L., Luini W.,
Bernasconi S., Sironi M., Santoro A., Garlanda C., Facchetti F.,
Wymann M.P., Vecchi A., Hirsch E., Mantovani A., Sozzani S.;
"Defective dendritic cell migration and activation of adaptive
immunity in PI3Kgamma-deficient mice.";
EMBO J. 23:3505-3515(2004).
[10]
FUNCTION IN T-CELL DEVELOPMENT.
PubMed=16116162; DOI=10.4049/jimmunol.175.5.2783;
Webb L.M.C., Vigorito E., Wymann M.P., Hirsch E., Turner M.;
"T cell development requires the combined activities of the p110gamma
and p110delta catalytic isoforms of phosphatidylinositol 3-kinase.";
J. Immunol. 175:2783-2787(2005).
[11]
FUNCTION ON INFLAMMATION AND CHEMOTACTIC RESPONSE, AND DISRUPTION
PHENOTYPE.
PubMed=16127437; DOI=10.1038/nm1284;
Camps M., Rueckle T., Ji H., Ardissone V., Rintelen F., Shaw J.,
Ferrandi C., Chabert C., Gillieron C., Francon B., Martin T.,
Gretener D., Perrin D., Leroy D., Vitte P.-A., Hirsch E., Wymann M.P.,
Cirillo R., Schwarz M.K., Rommel C.;
"Blockade of PI3Kgamma suppresses joint inflammation and damage in
mouse models of rheumatoid arthritis.";
Nat. Med. 11:936-943(2005).
[12]
FUNCTION ON PLATELET AGGREGATION, AND DISRUPTION PHENOTYPE.
PubMed=17673465; DOI=10.1074/jbc.M704358200;
Schoenwaelder S.M., Ono A., Sturgeon S., Chan S.M., Mangin P.,
Maxwell M.J., Turnbull S., Mulchandani M., Anderson K.,
Kauffenstein G., Rewcastle G.W., Kendall J., Gachet C., Salem H.H.,
Jackson S.P.;
"Identification of a unique co-operative phosphoinositide 3-kinase
signaling mechanism regulating integrin alpha IIb beta 3 adhesive
function in platelets.";
J. Biol. Chem. 282:28648-28658(2007).
[13]
FUNCTION IN NATURAL KILLER CELL MIGRATION, AND ENZYME REGULATION.
PubMed=19297623; DOI=10.1073/pnas.0808594106;
Saudemont A., Garcon F., Yadi H., Roche-Molina M., Kim N.,
Segonds-Pichon A., Martin-Fontecha A., Okkenhaug K., Colucci F.;
"p110gamma and p110delta isoforms of phosphoinositide 3-kinase
differentially regulate natural killer cell migration in health and
disease.";
Proc. Natl. Acad. Sci. U.S.A. 106:5795-5800(2009).
[14]
INTERACTION WITH HRAS.
PubMed=19906996; DOI=10.1073/pnas.0905506106;
Kurig B., Shymanets A., Bohnacker T., Prajwal X., Brock C.,
Ahmadian M.R., Schaefer M., Gohla A., Harteneck C., Wymann M.P.,
Jeanclos E., Nurnberg B.;
"Ras is an indispensable coregulator of the class IB phosphoinositide
3-kinase p87/p110gamma.";
Proc. Natl. Acad. Sci. U.S.A. 106:20312-20317(2009).
[15]
FUNCTION ON CARDIAC CONTRACTILITY, AND PHOSPHORYLATION AT THR-1024.
PubMed=21474070; DOI=10.1016/j.molcel.2011.01.030;
Perino A., Ghigo A., Ferrero E., Morello F., Santulli G.,
Baillie G.S., Damilano F., Dunlop A.J., Pawson C., Walser R., Levi R.,
Altruda F., Silengo L., Langeberg L.K., Neubauer G., Heymans S.,
Lembo G., Wymann M.P., Wetzker R., Houslay M.D., Iaccarino G.,
Scott J.D., Hirsch E.;
"Integrating cardiac PIP3 and cAMP signaling through a PKA anchoring
function of p110gamma.";
Mol. Cell 42:84-95(2011).
-!- 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. Together with PIK3CD is involved in natural killer (NK)
cell development and migration towards the sites of inflammation.
Participates in T-lymphocyte migration. Regulates T-lymphocyte
proliferation and cytokine production. Together with PIK3CD
participates in T-lymphocyte development. Required for B-
lymphocyte development and signaling. Together with PIK3CD
participates in neutrophil respiratory burst. Together with PIK3CD
is involved in neutrophil chemotaxis and 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, ECO:0000269|PubMed:10669416,
ECO:0000269|PubMed:10669418, ECO:0000269|PubMed:12297047,
ECO:0000269|PubMed:15294162, ECO:0000269|PubMed:15318168,
ECO:0000269|PubMed:16116162, ECO:0000269|PubMed:16127437,
ECO:0000269|PubMed:17673465, ECO:0000269|PubMed:19297623,
ECO:0000269|PubMed:21474070}.
-!- 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.
-!- ENZYME 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 subunit
PIK3R5 leading to the translocation from the cytosol to the plasma
membrane and to kinase activation; the respective activation
involving PIK3R6 requires HRAS for membrane recruitment.
Wortmannin sensitive in nM range. Inhibited by AS252424.
{ECO:0000269|PubMed:11054537, ECO:0000269|PubMed:19297623}.
-!- 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 (By similarity). Interaction with GRK2 is required
for targeting to agonist-occupied receptor. Interacts with PDE3B.
Interacts with TPM2 (By similarity). 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. {ECO:0000250,
ECO:0000269|PubMed:11416136, ECO:0000269|PubMed:15294162,
ECO:0000269|PubMed:19906996}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}.
-!- PTM: Phosphorylated at Thr-1024 by PKA. Phosphorylation inhibits
lipid kinase activity. {ECO:0000269|PubMed:21474070}.
-!- DISRUPTION PHENOTYPE: Viable and fertile. Display abnormalities
when the immune system is stressed. Reduced leukocyte migration in
response to chemotactic agents and towards the site of
inflammation. Reduced neutrophil oxidative burst in response to
chemotactic agents. Reduced thymocyte survival and defective T
lymphocyte activation. Protected from leukocyte infiltration of
synovia in a model of rheumatoid arthritis. Dendritic cell showed
reduced response to chemokines and migration to draining lymph
nodes under inflammatory conditions. Platelets have defects in
thrombus formation. Increased cardiac contractility. Display
myocardial damage after transverse aortic constriction.
{ECO:0000269|PubMed:10669416, ECO:0000269|PubMed:10669418,
ECO:0000269|PubMed:12297047, ECO:0000269|PubMed:15294162,
ECO:0000269|PubMed:15318168, ECO:0000269|PubMed:16127437,
ECO:0000269|PubMed:17673465}.
-!- 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; AJ249280; CAB89686.1; -; mRNA.
EMBL; AJ249413; CAB89851.1; -; Genomic_DNA.
EMBL; AJ249414; CAB89851.1; JOINED; Genomic_DNA.
EMBL; AJ249415; CAB89851.1; JOINED; Genomic_DNA.
EMBL; AJ249416; CAB89851.1; JOINED; Genomic_DNA.
EMBL; AJ249417; CAB89851.1; JOINED; Genomic_DNA.
EMBL; AJ249418; CAB89851.1; JOINED; Genomic_DNA.
EMBL; AJ249419; CAB89851.1; JOINED; Genomic_DNA.
EMBL; AJ249420; CAB89851.1; JOINED; Genomic_DNA.
EMBL; BC051246; AAH51246.1; -; mRNA.
CCDS; CCDS25870.1; -.
RefSeq; NP_001139672.1; NM_001146200.1.
RefSeq; NP_001139673.1; NM_001146201.1.
RefSeq; NP_064668.2; NM_020272.2.
RefSeq; XP_006515175.1; XM_006515112.3.
UniGene; Mm.101369; -.
UniGene; Mm.404021; -.
ProteinModelPortal; Q9JHG7; -.
SMR; Q9JHG7; -.
BioGrid; 206031; 2.
DIP; DIP-41862N; -.
IntAct; Q9JHG7; 6.
MINT; MINT-1612546; -.
STRING; 10090.ENSMUSP00000062864; -.
BindingDB; Q9JHG7; -.
ChEMBL; CHEMBL2189158; -.
iPTMnet; Q9JHG7; -.
PhosphoSitePlus; Q9JHG7; -.
EPD; Q9JHG7; -.
MaxQB; Q9JHG7; -.
PaxDb; Q9JHG7; -.
PRIDE; Q9JHG7; -.
Ensembl; ENSMUST00000053215; ENSMUSP00000062864; ENSMUSG00000020573.
Ensembl; ENSMUST00000085469; ENSMUSP00000082596; ENSMUSG00000020573.
Ensembl; ENSMUST00000156904; ENSMUSP00000123539; ENSMUSG00000020573.
Ensembl; ENSMUST00000220366; ENSMUSP00000151400; ENSMUSG00000020573.
GeneID; 30955; -.
KEGG; mmu:30955; -.
UCSC; uc007nib.2; mouse.
CTD; 5294; -.
MGI; MGI:1353576; Pik3cg.
eggNOG; KOG0904; Eukaryota.
eggNOG; COG5032; LUCA.
GeneTree; ENSGT00760000119110; -.
HOGENOM; HOG000252912; -.
HOVERGEN; HBG101026; -.
InParanoid; Q9JHG7; -.
KO; K21289; -.
OMA; FTEEVLW; -.
OrthoDB; EOG091G027R; -.
PhylomeDB; Q9JHG7; -.
TreeFam; TF102031; -.
BRENDA; 2.7.1.153; 3474.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
UniPathway; UPA00220; -.
ChiTaRS; Pik3cg; mouse.
PRO; PR:Q9JHG7; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000020573; -.
Genevisible; Q9JHG7; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005944; C:phosphatidylinositol 3-kinase complex, class IB; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:0046875; F:ephrin receptor binding; ISO:MGI.
GO; GO:0016301; F:kinase activity; ISO:MGI.
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:0071320; P:cellular response to cAMP; IMP:MGI.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:MGI.
GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IDA:MGI.
GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IEA:Ensembl.
GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:MGI.
GO; GO:0016310; P:phosphorylation; ISO:MGI.
GO; GO:0070527; P:platelet aggregation; IBA:GO_Central.
GO; GO:0002675; P:positive regulation of acute inflammatory response; IEA:Ensembl.
GO; GO:0043085; P:positive regulation of catalytic activity; IMP:MGI.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:1903169; P:regulation of calcium ion transmembrane transport; IMP:MGI.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
GO; GO:0032252; P:secretory granule localization; IEA:Ensembl.
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; IPR000008; C2_dom.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
InterPro; IPR018936; PI3/4_kinase_CS.
InterPro; IPR003113; PI3K_adapt-bd_dom.
InterPro; IPR002420; PI3K_C2_dom.
InterPro; IPR000341; PI3K_Ras-bd_dom.
InterPro; IPR015433; PI_Kinase.
InterPro; IPR001263; PInositide-3_kin_accessory_dom.
InterPro; IPR029071; Ubiquitin-rel_dom.
PANTHER; PTHR10048; PTHR10048; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
Pfam; PF00792; PI3K_C2; 1.
Pfam; PF00794; PI3K_rbd; 1.
Pfam; PF00613; PI3Ka; 1.
SMART; SM00142; PI3K_C2; 1.
SMART; SM00144; PI3K_rbd; 1.
SMART; SM00145; PI3Ka; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF49562; SSF49562; 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;
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_0000088793.
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:0000250}.
NP_BIND 864 872 ATP. {ECO:0000250}.
NP_BIND 961 969 ATP. {ECO:0000250}.
COMPBIAS 18 22 Poly-Arg.
MOD_RES 1024 1024 Phosphothreonine; by PKA.
{ECO:0000269|PubMed:21474070}.
MOD_RES 1101 1101 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:P48736}.
CONFLICT 262 262 S -> P (in Ref. 1; CAB89686/CAB89851).
{ECO:0000305}.
CONFLICT 350 350 F -> V (in Ref. 1; CAB89686/CAB89851).
{ECO:0000305}.
SEQUENCE 1102 AA; 126400 MW; 7675848792D76734 CRC64;
MELENYEQPV VLREDNLRRR RRMKPRSAAG SLSSMELIPI EFVLPTSQRI SKTPETALLH
VAGHGNVEQM KAQVWLRALE TSVAAEFYHR LGPDQFLLLY QKKGQWYEIY DRYQVVQTLD
CLHYWKLMHK SPGQIHVVQR HVPSEETLAF QKQLTSLIGY DVTDISNVHD DELEFTRRRL
VTPRMAEVAG RDAKLYAMHP WVTSKPLPDY LSKKIANNCI FIVIHRGTTS QTIKVSADDT
PGTILQSFFT KMAKKKSLMN ISESQSEQDF VLRVCGRDEY LVGETPLKNF QWVRQCLKNG
DEIHLVLDTP PDPALDEVRK EEWPLVDDCT GVTGYHEQLT IHGKDHESVF TVSLWDCDRK
FRVKIRGIDI PVLPRNTDLT VFVEANIQHG QQVLCQRRTS PKPFAEEVLW NVWLEFGIKI
KDLPKGALLN LQIYCCKTPS LSSKASAETP GSESKGKAQL LYYVNLLLID HRFLLRHGDY
VLHMWQISGK AEEQGSFNAD KLTSATNPDK ENSMSISILL DNYCHPIALP KHRPTPDPEG
DRVRAEMPNQ LRKQLEAIIA TDPLNPLTAE DKELLWHFRY ESLKHPKAYP KLFSSVKWGQ
QEIVAKTYQL LARREIWDQS ALDVGLTMQL LDCNFSDENV RAIAVQKLES LEDDDVLHYL
LQLVQAVKFE PYHDSALARF LLKRGLRNKR IGHFLFWFLR SEIAQSRHYQ QRFAVILEAY
LRGCGTAMLQ DFTQQVHVIE MLQKVTIDIK SLSAEKYDVS SQVISQLKQK LESLQNSNLP
ESFRVPYDPG LKAGTLVIEK CKVMASKKKP LWLEFKCADP TVLSNETIGI IFKHGDDLRQ
DMLILQILRI MESIWETESL DLCLLPYGCI STGDKIGMIE IVKDATTIAQ IQQSTVGNTG
AFKDEVLNHW LKEKCPIEEK FQAAVERFVY SCAGYCVATF VLGIGDRHND NIMISETGNL
FHIDFGHILG NYKSFLGINK ERVPFVLTPD FLFVMGSSGK KTSPHFQKFQ DVCVRAYLAL
RHHTNLLIIL FSMMLMTGMP QLTSKEDIEY IRDALTVGKS EEDAKKYFLD QIEVCRDKGW
TVQFNWFLHL VLGIKQGEKH SA


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