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Phosphatidylinositol 3-kinase catalytic subunit type 3 (PI3-kinase type 3) (PI3K type 3) (PtdIns-3-kinase type 3) (EC 2.7.1.137) (Phosphatidylinositol 3-kinase p100 subunit) (Phosphoinositide-3-kinase class 3) (hVps34)

 PK3C3_HUMAN             Reviewed;         887 AA.
Q8NEB9; Q15134;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
13-FEB-2019, entry version 164.
RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3;
Short=PI3-kinase type 3;
Short=PI3K type 3;
Short=PtdIns-3-kinase type 3;
EC=2.7.1.137;
AltName: Full=Phosphatidylinositol 3-kinase p100 subunit;
AltName: Full=Phosphoinositide-3-kinase class 3;
AltName: Full=hVps34;
Name=PIK3C3 {ECO:0000312|HGNC:HGNC:8974};
Synonyms=VPS34 {ECO:0000305};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, SUBUNIT, TISSUE
SPECIFICITY, AND INTERACTION WITH PIK3R4.
PubMed=7628435;
Volinia S., Dhand R., Vanhaesebroeck B., MacDougall L.K.,
Zvelebil M.J., Domin J., Panaretou C., Waterfield M.D.;
"A human phosphatidylinositol 3-kinase complex related to the yeast
Vps34p-Vps15p protein sorting system.";
EMBO J. 14:3339-3348(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis, and Uterus;
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] {ECO:0000305}
FUNCTION, INTERACTION WITH RAB7A AND PIK3R4, AND SUBCELLULAR LOCATION.
PubMed=14617358; DOI=10.1034/j.1600-0854.2003.00133.x;
Stein M.P., Feng Y., Cooper K.L., Welford A.M., Wandinger-Ness A.;
"Human VPS34 and p150 are Rab7 interacting partners.";
Traffic 4:754-771(2003).
[4]
INTERACTION WITH NCKAP1L.
PubMed=16417406; DOI=10.1371/journal.pbio.0040038;
Weiner O.D., Rentel M.C., Ott A., Brown G.E., Jedrychowski M.,
Yaffe M.B., Gygi S.P., Cantley L.C., Bourne H.R., Kirschner M.W.;
"Hem-1 complexes are essential for Rac activation, actin
polymerization, and myosin regulation during neutrophil chemotaxis.";
PLoS Biol. 4:E38-E38(2006).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[6]
INTERACTION WITH BECN1 AND ATG14.
PubMed=19050071; DOI=10.1073/pnas.0810452105;
Sun Q., Fan W., Chen K., Ding X., Chen S., Zhong Q.;
"Identification of Barkor as a mammalian autophagy-specific factor for
Beclin 1 and class III phosphatidylinositol 3-kinase.";
Proc. Natl. Acad. Sci. U.S.A. 105:19211-19216(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[8]
FUNCTION, AND SUBUNIT.
PubMed=20643123; DOI=10.1016/j.yexcr.2010.07.008;
Thoresen S.B., Pedersen N.M., Liestol K., Stenmark H.;
"A phosphatidylinositol 3-kinase class III sub-complex containing
VPS15, VPS34, Beclin 1, UVRAG and BIF-1 regulates cytokinesis and
degradative endocytic traffic.";
Exp. Cell Res. 316:3368-3378(2010).
[9]
INTERACTION WITH BECN1; RUBCN; ATG14; PIK3R4 AND UVRAG.
PubMed=19270696; DOI=10.1038/ncb1846;
Matsunaga K., Saitoh T., Tabata K., Omori H., Satoh T., Kurotori N.,
Maejima I., Shirahama-Noda K., Ichimura T., Isobe T., Akira S.,
Noda T., Yoshimori T.;
"Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally
regulate autophagy at different stages.";
Nat. Cell Biol. 11:385-396(2009).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20208530; DOI=10.1038/ncb2036;
Sagona A.P., Nezis I.P., Pedersen N.M., Liestol K., Poulton J.,
Rusten T.E., Skotheim R.I., Raiborg C., Stenmark H.;
"PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment
of FYVE-CENT to the midbody.";
Nat. Cell Biol. 12:362-371(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
INTERACTION WITH SLAMF1.
PubMed=22493499; DOI=10.1074/jbc.M112.367060;
Ma C., Wang N., Detre C., Wang G., O'Keeffe M., Terhorst C.;
"Receptor signaling lymphocyte-activation molecule family 1 (Slamf1)
regulates membrane fusion and NADPH oxidase 2 (NOX2) activity by
recruiting a Beclin-1/Vps34/ultraviolet radiation resistance-
associated gene (UVRAG) complex.";
J. Biol. Chem. 287:18359-18365(2012).
[13]
INTERACTION WITH BECN1P1/BECN2.
PubMed=23954414; DOI=10.1016/j.cell.2013.07.035;
He C., Wei Y., Sun K., Li B., Dong X., Zou Z., Liu Y., Kinch L.N.,
Khan S., Sinha S., Xavier R.J., Grishin N.V., Xiao G., Eskelinen E.L.,
Scherer P.E., Whistler J.L., Levine B.;
"Beclin 2 functions in autophagy, degradation of G protein-coupled
receptors, and metabolism.";
Cell 154:1085-1099(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
INTERACTION WITH BECN1.
PubMed=23878393; DOI=10.1128/MCB.00079-13;
Fogel A.I., Dlouhy B.J., Wang C., Ryu S.W., Neutzner A., Hasson S.A.,
Sideris D.P., Abeliovich H., Youle R.J.;
"Role of membrane association and Atg14-dependent phosphorylation in
beclin-1-mediated autophagy.";
Mol. Cell. Biol. 33:3675-3688(2013).
[16]
RECONSTITUTION OF THE PI3K COMPLEX I, AND ELECTRON MICROSCOPY OF THE
PI3K COMPLEX I.
PubMed=25490155; DOI=10.7554/eLife.05115;
Baskaran S., Carlson L.A., Stjepanovic G., Young L.N., Kim do J.,
Grob P., Stanley R.E., Nogales E., Hurley J.H.;
"Architecture and dynamics of the autophagic phosphatidylinositol 3-
kinase complex.";
Elife 3:0-0(2014).
-!- FUNCTION: Catalytic subunit of the PI3K complex that mediates
formation of phosphatidylinositol 3-phosphate; different complex
forms are believed to play a role in multiple membrane trafficking
pathways: PI3KC3-C1 is involved in initiation of autophagosomes
and PI3KC3-C2 in maturation of autophagosomes and endocytosis.
Involved in regulation of degradative endocytic trafficking and
required for the abcission step in cytokinesis, probably in the
context of PI3KC3-C2 (PubMed:20643123, PubMed:20208530). Involved
in the transport of lysosomal enzyme precursors to lysosomes.
Required for transport from early to late endosomes (By
similarity). {ECO:0000250|UniProtKB:O88763,
ECO:0000269|PubMed:14617358, ECO:0000269|PubMed:20208530,
ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:7628435,
ECO:0000305}.
-!- CATALYTIC ACTIVITY:
Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP
= a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 3-
phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709,
ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880,
ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137;
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:7628435};
-!- SUBUNIT: Component of the PI3K (PI3KC3/PI3K-III/class III
phosphatidylinositol 3-kinase) complex the core of which is
composed of the catalytic subunit PIK3C3, the regulatory subunit
PIK3R4 and BECN1 associating with additional regulatory/auxilliary
subunits to form alternative complex forms. Alternative complex
forms containing a forth regulatory subunit in a mutually
exclusive manner are: the PI3K complex I (PI3KC3-C1) containing
ATG14, and the PI3K complex II (PI3KC3-C2) containing UVRAG.
PI3KC3-C1 displays a V-shaped architecture with PIK3R4 serving as
a bridge between PIK3C3 and the ATG14:BECN1 subcomplex. Both,
PI3KC3-C1 and PI3KC3-C2, can associate with further regulatory
subunits such as RUBCN, SH3GLB1/Bif-1 and AMBRA1 (PubMed:7628435,
PubMed:19050071, PubMed:20643123, PubMed:19270696,
PubMed:23878393, PubMed:25490155). PI3KC3-C1 probably associates
with PIK3CB (By similarity). Interacts with RAB7A in the presence
of PIK3R4 (PubMed:14617358). Interacts with AMBRA1 (By
similarity). Interacts with BECN1P1/BECN2 (PubMed:23954414).
Interacts with SLAMF1(PubMed:22493499). May be a component of a
complex composed of RAB5A (in GDP-bound form), DYN2 and PIK3C3 (By
similarity). Interacts with NCKAP1L (PubMed:16417406).
{ECO:0000250|UniProtKB:Q6PF93, ECO:0000250|UniProtKB:Q9TXI7,
ECO:0000269|PubMed:14617358, ECO:0000269|PubMed:16417406,
ECO:0000269|PubMed:19050071, ECO:0000269|PubMed:19270696,
ECO:0000269|PubMed:20643123, ECO:0000269|PubMed:22493499,
ECO:0000269|PubMed:23878393, ECO:0000269|PubMed:23954414,
ECO:0000269|PubMed:25490155, ECO:0000269|PubMed:7628435,
ECO:0000305}.
-!- INTERACTION:
Q6ZNE5:ATG14; NbExp=25; IntAct=EBI-1056470, EBI-2690371;
Q14457:BECN1; NbExp=31; IntAct=EBI-1056470, EBI-949378;
Q96F24:NRBF2; NbExp=11; IntAct=EBI-1056470, EBI-2362014;
Q92622:RUBCN; NbExp=7; IntAct=EBI-1056470, EBI-2952709;
Q9P2Y5:UVRAG; NbExp=21; IntAct=EBI-1056470, EBI-2952704;
Q17UT5:X (xeno); NbExp=2; IntAct=EBI-1056470, EBI-15834514;
-!- SUBCELLULAR LOCATION: Midbody {ECO:0000269|PubMed:20208530}. Late
endosome {ECO:0000269|PubMed:14617358}. Cytoplasmic vesicle,
autophagosome {ECO:0000305|PubMed:14617358}. Note=As component of
the PI3K complex I localized to pre-autophagosome structures. As
component of the PI3K complex II localized predominantly to
endosomes (Probable). Localizes also to discrete punctae along the
ciliary axoneme and to the base of the ciliary axoneme (By
similarity). {ECO:0000250|UniProtKB:Q6PF93,
ECO:0000305|PubMed:14617358}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed, with a highest
expression in skeletal muscle. {ECO:0000269|PubMed:7628435}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
{ECO:0000255|PROSITE-ProRule:PRU00880}.
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EMBL; Z46973; CAA87094.1; -; mRNA.
EMBL; BC033004; AAH33004.1; -; mRNA.
EMBL; BC053651; AAH53651.1; -; mRNA.
CCDS; CCDS11920.1; -.
PIR; S57219; S57219.
RefSeq; NP_002638.2; NM_002647.3.
UniGene; Hs.464971; -.
UniGene; Hs.656958; -.
PDB; 3IHY; X-ray; 2.80 A; A/B/C/D/E=282-879.
PDB; 3LS8; X-ray; 2.25 A; A/B=268-879.
PDB; 4OYS; X-ray; 2.90 A; A=282-879.
PDB; 4PH4; X-ray; 2.80 A; B=293-887.
PDB; 4UWF; X-ray; 2.99 A; A=282-879.
PDB; 4UWG; X-ray; 2.70 A; A=282-879.
PDB; 4UWH; X-ray; 1.93 A; A=282-879.
PDB; 4UWK; X-ray; 2.83 A; A=282-879.
PDB; 4UWL; X-ray; 2.80 A; A=282-879.
PDB; 5ANL; X-ray; 2.70 A; A=282-879.
PDB; 5ENN; X-ray; 2.70 A; A/B=293-887.
PDBsum; 3IHY; -.
PDBsum; 3LS8; -.
PDBsum; 4OYS; -.
PDBsum; 4PH4; -.
PDBsum; 4UWF; -.
PDBsum; 4UWG; -.
PDBsum; 4UWH; -.
PDBsum; 4UWK; -.
PDBsum; 4UWL; -.
PDBsum; 5ANL; -.
PDBsum; 5ENN; -.
ProteinModelPortal; Q8NEB9; -.
SMR; Q8NEB9; -.
BioGrid; 111307; 38.
ComplexPortal; CPX-73; Phosphatidylinositol 3-kinase complex, class III, ATG14 variant.
ComplexPortal; CPX-74; Phosphatidylinositol 3-kinase complex, class III, UVRAG variant.
CORUM; Q8NEB9; -.
DIP; DIP-42272N; -.
IntAct; Q8NEB9; 23.
MINT; Q8NEB9; -.
STRING; 9606.ENSP00000262039; -.
BindingDB; Q8NEB9; -.
ChEMBL; CHEMBL1075165; -.
DrugBank; DB06836; N-(5-(4-CHLORO-3-(2-HYDROXY-ETHYLSULFAMOYL)- PHENYLTHIAZOLE-2-YL)-ACETAMIDE.
GuidetoPHARMACOLOGY; 2152; -.
SwissLipids; SLP:000000904; -.
iPTMnet; Q8NEB9; -.
PhosphoSitePlus; Q8NEB9; -.
BioMuta; PIK3C3; -.
DMDM; 74730233; -.
EPD; Q8NEB9; -.
jPOST; Q8NEB9; -.
MaxQB; Q8NEB9; -.
PaxDb; Q8NEB9; -.
PeptideAtlas; Q8NEB9; -.
PRIDE; Q8NEB9; -.
ProteomicsDB; 73147; -.
DNASU; 5289; -.
Ensembl; ENST00000262039; ENSP00000262039; ENSG00000078142.
GeneID; 5289; -.
KEGG; hsa:5289; -.
UCSC; uc002lap.4; human.
CTD; 5289; -.
DisGeNET; 5289; -.
EuPathDB; HostDB:ENSG00000078142.11; -.
GeneCards; PIK3C3; -.
HGNC; HGNC:8974; PIK3C3.
HPA; HPA040718; -.
MIM; 602609; gene.
neXtProt; NX_Q8NEB9; -.
OpenTargets; ENSG00000078142; -.
PharmGKB; PA33307; -.
eggNOG; KOG0906; Eukaryota.
eggNOG; COG5032; LUCA.
GeneTree; ENSGT00940000156943; -.
HOGENOM; HOG000174003; -.
HOVERGEN; HBG082145; -.
InParanoid; Q8NEB9; -.
KO; K00914; -.
OMA; VFADHEY; -.
OrthoDB; 1000890at2759; -.
PhylomeDB; Q8NEB9; -.
TreeFam; TF102032; -.
BioCyc; MetaCyc:HS01275-MONOMER; -.
BRENDA; 2.7.1.137; 2681.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-1660514; Synthesis of PIPs at the Golgi membrane.
Reactome; R-HSA-1660516; Synthesis of PIPs at the early endosome membrane.
Reactome; R-HSA-1660517; Synthesis of PIPs at the late endosome membrane.
Reactome; R-HSA-168138; Toll Like Receptor 9 (TLR9) Cascade.
Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
SIGNOR; Q8NEB9; -.
ChiTaRS; PIK3C3; human.
EvolutionaryTrace; Q8NEB9; -.
GeneWiki; PIK3C3; -.
GenomeRNAi; 5289; -.
PRO; PR:Q8NEB9; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000078142; Expressed in 230 organ(s), highest expression level in corpus callosum.
ExpressionAtlas; Q8NEB9; baseline and differential.
Genevisible; Q8NEB9; HS.
GO; GO:0044754; C:autolysosome; IDA:MGI.
GO; GO:0005930; C:axoneme; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; IBA:GO_Central.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IBA:GO_Central.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
GO; GO:0035032; C:phosphatidylinositol 3-kinase complex, class III; ISS:UniProtKB.
GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IBA:GO_Central.
GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IBA:GO_Central.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IMP:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0004672; F:protein kinase activity; IEA:Ensembl.
GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
GO; GO:0006914; P:autophagy; IMP:MGI.
GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; IBA:GO_Central.
GO; GO:0007032; P:endosome organization; IEA:Ensembl.
GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IBA:GO_Central.
GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
GO; GO:0006497; P:protein lipidation; IMP:MGI.
GO; GO:0034497; P:protein localization to phagophore assembly site; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
GO; GO:0016485; P:protein processing; IEA:Ensembl.
GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0050708; P:regulation of protein secretion; IEA:Ensembl.
GO; GO:0043201; P:response to leucine; IEA:Ensembl.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome.
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; IPR002420; PI3K_C2_dom.
InterPro; IPR008290; PI3K_Vps34.
InterPro; IPR015433; PI_Kinase.
InterPro; IPR001263; PInositide-3_kin_accessory_dom.
PANTHER; PTHR10048; PTHR10048; 1.
Pfam; PF00454; PI3_PI4_kinase; 1.
Pfam; PF00792; PI3K_C2; 1.
Pfam; PF00613; PI3Ka; 1.
PIRSF; PIRSF000587; PI3K_Vps34; 1.
SMART; SM00142; PI3K_C2; 1.
SMART; SM00145; PI3Ka; 1.
SMART; SM00146; PI3Kc; 1.
SUPFAM; SSF48371; SSF48371; 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; PS51547; PI3K_C2; 1.
PROSITE; PS51545; PIK_HELICAL; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Autophagy; Cell cycle; Cell division;
Complete proteome; Cytoplasmic vesicle; Endosome; Kinase; Manganese;
Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 887 Phosphatidylinositol 3-kinase catalytic
subunit type 3.
/FTId=PRO_0000088802.
DOMAIN 35 184 C2 PI3K-type. {ECO:0000255|PROSITE-
ProRule:PRU00880}.
DOMAIN 283 520 PIK helical. {ECO:0000255|PROSITE-
ProRule:PRU00878}.
DOMAIN 631 885 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
MOD_RES 163 163 Phosphothreonine; by AMPK.
{ECO:0000250|UniProtKB:Q6PF93}.
MOD_RES 165 165 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:Q6PF93}.
MOD_RES 244 244 Phosphoserine.
{ECO:0000250|UniProtKB:O88763}.
MOD_RES 261 261 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 282 282 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CONFLICT 36 36 K -> N (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 70 70 L -> S (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 136 136 F -> S (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 158 158 K -> N (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 208 208 E -> V (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 219 220 VE -> GG (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 262 262 M -> L (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 272 274 KLA -> NLP (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 289 292 NAAT -> YPSP (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 297 298 NI -> KN (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 305 308 TKQL -> SKPP (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 318 318 K -> E (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 327 327 E -> D (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 333 338 FLKCVN -> ILTSVI (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 344 344 E -> G (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 350 350 E -> A (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 356 356 K -> N (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 367 367 L -> I (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 397 397 L -> S (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 428 428 E -> G (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 484 484 C -> S (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 750 750 L -> V (in Ref. 1; CAA87094).
{ECO:0000305}.
CONFLICT 826 826 A -> P (in Ref. 1; CAA87094).
{ECO:0000305}.
HELIX 283 285 {ECO:0000244|PDB:3LS8}.
HELIX 290 300 {ECO:0000244|PDB:4UWH}.
STRAND 304 306 {ECO:0000244|PDB:4UWG}.
HELIX 310 318 {ECO:0000244|PDB:4UWH}.
HELIX 320 323 {ECO:0000244|PDB:4UWH}.
HELIX 327 329 {ECO:0000244|PDB:4UWH}.
HELIX 330 334 {ECO:0000244|PDB:4UWH}.
HELIX 342 352 {ECO:0000244|PDB:4UWH}.
HELIX 360 365 {ECO:0000244|PDB:4UWH}.
HELIX 374 384 {ECO:0000244|PDB:4UWH}.
HELIX 389 402 {ECO:0000244|PDB:4UWH}.
HELIX 403 405 {ECO:0000244|PDB:4UWH}.
HELIX 408 413 {ECO:0000244|PDB:4UWH}.
HELIX 437 439 {ECO:0000244|PDB:4UWH}.
HELIX 442 444 {ECO:0000244|PDB:4UWH}.
TURN 445 447 {ECO:0000244|PDB:4UWH}.
HELIX 475 485 {ECO:0000244|PDB:4UWH}.
HELIX 487 502 {ECO:0000244|PDB:4UWH}.
HELIX 504 509 {ECO:0000244|PDB:4UWH}.
HELIX 511 529 {ECO:0000244|PDB:4UWH}.
HELIX 533 561 {ECO:0000244|PDB:4UWH}.
HELIX 566 578 {ECO:0000244|PDB:4UWH}.
HELIX 580 583 {ECO:0000244|PDB:4UWH}.
STRAND 591 593 {ECO:0000244|PDB:4UWH}.
STRAND 596 604 {ECO:0000244|PDB:4UWH}.
HELIX 606 608 {ECO:0000244|PDB:4UWH}.
STRAND 613 616 {ECO:0000244|PDB:4PH4}.
STRAND 619 625 {ECO:0000244|PDB:4UWH}.
STRAND 630 639 {ECO:0000244|PDB:4UWH}.
HELIX 642 660 {ECO:0000244|PDB:4UWH}.
STRAND 672 683 {ECO:0000244|PDB:4UWH}.
HELIX 690 697 {ECO:0000244|PDB:4UWH}.
HELIX 700 707 {ECO:0000244|PDB:4UWH}.
STRAND 711 713 {ECO:0000244|PDB:4UWH}.
HELIX 714 716 {ECO:0000244|PDB:4UWH}.
HELIX 719 738 {ECO:0000244|PDB:4UWH}.
STRAND 748 751 {ECO:0000244|PDB:4UWH}.
STRAND 757 759 {ECO:0000244|PDB:4UWH}.
STRAND 770 773 {ECO:0000244|PDB:4UWH}.
HELIX 781 787 {ECO:0000244|PDB:4UWH}.
STRAND 790 792 {ECO:0000244|PDB:4UWF}.
HELIX 793 811 {ECO:0000244|PDB:4UWH}.
HELIX 813 821 {ECO:0000244|PDB:4UWH}.
TURN 822 825 {ECO:0000244|PDB:4UWH}.
HELIX 829 832 {ECO:0000244|PDB:4UWH}.
HELIX 835 837 {ECO:0000244|PDB:4UWH}.
HELIX 838 845 {ECO:0000244|PDB:4UWH}.
TURN 846 849 {ECO:0000244|PDB:4UWH}.
HELIX 852 872 {ECO:0000244|PDB:4UWH}.
SEQUENCE 887 AA; 101549 MW; 1C03D97338E44976 CRC64;
MGEAEKFHYI YSCDLDINVQ LKIGSLEGKR EQKSYKAVLE DPMLKFSGLY QETCSDLYVT
CQVFAEGKPL ALPVRTSYKA FSTRWNWNEW LKLPVKYPDL PRNAQVALTI WDVYGPGKAV
PVGGTTVSLF GKYGMFRQGM HDLKVWPNVE ADGSEPTKTP GRTSSTLSED QMSRLAKLTK
AHRQGHMVKV DWLDRLTFRE IEMINESEKR SSNFMYLMVE FRCVKCDDKE YGIVYYEKDG
DESSPILTSF ELVKVPDPQM SMENLVESKH HKLARSLRSG PSDHDLKPNA ATRDQLNIIV
SYPPTKQLTY EEQDLVWKFR YYLTNQEKAL TKFLKCVNWD LPQEAKQALE LLGKWKPMDV
EDSLELLSSH YTNPTVRRYA VARLRQADDE DLLMYLLQLV QALKYENFDD IKNGLEPTKK
DSQSSVSENV SNSGINSAEI DSSQIITSPL PSVSSPPPAS KTKEVPDGEN LEQDLCTFLI
SRACKNSTLA NYLYWYVIVE CEDQDTQQRD PKTHEMYLNV MRRFSQALLK GDKSVRVMRS
LLAAQQTFVD RLVHLMKAVQ RESGNRKKKN ERLQALLGDN EKMNLSDVEL IPLPLEPQVK
IRGIIPETAT LFKSALMPAQ LFFKTEDGGK YPVIFKHGDD LRQDQLILQI ISLMDKLLRK
ENLDLKLTPY KVLATSTKHG FMQFIQSVPV AEVLDTEGSI QNFFRKYAPS ENGPNGISAE
VMDTYVKSCA GYCVITYILG VGDRHLDNLL LTKTGKLFHI DFGYILGRDP KPLPPPMKLN
KEMVEGMGGT QSEQYQEFRK QCYTAFLHLR RYSNLILNLF SLMVDANIPD IALEPDKTVK
KVQDKFRLDL SDEEAVHYMQ SLIDESVHAL FAAVVEQIHK FAQYWRK


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