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

 PK3C3_CAEEL             Reviewed;         901 AA.
Q9TXI7; Q5TYK9; Q9TXI6; Q9XZR0;
11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-MAR-2018, entry version 150.
RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3 {ECO:0000250|UniProtKB:Q8NEB9};
Short=PI3-kinase type 3 {ECO:0000250|UniProtKB:Q8NEB9};
Short=PI3K type 3 {ECO:0000250|UniProtKB:Q8NEB9};
EC=2.7.1.137 {ECO:0000255|PIRNR:PIRNR000587, ECO:0000269|PubMed:11927551};
AltName: Full=Phosphoinositide-3-kinase class 3 {ECO:0000250|UniProtKB:Q8NEB9};
Name=vps-34 {ECO:0000312|WormBase:B0025.1a};
Synonyms=let-512 {ECO:0000312|WormBase:B0025.1a};
ORFNames=B0025.1 {ECO:0000312|WormBase:B0025.1a};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|EMBL:CAA73142.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND DEVELOPMENTAL STAGE.
PubMed=11927551; DOI=10.1093/emboj/21.7.1673;
Roggo L., Bernard V., Kovacs A.L., Rose A.M., Savoy F., Zetka M.,
Wymann M.P., Mueller F.;
"Membrane transport in Caenorhabditis elegans: an essential role for
VPS34 at the nuclear membrane.";
EMBO J. 21:1673-1683(2002).
[2] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3] {ECO:0000305}
FUNCTION, AND INTERACTION WITH BEC-1.
PubMed=16111945; DOI=10.1016/j.cub.2005.07.035;
Takacs-Vellai K., Vellai T., Puoti A., Passannante M., Wicky C.,
Streit A., Kovacs A.L., Mueller F.;
"Inactivation of the autophagy gene bec-1 triggers apoptotic cell
death in C. elegans.";
Curr. Biol. 15:1513-1517(2005).
[4] {ECO:0000305}
FUNCTION.
PubMed=15843430; DOI=10.1091/mbc.E05-01-0060;
Hermann G.J., Schroeder L.K., Hieb C.A., Kershner A.M., Rabbitts B.M.,
Fonarev P., Grant B.D., Priess J.R.;
"Genetic analysis of lysosomal trafficking in Caenorhabditis
elegans.";
Mol. Biol. Cell 16:3273-3288(2005).
[5] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DYN-1, AND DISRUPTION
PHENOTYPE.
PubMed=18425118; DOI=10.1038/ncb1718;
Kinchen J.M., Doukoumetzidis K., Almendinger J., Stergiou L.,
Tosello-Trampont A., Sifri C.D., Hengartner M.O., Ravichandran K.S.;
"A pathway for phagosome maturation during engulfment of apoptotic
cells.";
Nat. Cell Biol. 10:556-566(2008).
[6] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21183797; DOI=10.4161/auto.7.4.14391;
Ruck A., Attonito J., Garces K.T., Nunez L., Palmisano N.J., Rubel Z.,
Bai Z., Nguyen K.C., Sun L., Grant B.D., Hall D.H., Melendez A.;
"The Atg6/Vps30/Beclin 1 ortholog BEC-1 mediates endocytic retrograde
transport in addition to autophagy in C. elegans.";
Autophagy 7:386-400(2011).
[7] {ECO:0000305}
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22272187; DOI=10.1371/journal.pbio.1001245;
Lu N., Shen Q., Mahoney T.R., Neukomm L.J., Wang Y., Zhou Z.;
"Two PI 3-kinases and one PI 3-phosphatase together establish the
cyclic waves of phagosomal PtdIns(3)P critical for the degradation of
apoptotic cells.";
PLoS Biol. 10:E1001245-E1001245(2012).
[8]
INTERACTION WITH BEC-1.
PubMed=26783301; DOI=10.1083/jcb.201506081;
Liu K., Jian Y., Sun X., Yang C., Gao Z., Zhang Z., Liu X., Li Y.,
Xu J., Jing Y., Mitani S., He S., Yang C.;
"Negative regulation of phosphatidylinositol 3-phosphate levels in
early-to-late endosome conversion.";
J. Cell Biol. 212:181-198(2016).
[9]
ERRATUM.
PubMed=26975852; DOI=10.1083/jcb.20150608103012016c;
Liu K., Jian Y., Sun X., Yang C., Gao Z., Zhang Z., Liu X., Li Y.,
Xu J., Jing Y., Mitani S., He S., Yang C.;
"Correction: Negative regulation of phosphatidylinositol 3-phosphate
levels in early-to-late endosome conversion.";
J. Cell Biol. 212:739-739(2016).
-!- FUNCTION: Catalytic subunit of the PI3K complex that mediates
formation of phosphatidylinositol 3-phosphate (PubMed:11927551).
Together with bec-1, mediates the production of
phosphatidylinositol 3-phosphate on intracellular vesicles and
thereby regulates membrane trafficking (PubMed:11927551,
PubMed:16111945). Plays a role in endosome-to-Golgi retrograde
transport of mig-14 (PubMed:21183797). Involved in clearance of
apoptotic cell corpses by phagosomes (PubMed:22272187). Phagosome
maturation requires two sequential and non-overlapping pulses of
phosphatidylinositol-3-phosphate (PI3P) on the vesicle surface
which mediates recruitment of sortins snx-1 and lst-4 and small
GTPases rab-5, rab-2 and rab-7, downstream of dynamin dyn-1
(PubMed:22272187, PubMed:18425118). The first pulse is initiated
by piki-1, then maintained by vps-34 which also produces the
second pulse (PubMed:22272187). Required for embryonic development
(PubMed:22272187). Together with bec-1, involved in L3/L4 larval
molting stage probably by regulating cuticle shedding
(PubMed:11927551). Regulates the expansion of the nucleus outer
membrane (PubMed:11927551). Involved in the secretion and
localization of lrp-1 at the apical surface of hyp7 syncytium
(PubMed:16111945). May regulate endocytosis in hypodermal cells
(PubMed:11927551). May play a role in the formation of gut
granules (a lysosome-related organelle) (PubMed:15843430).
{ECO:0000269|PubMed:11927551, ECO:0000269|PubMed:15843430,
ECO:0000269|PubMed:16111945, ECO:0000269|PubMed:18425118,
ECO:0000269|PubMed:21183797, ECO:0000269|PubMed:22272187}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
1-phosphatidyl-1D-myo-inositol 3-phosphate.
{ECO:0000255|PIRNR:PIRNR000587, ECO:0000269|PubMed:11927551}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:11927551};
-!- ENZYME REGULATION: Inhibited by wortmannin.
{ECO:0000269|PubMed:11927551}.
-!- SUBUNIT: Interacts with bec-1 (PubMed:16111945, PubMed:26783301).
May interact with dyn-1 (PubMed:18425118).
{ECO:0000269|PubMed:16111945, ECO:0000269|PubMed:26783301,
ECO:0000305|PubMed:18425118}.
-!- SUBCELLULAR LOCATION: Nucleus outer membrane
{ECO:0000269|PubMed:11927551}; Peripheral membrane protein
{ECO:0000269|PubMed:11927551}. Cytoplasm
{ECO:0000269|PubMed:11927551}. Cytoplasmic granule
{ECO:0000269|PubMed:11927551}. Cell projection, phagocytic cup
{ECO:0000269|PubMed:18425118}. Note=Colocalizes with rab-5 and
dyn-1 at the phagocytic cup. {ECO:0000269|PubMed:18425118}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a {ECO:0000312|WormBase:B0025.1a};
IsoId=Q9TXI7-1; Sequence=Displayed;
Note=No experimental confirmation available. {ECO:0000305};
Name=b {ECO:0000312|WormBase:B0025.1b};
IsoId=Q9TXI7-2; Sequence=VSP_058340;
Note=No experimental confirmation available. {ECO:0000305};
Name=c {ECO:0000312|WormBase:B0025.1c};
IsoId=Q9TXI7-3; Sequence=VSP_058341;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11927551}.
-!- DEVELOPMENTAL STAGE: Highly expressed in embryos and at L2 larval
stage, and to a lower extent in subsequent larval stages and in
adults. {ECO:0000269|PubMed:11927551}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a defect in
the clearance of apoptotic cell corpses in gonads, a loss of rab-5
recruitment to cell corpse-containing nascent phagosomes and a
decrease in PI3P levels on phagosome membranes (PubMed:18425118,
PubMed:22272187). In addition, causes a reduction in mig-14 and
rme-8 association with puncta structures as well as an increase in
mig-14 protein levels (PubMed:21183797).
{ECO:0000269|PubMed:18425118, ECO:0000269|PubMed:21183797,
ECO:0000269|PubMed:22272187}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
{ECO:0000255|PIRNR:PIRNR000587}.
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EMBL; Y12543; CAA73142.1; -; mRNA.
EMBL; BX284601; CCD61194.1; -; Genomic_DNA.
EMBL; BX284601; CCD61195.1; -; Genomic_DNA.
EMBL; BX284601; CCD61196.1; -; Genomic_DNA.
PIR; T43628; T43628.
RefSeq; NP_001020953.1; NM_001025782.2. [Q9TXI7-2]
RefSeq; NP_001020954.1; NM_001025783.2. [Q9TXI7-3]
RefSeq; NP_491741.1; NM_059340.4. [Q9TXI7-1]
UniGene; Cel.6170; -.
ProteinModelPortal; Q9TXI7; -.
SMR; Q9TXI7; -.
STRING; 6239.B0025.1a; -.
EPD; Q9TXI7; -.
PaxDb; Q9TXI7; -.
PeptideAtlas; Q9TXI7; -.
EnsemblMetazoa; B0025.1a; B0025.1a; WBGene00006932. [Q9TXI7-1]
GeneID; 172280; -.
KEGG; cel:CELE_B0025.1; -.
UCSC; B0025.1b.2; c. elegans.
CTD; 172280; -.
WormBase; B0025.1a; CE24759; WBGene00006932; vps-34. [Q9TXI7-1]
WormBase; B0025.1b; CE24760; WBGene00006932; vps-34. [Q9TXI7-2]
WormBase; B0025.1c; CE37691; WBGene00006932; vps-34. [Q9TXI7-3]
eggNOG; KOG0906; Eukaryota.
eggNOG; COG5032; LUCA.
GeneTree; ENSGT00760000119110; -.
HOGENOM; HOG000174003; -.
InParanoid; Q9TXI7; -.
KO; K00914; -.
OMA; FKKHEMG; -.
OrthoDB; EOG091G036A; -.
PhylomeDB; Q9TXI7; -.
Reactome; R-CEL-1632852; Macroautophagy.
Reactome; R-CEL-1660514; Synthesis of PIPs at the Golgi membrane.
Reactome; R-CEL-1660516; Synthesis of PIPs at the early endosome membrane.
Reactome; R-CEL-1660517; Synthesis of PIPs at the late endosome membrane.
Reactome; R-CEL-5668599; RHO GTPases Activate NADPH Oxidases.
SignaLink; Q9TXI7; -.
PRO; PR:Q9TXI7; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00006932; -.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0005768; C:endosome; IBA:GO_Central.
GO; GO:0005640; C:nuclear outer membrane; IDA:WormBase.
GO; GO:0005730; C:nucleolus; IDA:WormBase.
GO; GO:0005777; C:peroxisome; IBA:GO_Central.
GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
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; IDA:WormBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
GO; GO:0042395; P:ecdysis, collagen and cuticulin-based cuticle; IMP:WormBase.
GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
GO; GO:0002119; P:nematode larval development; IMP:WormBase.
GO; GO:0006998; P:nuclear envelope organization; IMP:WormBase.
GO; GO:0090386; P:phagosome maturation involved in apoptotic cell clearance; IMP:WormBase.
GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IMP:WormBase.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:WormBase.
GO; GO:0061365; P:positive regulation of triglyceride lipase activity; IMP:WormBase.
GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
GO; GO:0030100; P:regulation of endocytosis; IMP:WormBase.
GO; GO:0051036; P:regulation of endosome size; IGI:UniProtKB.
GO; GO:0050708; P:regulation of protein secretion; IMP:WormBase.
GO; GO:0000003; P:reproduction; IMP:WormBase.
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; 2.
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; 2.
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;
Alternative splicing; ATP-binding; Cell projection; Complete proteome;
Cytoplasm; Endocytosis; Kinase; Lipid biosynthesis; Lipid metabolism;
Membrane; Nucleotide-binding; Nucleus; Phagocytosis;
Reference proteome; Transferase.
CHAIN 1 901 Phosphatidylinositol 3-kinase catalytic
subunit type 3. {ECO:0000305}.
/FTId=PRO_0000436297.
DOMAIN 21 189 C2 PI3K-type. {ECO:0000255|PROSITE-
ProRule:PRU00880}.
DOMAIN 302 527 PIK helical. {ECO:0000255|PROSITE-
ProRule:PRU00878}.
DOMAIN 642 900 PI3K/PI4K. {ECO:0000255|PROSITE-
ProRule:PRU00269}.
VAR_SEQ 1 251 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_058340.
VAR_SEQ 1 4 Missing (in isoform c). {ECO:0000305}.
/FTId=VSP_058341.
CONFLICT 8 8 T -> R (in Ref. 1; CAA73142).
{ECO:0000305}.
CONFLICT 180 180 D -> H (in Ref. 1; CAA73142).
{ECO:0000305}.
CONFLICT 220 220 P -> A (in Ref. 1; CAA73142).
{ECO:0000305}.
CONFLICT 516 516 E -> A (in Ref. 1; CAA73142).
{ECO:0000305}.
CONFLICT 526 526 D -> H (in Ref. 1; CAA73142).
{ECO:0000305}.
CONFLICT 530 530 E -> D (in Ref. 1; CAA73142).
{ECO:0000305}.
CONFLICT 641 641 E -> A (in Ref. 1; CAA73142).
{ECO:0000305}.
CONFLICT 715 715 C -> R (in Ref. 1; CAA73142).
{ECO:0000305}.
SEQUENCE 901 AA; 103059 MW; 3B490B64FD3F5E78 CRC64;
MIPGMRATPT ESFSFVYSCD LQTNVQVKVA EFEGIFRDVL NPVRRLNQLF AEITVYCNNQ
QIGYPVCTSF HTPPDSSQLA RQKLIQKWNE WLTLPIRYSD LSRDAFLHIT IWEHEDDEIV
NNSTFSRRLV AQSKLSMFSK RGILKSGVID VQMNVSTTPD PFVKQPETWK YSDAWGDEID
LLFKQVTRQS RGLVEDVPWL DPFASRRIEM IRAKYKYSSP DRHVFLVLEM AAIRLGPTFY
KVVYYEDETK NMRVSTSVNG GVGIVSACTR YCVADPELLL ESLAEVKHSA MTRRIRDVED
ERHRQVKPNK QAKDRLETIV NLPSSQVLTR EQRDLVWKFR HYLRQFPKAL NKYLRSVNWV
HPQEVKTALA LMNDWELIEA EDALELLSSA FTHPAVRAYS VSRLLEAASP EQVLLYLPQL
VQALKYEQGQ QLPEEGNPVP VVSEEEGKIP SVATTPTEEL EGRDMTVVTK KEARKAASGD
LATFLIDYAL ASPKVSNYLY WHLKTEIEST KESKEEHSKM YQNIQDRLME ALVKRPDTRA
QVDSLHQQQI FVEDLIILMN EAKARGGRLN ESKSAEFRTM LSRAKHMLDL KGVHLPLDPS
FRLSSVIPDT ASFFKSEMMP AKISFKVLQP NGKADRNIPE EYTVIFKTGD DLRQDQLIQQ
MVRLIDIILK KGQLDLKLTP YLVLSTGVGQ GFVQCIKSKP LRAIQEQYKA HKMDCIREAM
KELRPGDGPF GIEPNVIDNY VRSLAGYSVI MYILGLGDRH LDNLLLCENG KLFHVDFGFI
LGRDPKPMPP PMKLTSEMVQ VMGGVKSKQF LEFVQHVDSA YRILRRHSNV LLNLFSLMLD
AGIPDIAAEP DKAIFKIEQR LRLDLSDEAA TKHIFTQIES SLNAKMAMIS DIIHAYKQNL
M


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CSB-EL017997RA Rat Phosphatidylinositol 3-kinase catalytic subunit type 3(PIK3C3) ELISA kit 96T
E1898h Mouse ELISA Kit FOR Phosphatidylinositol 3-kinase catalytic subunit type 3 96T


 

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