ID F8VPL2_MOUSE Unreviewed; 1686 AA.
AC F8VPL2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 alpha {ECO:0000313|Ensembl:ENSMUSP00000126092.2};
GN Name=Pik3c2a {ECO:0000313|Ensembl:ENSMUSP00000126092.2,
GN ECO:0000313|MGI:MGI:1203729};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000126092.2, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:17114649}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000126092.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000126092.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000126092.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000126092.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR RefSeq; NP_035213.2; NM_011083.2.
DR RefSeq; XP_006507503.1; XM_006507440.3.
DR ProteomicsDB; 342768; -.
DR Antibodypedia; 24799; 786 antibodies from 34 providers.
DR DNASU; 18704; -.
DR Ensembl; ENSMUST00000170430.3; ENSMUSP00000126092.2; ENSMUSG00000030660.10.
DR Ensembl; ENSMUST00000206219.2; ENSMUSP00000146181.2; ENSMUSG00000030660.10.
DR GeneID; 18704; -.
DR KEGG; mmu:18704; -.
DR UCSC; uc009jjg.1; mouse.
DR AGR; MGI:1203729; -.
DR CTD; 5286; -.
DR MGI; MGI:1203729; Pik3c2a.
DR VEuPathDB; HostDB:ENSMUSG00000030660; -.
DR GeneTree; ENSGT00940000157813; -.
DR HOGENOM; CLU_002191_0_2_1; -.
DR OMA; HQWPALY; -.
DR OrthoDB; 10350at2759; -.
DR TreeFam; TF102031; -.
DR BioGRID-ORCS; 18704; 5 hits in 76 CRISPR screens.
DR ChiTaRS; Pik3c2a; mouse.
DR Proteomes; UP000000589; Chromosome 7.
DR Bgee; ENSMUSG00000030660; Expressed in metanephric proximal tubule and 245 other cell types or tissues.
DR Genevisible; F8VPL2; MM.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:Ensembl.
DR GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:Ensembl.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0030276; F:clathrin binding; IEA:Ensembl.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
DR CDD; cd04012; C2A_PI3K_class_II; 1.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd00869; PI3Ka_II; 1.
DR CDD; cd05176; PI3Kc_C2_alpha; 1.
DR CDD; cd07289; PX_PI3K_C2_alpha; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR037705; PI3K-C2-alpha_dom.
DR InterPro; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR042133; PX_PI3K_C2_alpha.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF28; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 3-KINASE C2 DOMAIN-CONTAINING SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Proteomics identification {ECO:0007829|EPD:F8VPL2,
KW ECO:0007829|MaxQB:F8VPL2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 422..510
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 682..841
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 861..1037
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1105..1383
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1422..1538
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1559..1678
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1686 AA; 190744 MW; E390BA02ED774987 CRC64;
MAQISNNSEF KQCSSSHPEP IRTKDVNKAE ALQMEAEALA KLQKDRQMTD SPRGFELSSS
TRQRTQGFNK QDYDLMVFPE LDSQKRAVDI DVEKLTQAEL EKILLDDNFE TRKPPALPVT
PVLSPSFSTQ LYLRPSGQRG QWPPGLCGPS TYTLPSTYPS AYSKQATFQN GFSPRMPTFP
STESVYLRLP GQSPYFSYPL TPATPFHPQG SLPVYRPLVS PDMAKLFEKI ASTSEFLKNG
KARTDLEIAN SKASVCNLQI SPKSEDINKF DWLDLDPLSK PKVDYVEVLE HEEEKKDPVL
LAEDPWDAVL LEERSPSCHL ERKVNGKSLS GATVTRSQSL IIRTAQFTKA QGQVSQKDPN
GTSSLPTGSS LLQEFEVQND EVAAFCQSIM KLKTKFPYTD HCTNPGYLLS PVTVQRNMCG
ENASVKVSIE IEGLQLPVTF TCDVSSTVEI IIMQALCWVH DDLNQVDVGS YILKVCGQEE
VLQNNHCLGS HEHIQNCRKW DTEIKLQLLT LSAMCQNLAR TAEDDEAPVD LNKYLYQIEK
PYKEVMTRHP VEELLDSYHY QVELALQTEN QHRAVDQVIK AVRKICSALD GVETPSVTEA
VKKLKRAVNL PRNKSADVTS LSGSDTRKNS TKGSLNPENP VQVSMDHLTT AIYDLLRLHA
NSSRCSTGCP RGSRNIKEAW TATEQLQFTV YAAHGISSNW VSNYEKYYLI CSLSHNGKDL
FKPIQSKKVG TYKNFFYLIK WDELIIFPIQ ISQLPLESVL HLTLFGVLNQ SSGSSPDSNK
QRKGPEALGK VSLTLFDFKR FLTCGTKLLY LWTSSHTNSI PGAIPKKSYV MERIVLQVDF
PSPAFDIIYT SPQIDRNIIQ QDKLETLESD IKGKLLDIIH RDSSFGLSKE DKVFLWENRY
YCLKHPNCLP KILASAPNWK WANLAKTYSL LHQWPPLCPL AALELLDAKF ADQEVRSLAV
SWMEAISDDE LADLLPQFVQ ALKYEIYLNS SLVRFLLSRA LGNIQIAHSL YWLLKDALHD
THFGSRYEHV LGALLSVGGK GLREELSKQM KLVQLLGGVA EKVRQASGST RQVVLQKSME
RVQSFFLRNK CRLPLKPSLV AKELNIKSCS FFSSNAMPLK VTMVNADPLG EEINVMFKVG
EDLRQDMLAL QMIKIMDKIW LKEGLDLRMV IFRCLSTGRD RGMVELVPAS DTLRKIQVEY
GVTGSFKDKP LAEWLRKYNP SEEEYEKASE NFIYSCAGCC VATYVLGICD RHNDNIMLRS
TGHMFHIDFG KFLGHAQMFG SFKRDRAPFV LTSDMAYVIN GGEKPTIRFQ LFVDLCCQAY
NLIRKQTNLF LNLLSLMIPS GLPELTSIQD LKYVRDALQP QTTDAEATIF FTRLIESSLG
SIATKFNFFI HNLAQLRFSG LPSNDEPILS FSPKTYSFRQ DGRIKEVSVF TYHKKYNPDK
HYIYVVRILR EGHLEPSFVF RTFDEFQELH NKLSIIFPLW KLPGFPNRMV LGRTHIKDVA
AKRKIELNSY LQSLMNASTD VAECDLVCTF FHPLLRDEKA EGIARSAGAV PFSPTLGQIG
GAVKLSVSYR NGTLFIMVMH IKDLVTEDGA DPNPYVKTYL LPDTHKTSKR KTKISRKTRN
PTFNEMLVYS GYSKETLRQR ELQLSVLSAE SLRENFFLGG ITLPLKDFNL SKETVKWYQL
TAATYL
//
