ID A0A671UF03_SPAAU Unreviewed; 884 AA.
AC A0A671UF03;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3 {ECO:0000256|ARBA:ARBA00019787, ECO:0000256|PIRNR:PIRNR000587};
DE EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073, ECO:0000256|PIRNR:PIRNR000587};
GN Name=PIK3C3 {ECO:0000313|Ensembl:ENSSAUP00010012332.1};
GN Synonyms=pik3c3 {ECO:0000313|Ensembl:ENSSAUP00010012332.1};
OS Sparus aurata (Gilthead sea bream).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Sparus.
OX NCBI_TaxID=8175 {ECO:0000313|Ensembl:ENSSAUP00010012332.1, ECO:0000313|Proteomes:UP000472265};
RN [1] {ECO:0000313|Ensembl:ENSSAUP00010012332.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSAUP00010012332.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSSAUP00010012332.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Midbody {ECO:0000256|ARBA:ARBA00004214}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR AlphaFoldDB; A0A671UF03; -.
DR Ensembl; ENSSAUT00010013107.1; ENSSAUP00010012332.1; ENSSAUG00010003198.1.
DR GeneTree; ENSGT00940000156943; -.
DR Proteomes; UP000472265; Chromosome 10.
DR GO; GO:0005768; C:endosome; IEA:TreeGrafter.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:TreeGrafter.
DR GO; GO:0000407; C:phagophore assembly site; IEA:TreeGrafter.
DR GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IEA:TreeGrafter.
DR GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IEA:TreeGrafter.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000045; P:autophagosome assembly; IEA:UniProtKB-ARBA.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:TreeGrafter.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:TreeGrafter.
DR CDD; cd08397; C2_PI3K_class_III; 1.
DR CDD; cd00870; PI3Ka_III; 1.
DR CDD; cd00896; PI3Kc_III; 1.
DR FunFam; 1.10.1070.11:FF:000002; Phosphatidylinositol 3-kinase catalytic subunit type 3; 1.
DR FunFam; 1.25.40.70:FF:000003; Phosphatidylinositol 3-kinase catalytic subunit type 3; 1.
DR FunFam; 2.60.40.150:FF:000043; Phosphatidylinositol 3-kinase catalytic subunit type 3; 1.
DR FunFam; 3.30.1010.10:FF:000002; Phosphatidylinositol 3-kinase catalytic subunit type 3; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR057756; PI3-kinase_type3/VPS34_cat.
DR InterPro; IPR015433; PI3/4_kinase.
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; IPR002420; PI3K-type_C2_dom.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR008290; PI3K_Vps34.
DR PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR PIRSF; PIRSF000587; PI3K_Vps34; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; PS51545; PIK_HELICAL; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000587};
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000587};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000472265};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 34..181
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 291..517
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 602..868
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 146..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..167
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 100659 MW; E4D7634053FFC621 CRC64;
METDKFNYVY SCDMDINVQL KIGSLEGKRE QKSYKALLED PMLRFSGLYQ ENCSDLYVTC
QVFAEGKPLA LPVRTSYKAF STRWNWNEWL RLPVKYPDLP QSAQVALTVW DIYGPGRAVP
VGGTTVTLFG KYGMFRQGMH DLKVWPGVEG DGGEPTTTPG RTSSSLTEDQ MGRLAKGPDL
EVLSDLTKAH RQGHMVKVDW LDRLTFREIE MINESEKRSS NFMYLMVEFP RVKTNDKEYS
IVYYEKDGDD SSPVLTSCDI VKVPDPQMGM ENLVESKHHK LARSLRSGPS DHDLKPNAAT
RDQLNIIVSY PPTKQLSSEE QDLVWKFRYY LTTQEKALTK FLKCVNWDLP QEAKQALELL
GKWRPMDVED SLELLSSQFT NPTVRRYAVA RLQQADDEDL LMYLLQLVQA LKYENFSDIQ
GGLEPGSKRD SQGLSDDSSM DSSQILSGTS GPSAAPQKGK EGADSENLEQ DLCTFLISRA
CKNSTLANYL YWYVIVECED QDTQQRDPKT HEMYLNVMRR FSQALLKGDK SVRVMRSLLA
AQQTFVDRLV QLMKAVQRES GNRKKKTERL QALLADNEKV NLSEIEPIPL PLEPQIRIRG
IVPETATLFK SALMPAKLIF KAEDGAMYPV IFKHGDDLRQ DQLILQIISL MDKLLRKENL
DLKLTPYKVL ATSTKHGFMQ FVQSVPVAEV LATEGNIQSF FRKHAPSEKG PYGISSEVMD
TYVKSCAGYC VITYILGVGD RHLDNLLLTK TGKLFHIDFG YILGRDPKPL PPPMKLSKEM
VEGMGGMQSE QYQEFRKQCY TAFLHLRRYS NLILNLFSLM VDANIPDIAL EPDKTVKKVQ
DKFRLDLSDE EAVHYMQSLI DESVGALFAA VVEQIHKFAQ YWRR
//
