ID A0A3Q1FZN2_9TELE Unreviewed; 875 AA.
AC A0A3Q1FZN2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000011725.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000011725.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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|PIRNR:PIRNR000587};
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; A0A3Q1FZN2; -.
DR STRING; 80966.ENSAPOP00000011725; -.
DR Ensembl; ENSAPOT00000019382.1; ENSAPOP00000011725.1; ENSAPOG00000014440.1.
DR GeneTree; ENSGT00940000156943; -.
DR InParanoid; A0A3Q1FZN2; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd08397; C2_PI3K_class_III; 1.
DR CDD; cd00870; PI3Ka_III; 1.
DR CDD; cd00896; PI3Kc_III; 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; 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; 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 InterPro; IPR015433; PI_Kinase.
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|PIRNR:PIRNR000587};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000587};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000587}.
FT DOMAIN 34..183
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 282..508
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 593..859
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT REGION 147..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 875 AA; 99712 MW; 83EE024B8C669CC7 CRC64;
MDTDKFNYVY SCDMDINVQL KIGSLEGKRE QRSYKALLED PMLRFSGLYQ ENCSDLYVTC
QVFAEGKPLA LPVRTSYKAF STRWNWNEWL RLPVKYPDLP QSAQVALTVW DIYGPGRAVP
VGGTTVTLFG KYGMFRQGMH DLKVWPGVEG DGGEPTTTPG RTSSSLAEDQ MGRLAKLTKA
HRQGHMVKVD WLDRLTFREI EMINESEKRS SNFMYLMVEF PRVKTNDKEY SIVYYEKDGD
DASPVLTSCD IVKVPDPQMG MENLVESKHH KLARSLRSGP SDHDLKPNAA TRDQLNIIVS
YPPTKQLSSE EQDLVWKFRY YLTTQEKALT KFLKCVNWDL PQEAKQALEL LGKWRPMDVE
DSLELLSSHF TNPTVRRYAV ARLQQADDED LLMYLLQLVQ ALKYENFSDI QGGLEPGSKR
DSQGLSDDST LDSSQILSGS SGSSTAPQKG KEGADSENLE QDLCTFLISR ACKNSTLANY
LYWYVIVECE DQDTQQRDPK THEMYLNVMR RFSQALLKGD KSVRVMRSLL AAQQTFVDRL
VQLMKAVQRE SGNRKKKTER LQALLADNEK VNLSEIEPIP LPLEPQIRIR GIVPETATLF
KSALMPAKLI FKAEDGAMYP VIFKHGDDLR QDQLILQIIS LMDKLLRKEN LDLKLTPYKV
LATSTKHGFM QFVQSVPVAE VLATEGNIQS FFRKHAPSEK GPYGISSEVM DTYVKSCAGY
CVITYILGVG DRHLDNLLLT KTGKLFHIDF GYILGRDPKP LPPPMKLSKE MVEGMGGMQS
EQYQEFRKQC YTAFLHLRRY SNLILNLFSL MVDANIPDIA LEPDKTVKKV QDKFRLDLSD
EEAVHYMQSL IDESVGALFA AVVEQIHKFA QYWRR
//
