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Database: UniProt
Entry: A0A3Q1IZ07_ANATE
LinkDB: A0A3Q1IZ07_ANATE
Original site: A0A3Q1IZ07_ANATE 
ID   A0A3Q1IZ07_ANATE        Unreviewed;       813 AA.
AC   A0A3Q1IZ07;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Phosphatidylinositol 4-kinase beta {ECO:0000256|ARBA:ARBA00039877};
DE            EC=2.7.1.67 {ECO:0000256|ARBA:ARBA00012169};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000025765.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000025765.2}
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 4-phosphate) + ADP +
CC         H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC         EC=2.7.1.67; Evidence={ECO:0000256|ARBA:ARBA00036767};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC         Evidence={ECO:0000256|ARBA:ARBA00036767};
CC   -!- SUBCELLULAR LOCATION: Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00004308}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004406}. Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004450}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004450}. Rough endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00037860}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00037860}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC       subfamily. {ECO:0000256|ARBA:ARBA00006209}.
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DR   AlphaFoldDB; A0A3Q1IZ07; -.
DR   Ensembl; ENSATET00000026183.2; ENSATEP00000025765.2; ENSATEG00000017861.2.
DR   GeneTree; ENSGT00550000074892; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05168; PI4Kc_III_beta; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
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; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR049160; PI4KB-PIK1_PIK.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          36..245
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          532..798
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          23..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   813 AA;  91528 MW;  F787EAA0CB376972 CRC64;
     LTYLTSHRSS VSVGRWCLPA TMMEDTEPEP SPTPSDQNSP SGVGELSLVI NAEVAQRACQ
     EVLQKVKLQQ VEGDDTHLQN GPGPESETPS ALASAMKQPK IREEEDDPEG SAPCSVKSAR
     RRQRHNPSKQ SWLLRLFESK LFDVSMAISY LHNSKEPGVQ AYIGNRLFSF PHEEVDFYLP
     QLLNMYIHMD EDVGDAIKPY VVHRCRQSIS FSLQCAWLLG AYSSDMHIST QRHSRGTKLR
     KLILSDELKP AGPRARRDPL TLTPFYHGLS PSKRTHQRSK SDATVSISLS SNLKRTASNP
     KVESSQDEVT QQSLNPVRLA PQREFIKSLM GIGKRLATLP TKEQKTSRLI SELSLLNHKL
     PSRVWLPTAA FDHHVVRVPH TQAVVLNSKD KAPYLIYVEV LECDNFETSS VPIRIPENRI
     RSTRSVENLP DCGITAEQRA GSFSVVPNYD NDDEAWSVDD IGDLQVELPE VHTNSCDNIS
     QFSVDSITSL ESKEPVFIAA GDIRRRLSEQ LAQAPTTFKR DPEDPSAVAL KEPWEEKVRR
     IREGSPYGHL PNWRLLSVIV KCGDDLRQEL LAFQVLQQLK SIWEQERVPL WIKPYKILVL
     SSDSGMIEPV VNAVSLHQVK KQSQLSLLDY FLQEHGAPTT EAFLSAQRNF VQSCAGYSLI
     CYLLQVKDRH NGNILLDADG HIIHIDFGFI LSSSPKNLGF ETSAFKLTSE FVDVMGGPDG
     DMFNYYKMLM LQGLIAARKH MDRVLQIVEI MQQGSQLPCF HGSSTMRALK ERFHMSLTEE
     QLQLLVDQLV DGSMRSLTTK LYDGFQYLTN GIM
//
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