PI4KB_BOVIN
ID PI4KB_BOVIN Reviewed; 816 AA.
AC O02810;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Phosphatidylinositol 4-kinase beta;
DE Short=PI4K-beta;
DE Short=PI4Kbeta;
DE Short=PtdIns 4-kinase beta;
DE EC=2.7.1.67 {ECO:0000269|PubMed:11526106, ECO:0000269|PubMed:9218477};
GN Name=PI4KB; Synonyms=PIK4CB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000312|EMBL:AAC48729.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 153-158;
RP 298-303; 319-321; 327-330; 339-345; 497-507; 510-522 AND 581-589, FUNCTION,
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC TISSUE=Adrenal cortex {ECO:0000269|PubMed:9218477};
RX PubMed=9218477; DOI=10.1074/jbc.272.29.18358;
RA Balla T., Downing G.J., Jaffe H., Kim S., Zolyomi A., Catt K.J.;
RT "Isolation and molecular cloning of wortmannin-sensitive bovine type III
RT phosphatidylinositol 4-kinases.";
RL J. Biol. Chem. 272:18358-18366(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH NCS1, ACTIVITY REGULATION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=11526106; DOI=10.1074/jbc.m104048200;
RA Zhao X., Varnai P., Tuymetova G., Balla A., Toth Z.E., Oker-Blom C.,
RA Roder J., Jeromin A., Balla T.;
RT "Interaction of neuronal calcium sensor-1 (NCS-1) with phosphatidylinositol
RT 4-kinase beta stimulates lipid kinase activity and affects membrane
RT trafficking in COS-7 cells.";
RL J. Biol. Chem. 276:40183-40189(2001).
CC -!- FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first
CC committed step in the production of the second messenger inositol-
CC 1,4,5,-trisphosphate (PIP) (PubMed:9218477, PubMed:11526106). May
CC regulate Golgi disintegration/reorganization during mitosis, possibly
CC via its phosphorylation (By similarity). Involved in Golgi-to-plasma
CC membrane trafficking (By similarity). {ECO:0000250|UniProtKB:O08561,
CC ECO:0000250|UniProtKB:Q9UBF8, ECO:0000269|PubMed:11526106,
CC ECO:0000269|PubMed:9218477}.
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:0000269|PubMed:11526106,
CC ECO:0000269|PubMed:9218477};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC Evidence={ECO:0000305|PubMed:9218477};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9UBF8};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9UBF8};
CC -!- ACTIVITY REGULATION: Inhibited by wortmannin. Increased kinase activity
CC upon interaction with NCS1/FREQ. {ECO:0000269|PubMed:11526106,
CC ECO:0000269|PubMed:9218477}.
CC -!- SUBUNIT: Interacts with ARF1 and ARF3 in the Golgi complex, but not
CC with ARF4, ARF5 or ARF6 (By similarity). Interacts with NCS1/FREQ in a
CC calcium-independent manner. Interacts with CALN1/CABP8 and CALN2/CABP7;
CC in a calcium-dependent manner; this interaction competes with NCS1/FREQ
CC binding (PubMed:11526106). Interacts with ACBD3. Interacts with ARMH3,
CC YWHAB, YWHAE, YWHAG, YWHAH, YWHAQ, YWHAZ and SFN (By similarity).
CC Interacts with GGA2 (via VHS domain); the interaction is important for
CC PI4KB location at the Golgi apparatus membrane (By similarity).
CC Interacts with ATG9A (By similarity). {ECO:0000250|UniProtKB:Q9UBF8,
CC ECO:0000269|PubMed:11526106}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Mitochondrion
CC outer membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Golgi apparatus
CC {ECO:0000269|PubMed:11526106}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9UBF8}. Note=Found in the outer membrane of
CC mitochondria and membranes of the rough endoplasmic reticulum.
CC Recruited to the Golgi complex by the small GTPase ARF to stimulate the
CC synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi
CC complex. Recruited to the Golgi apparatus membrane by ACBD3, GGA2 is
CC also involved in the recruitment. {ECO:0000250|UniProtKB:Q9UBF8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:9218477};
CC IsoId=O02810-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9218477};
CC IsoId=O02810-2; Sequence=VSP_050628;
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; U88531; AAC48729.1; -; mRNA.
DR RefSeq; NP_777208.1; NM_174783.2. [O02810-2]
DR PDB; 5EUQ; X-ray; 3.20 A; E=288-422.
DR PDBsum; 5EUQ; -.
DR AlphaFoldDB; O02810; -.
DR SMR; O02810; -.
DR STRING; 9913.ENSBTAP00000009627; -.
DR PaxDb; O02810; -.
DR PRIDE; O02810; -.
DR GeneID; 286846; -.
DR KEGG; bta:286846; -.
DR CTD; 5298; -.
DR eggNOG; KOG0903; Eukaryota.
DR InParanoid; O02810; -.
DR OrthoDB; 1147978at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1070.11; -; 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; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; SSF56112; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus; Kinase;
KW Lipid metabolism; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT CHAIN 2..816
FT /note="Phosphatidylinositol 4-kinase beta"
FT /id="PRO_0000088828"
FT DOMAIN 29..242
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 535..801
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..68
FT /note="Interaction with ACBD3"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT REGION 101..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..547
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 668..676
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 687..711
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 277..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 263
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKC8"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKC8"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 517
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 519
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT VAR_SEQ 304..318
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9218477"
FT /id="VSP_050628"
FT HELIX 323..337
FT /evidence="ECO:0007829|PDB:5EUQ"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:5EUQ"
FT HELIX 345..357
FT /evidence="ECO:0007829|PDB:5EUQ"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:5EUQ"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:5EUQ"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:5EUQ"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:5EUQ"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:5EUQ"
FT STRAND 397..405
FT /evidence="ECO:0007829|PDB:5EUQ"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:5EUQ"
SQ SEQUENCE 816 AA; 91375 MW; 4388D127636B500A CRC64;
MGDTIVEPAP LKPTSEPAPG PPGNNGGSLL SVITEGVGEL SVIDPEVAQK ACQEVLEKVK
LLHGGVAISS RGTPLELVNG DGVDSEIRCL DDPPAQIREE EDEMGATVAS GTAKGARRRR
QNNSAKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL
NMYIHMDEDV GDAIKPYIVH RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI
LSDELKPAHR KRELPSLSPA PDTGLSPSKR THQRSKSDAT ASISLSSNLK RTASNPKVEN
EDEELSSSTE SIDNSFSSPV RLAPEREFIK SLMAIGKRLA TLPTKEQKTQ RLISELSLLN
HKLPARVWLP TAGFDHHVVR VPHTQAVVLN SKDKAPYLIY VEVLECENFD TTSVPARIPE
NRIRSTRSVE NLPECGITHE QRAGSFSTVP NYDNDDEAWS VDDIGELQVE LPEVHTNSCD
NISQFSVDSI TSQESKEPVF IAAGDIRRRL SEQLAHTPTA FKRDPEDPSA VALKEPWQEK
VRRIREGSPY GHLPNWRLLS VIVKCGDDLR QELLAFQVLK QLQSIWEQER VPLWIKPYKI
LVISADSGMI EPVVNAVSIH QVKKQSQLSL LDYFLQEHGS YTTEAFLSAQ RNFVQSCAGY
CLGCYLLQVK DRHNGNILLD AEGHIIHIDF GFILSSSPRN LGFETSAFKL TTEFVDVMGG
LDGDMFNYYK MLMLQGLIAA RKHMDKVVQI VEIMQQGSQL PCFHGSSTIR NLKERFHMSM
TEEQLQLLVE QMVDGSMRSI TTKLYDGFQY LTNGIM
