PI4KB_RHIFE
ID PI4KB_RHIFE Reviewed; 816 AA.
AC B2KI64;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
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:0000250|UniProtKB:Q9UBF8};
GN Name=PI4KB; Synonyms=PIK4CB;
OS Rhinolophus ferrumequinum (Greater horseshoe bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=59479;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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). May regulate Golgi
CC disintegration/reorganization during mitosis, possibly via its
CC phosphorylation (By similarity). Involved in Golgi-to-plasma membrane
CC trafficking (By similarity). {ECO:0000250|UniProtKB:O08561,
CC ECO:0000250|UniProtKB:Q9UBF8}.
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:0000250|UniProtKB:Q9UBF8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC Evidence={ECO:0000250|UniProtKB:Q9UBF8};
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:0000250|UniProtKB:O02810}.
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 (By similarity). 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. {ECO:0000250|UniProtKB:O08561,
CC ECO:0000250|UniProtKB:Q9UBF8}.
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:0000250}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UBF8}.
CC Note=Found in the outer membrane of mitochondria and membranes of the
CC rough endoplasmic reticulum. Recruited to the Golgi complex by the
CC small GTPase ARF to stimulate the synthesis of phosphatidylinositol
CC 4,5-bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi
CC apparatus membrane by ACBD3, GGA2 is also involved in the recruitment.
CC {ECO:0000250|UniProtKB:Q9UBF8}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; DP000710; ACC64591.1; -; Genomic_DNA.
DR AlphaFoldDB; B2KI64; -.
DR SMR; B2KI64; -.
DR Ensembl; ENSRFET00010035587; ENSRFEP00010032859; ENSRFEG00010021595.
DR GeneTree; ENSGT00550000074892; -.
DR Proteomes; UP000472240; Chromosome 22.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; ISS: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:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
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 3: Inferred from homology;
KW Acetylation; ATP-binding; 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_0000365167"
FT DOMAIN 49..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..28
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 93..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..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 93..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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"
SQ SEQUENCE 816 AA; 91232 MW; 3FF1048408FE9578 CRC64;
MGDTVVAPAP LKPASESTPG PPGNNGGSLL SVITEGVGEL SVIDPEVAQK ACQEVLQKVK
LSHGGVASSD RGTPLELVNG DGVDGEIRCL DDPPTGIREE DDETEATVAS GTAKGARRRR
QNNSAKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL
NMYVHMDEDV GDAIKPYIVH RCRQSVDFSL QCALLLGAYS SDMHISTQRH SRGTKLRRLI
LSDELKPAHR KRELPSLSPA PDTGLSPSKR THQRSKSDAT ASISLSSSLK RTASNPKVES
EDEELSSSTE SIDNSFSSPV RLAPEREFIK SLMAIGKRLA TLPTKEQKTQ RLISELSLLN
HKLPARVWLP TAGFDHHVVR VPHTQAVVLN SKDKAPYLIY VEVLECENFD TTSVPARIPE
NRIRSTRSVE NLPECGISHE QRAGSFSTVP NYDNDDEAWS VDDIGELQVE LPEMHTNSCD
NISQFSVDSI TSQESKEPVF IAAGDIRRRL SEQLAHTPTA FKRDPEDPSA VALKEPWQEK
VRRIREGSPY GHLPNWRLLS VIVKCGDDLR QELLAFQVLK QLQSIWEQER VPLWIKPYKI
LVISADSGMI EPVVNAVSIH QVKKQSQLSL LDYFLQEHGS YTTEAFLSAQ RNFVQSCAGY
CLVCYLLQVK DRHNGNILLD AEGHIIHIDF GFILSSSPRN LGFETSAFKL TTEFVDVMGG
LDGDMFNYYK MLMLQGLIAA RKHMDKVVQI VEIMQQGSQL PCFHGSSTIR NLKERFHMSM
TEEQLQLLVE QMVDGSMRSI TTKLYDGFQY LTNGIM
