PI4KB_SORAR
ID PI4KB_SORAR Reviewed; 801 AA.
AC B3EX61;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 Sorex araneus (Eurasian common shrew) (European shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Soricinae; Sorex.
OX NCBI_TaxID=42254;
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 (JUN-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; DP000772; ACE75819.1; -; Genomic_DNA.
DR RefSeq; XP_004618146.1; XM_004618089.1.
DR AlphaFoldDB; B3EX61; -.
DR SMR; B3EX61; -.
DR GeneID; 101556829; -.
DR KEGG; sara:101556829; -.
DR CTD; 5298; -.
DR OrthoDB; 1147978at2759; -.
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; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT CHAIN 2..801
FT /note="Phosphatidylinositol 4-kinase beta"
FT /id="PRO_0000365168"
FT DOMAIN 29..242
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 520..786
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..29
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..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..532
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 653..661
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 672..696
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 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 423
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 502
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
SQ SEQUENCE 801 AA; 89991 MW; 63547909A887330A CRC64;
MGDTAVEPAP LKPASEPAPG PPGNNGGSLL SVITEGVGEL SVIDPEVAQK ACQEVLEKVR
LLHGAVAVSK RGTALELVNG DGVDTEIRCL DDPPAQIREE EDEMGATVTS GTAKGARRRR
QNNSAKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL
NMYIHMDEDV GDAIKPYIVH RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI
LSDELKPAHR KRELPSLSPA LNTGLSPSKR THQRSKSDAT ASISLSSSLK RTASNPKVEN
EDEPIRLAPE REFIKSLMAI GKRLATLPTK EQKTQRLISE LSLLNHKLPA RVWLPTAAFD
HHVVRVPHTQ AVVLNSKDKA PYLIYVEVLE CENFDTTNVP ARIPENRIRS TRSVENLPEC
GITHEQRAGS FSTVPNYDND DEAWSVDDIG ELQVELPEMH TNSCDNISQF SVDSITSQES
KEPVFIAAGD IRRRLSEQLA HTPTAFRRDP EDPSAVALKE PWQEKVRRIR EGSPYGHLPN
WRLLSVIVKC GDDLRQELLA FQVLKQLQSI WEQERVPLWI KPYKILVISA DSGMIEPVVN
AVSIHQVKKQ SQLSLLDYFL QEHGSYTTEA FLSAQRNFVQ SCAGYCLVCY LLQVKDRHNG
NILLDAEGHI IHIDFGFILS SSPRNLGFET SAFKLTTEFV DVMGGLDGDM FNYYKMLMLQ
GLIAARKHMD KVVQIVEIMQ QGSQLPCFHG SSTIRNLKER FHMNMTEEQL QLLVEQMVDG
SMRSITTKLY DGFQYLTNGI M
