PI4KB_RAT
ID PI4KB_RAT Reviewed; 816 AA.
AC O08561;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
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:8973579};
GN Name=Pi4kb; Synonyms=Pik4cb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:BAA18969.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar Imamichi {ECO:0000269|PubMed:8973579};
RC TISSUE=Brain {ECO:0000269|PubMed:8973579};
RX PubMed=8973579; DOI=10.1042/bj3200643;
RA Nakagawa T., Goto K., Kondo H.;
RT "Cloning and characterization of a 92 kDa soluble phosphatidylinositol 4-
RT kinase.";
RL Biochem. J. 320:643-649(1996).
RN [2]
RP INTERACTION WITH NCS1, 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).
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CALN1/CABP8 AND CALN2/CABP7.
RX PubMed=19458041; DOI=10.1073/pnas.0903001106;
RA Mikhaylova M., Reddy P.P., Munsch T., Landgraf P., Suman S.K.,
RA Smalla K.-H., Gundelfinger E.D., Sharma Y., Kreutz M.R.;
RT "Calneurons provide a calcium threshold for trans-Golgi network to plasma
RT membrane trafficking.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9093-9098(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428 AND SER-511, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:8973579). May regulate Golgi
CC disintegration/reorganization during mitosis, possibly via its
CC phosphorylation (By similarity). Involved in Golgi-to-plasma membrane
CC trafficking (PubMed:8973579). {ECO:0000250|UniProtKB:Q9UBF8,
CC ECO:0000269|PubMed:8973579}.
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:8973579};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878;
CC Evidence={ECO:0000305|PubMed:8973579};
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 (PubMed:8973579).
CC Increased kinase activity upon interaction with NCS1/FREQ (By
CC similarity). {ECO:0000250|UniProtKB:O02810,
CC ECO:0000269|PubMed:8973579}.
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:19458041). 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:Q9UBF8,
CC ECO:0000269|PubMed:19458041}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11526106,
CC ECO:0000269|PubMed:19458041, ECO:0000269|PubMed:8973579}. Endomembrane
CC system {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Rough endoplasmic reticulum
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UBF8}. Note=Found in
CC the outer membrane of mitochondria and membranes of the rough
CC endoplasmic reticulum. Recruited to the Golgi complex by the small
CC GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-
CC 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 -!- TISSUE SPECIFICITY: Strongly expressed in brain, kidney, lung, small
CC intestine, uterus and adrenal gland. Weaker expression in liver, heart,
CC skeletal muscle, thymus and testis. Not detected in spleen.
CC {ECO:0000269|PubMed:8973579}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; D84667; BAA18969.1; -; mRNA.
DR RefSeq; NP_112345.1; NM_031083.1.
DR AlphaFoldDB; O08561; -.
DR SMR; O08561; -.
DR IntAct; O08561; 4.
DR MINT; O08561; -.
DR STRING; 10116.ENSRNOP00000039342; -.
DR iPTMnet; O08561; -.
DR PhosphoSitePlus; O08561; -.
DR jPOST; O08561; -.
DR PaxDb; O08561; -.
DR PRIDE; O08561; -.
DR GeneID; 81747; -.
DR KEGG; rno:81747; -.
DR CTD; 5298; -.
DR RGD; 621214; Pi4kb.
DR VEuPathDB; HostDB:ENSRNOG00000021024; -.
DR eggNOG; KOG0903; Eukaryota.
DR HOGENOM; CLU_002446_6_0_1; -.
DR InParanoid; O08561; -.
DR PhylomeDB; O08561; -.
DR TreeFam; TF102042; -.
DR Reactome; R-RNO-1660514; Synthesis of PIPs at the Golgi membrane.
DR PRO; PR:O08561; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000021024; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; O08561; baseline and differential.
DR Genevisible; O08561; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:RGD.
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:0007040; P:lysosome organization; ISO:RGD.
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 GO; GO:0007165; P:signal transduction; TAS:RGD.
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 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_0000088831"
FT DOMAIN 61..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..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 99..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..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:0007744|PubMed:22673903"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBF8"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 91655 MW; D7460076CE0AC362 CRC64;
MGDMVVEPAT LKPTSEPTPS PSGNNGGSLL SVITEGVGEL SVIDPEVAQK ACQEVLEKVK
LLHGGVAISS KGSPLELVNG DGVDNEIRCL DDPPTEIREE EDEMEPGVVS GTAKGTRRRR
QNNSAKQSWL LRLFESKLFD ISMAISYLYN SKEPGVQAYI GNRLFCFRNE DVDFYLPQLL
NMYIHMDEDV GDAIKPYIVH RCRQSINFSL QCALLLGAYS SDMHISTQRH SRGTKLRKLI
LSDELKPAHR KRELPTLSPA PDTGLSPSKR THQRSKSDAT ASISLSSNLK RTASNPKVEN
EDEELSSSTE SIDNSFSSPV RLAPEREFIK SLMAIGKRLA TLPTKEQKTQ RLISELSLLN
HKLPARVWLP TAGFDHHVVR VPHTQAVVLN SKDKAPYLIY VEVLECENFD TTNVPARIPE
NRIRSTRSVE NLPECGITHE QRAGSFSTVP NYDNDDEAWS VDDIGELQVE LPEVHTNSCD
NISQFSVDSI TSQESKEPVF IAAGDIRRRL SEQLAHTPTA FKRDPEDPSA VALKEPWQEK
VRRIREGSPY GHLPNWRLLS VIVKCGDDLR QELLAFQVLK QLQSIWEQER VPLWIKPYKI
LVISADSGMI EPVVNAVSIH QVKKQSQLSL LDYFLQEHGS YTTEAFLSAQ RNFVQSCAGY
CLVCYLLQVK DRHNGNILLD AEGHIIHIDF GFILSSSPRN LGFETSAFKL TTEFVDVMGG
LNGDMFNYYK MLMLQGLIAA RKHMDKVVQI VEIMQQGSQL PCFHGSSTIR NLKERFHMSM
TEEQLQLLVE QMVDGSMRSI TTKLYDGFQY LTNGIM
