LSB6_YEAST
ID LSB6_YEAST Reviewed; 607 AA.
AC P42951; D6VW84;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Phosphatidylinositol 4-kinase LSB6;
DE Short=PI4-kinase;
DE Short=PtdIns-4-kinase;
DE EC=2.7.1.67;
DE AltName: Full=LAS seventeen-binding protein 6;
DE Short=LAS17-binding protein 6;
GN Name=LSB6; OrderedLocusNames=YJL100W; ORFNames=J0834;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7483851; DOI=10.1002/yea.320110909;
RA Rasmussen S.W.;
RT "A 37.5 kb region of yeast chromosome X includes the SME1, MEF2, GSH1 and
RT CSD3 genes, a TCP-1-related gene, an open reading frame similar to the
RT DAL80 gene, and a tRNA(Arg).";
RL Yeast 11:873-883(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CATALYTIC ACTIVITY, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=12361950; DOI=10.1074/jbc.m207996200;
RA Han G.-S., Audhya A., Markley D.J., Emr S.D., Carman G.M.;
RT "The Saccharomyces cerevisiae LSB6 gene encodes phosphatidylinositol 4-
RT kinase activity.";
RL J. Biol. Chem. 277:47709-47718(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH LAS17, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12523934; DOI=10.1042/bj20021407;
RA Shelton S.N., Barylko B., Binns D.D., Horazdovsky B.F., Albanesi J.P.,
RA Goodman J.M.;
RT "Saccharomyces cerevisiae contains a Type II phosphoinositide 4-kinase.";
RL Biochem. J. 371:533-540(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: May play a role in endocytic and/or exocytic pathways.
CC {ECO:0000269|PubMed:12523934}.
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:12361950,
CC ECO:0000269|PubMed:12523934};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12361950};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12361950};
CC -!- SUBUNIT: Interacts with LAS17. {ECO:0000269|PubMed:12523934}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12361950};
CC Peripheral membrane protein {ECO:0000269|PubMed:12361950}. Vacuole
CC membrane {ECO:0000269|PubMed:12361950, ECO:0000269|PubMed:12523934};
CC Peripheral membrane protein {ECO:0000269|PubMed:12361950,
CC ECO:0000269|PubMed:12523934}. Note=Located at both the plasma and
CC vacuolar membrane. {ECO:0000269|PubMed:12361950,
CC ECO:0000269|PubMed:12523934}.
CC -!- MISCELLANEOUS: Present with 56 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; X85021; CAA59394.1; -; Genomic_DNA.
DR EMBL; Z49375; CAA89395.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08700.1; -; Genomic_DNA.
DR PIR; S53387; S53387.
DR RefSeq; NP_012435.1; NM_001181533.1.
DR AlphaFoldDB; P42951; -.
DR SMR; P42951; -.
DR BioGRID; 33657; 19.
DR DIP; DIP-4035N; -.
DR IntAct; P42951; 1.
DR MINT; P42951; -.
DR STRING; 4932.YJL100W; -.
DR SwissPalm; P42951; -.
DR MaxQB; P42951; -.
DR PaxDb; P42951; -.
DR PRIDE; P42951; -.
DR EnsemblFungi; YJL100W_mRNA; YJL100W; YJL100W.
DR GeneID; 853345; -.
DR KEGG; sce:YJL100W; -.
DR SGD; S000003636; LSB6.
DR VEuPathDB; FungiDB:YJL100W; -.
DR eggNOG; KOG2381; Eukaryota.
DR GeneTree; ENSGT00390000010434; -.
DR HOGENOM; CLU_009049_1_0_1; -.
DR InParanoid; P42951; -.
DR OMA; IEYSVFQ; -.
DR BioCyc; YEAST:MON3O-352; -.
DR Reactome; R-SCE-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-SCE-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-SCE-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-SCE-1660516; Synthesis of PIPs at the early endosome membrane.
DR PRO; PR:P42951; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P42951; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR039756; Lsb6/PI4K2.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR PANTHER; PTHR12865; PTHR12865; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Kinase; Magnesium; Manganese; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Vacuole.
FT CHAIN 1..607
FT /note="Phosphatidylinositol 4-kinase LSB6"
FT /id="PRO_0000088850"
FT DOMAIN 161..522
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 73..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..173
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 318..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..392
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 411..431
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 73..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 70217 MW; 9969EC2488A72456 CRC64;
MSNEAYQHDH TVNPHQKIVV NSYDWLQFRD EQDHCKSKNP ITHASPGVGS NAQNSDIAEA
PQVFHPSYQS LVNVPSESPR PDQTSGSNPA VGLLHNAEDK ASGQEEEGSQ YEIQYSVFRP
LHAYPTKGLA YEQLRRKEEQ EQRENFNHLV SDCIEAVETF GRELERIQTG SSGSYFVYGT
RADESVPVGV FKPKDEEPYG PFSPKWTKWA HRTFFPCLFG RSCLIPNLGY ICESAASLLD
RRLETHLVPY TDTASIESFN FYDNRKKWVL GYNLQKKKQK KLGSFQLFLK EYINADEFFH
KYPLPGMYSD VKHSFHRKSS GEDINHKPET TRNLTDETEP SKQINSSPIS TESEENSKFE
WTESSLSQFR LELEKLIILD YIMRNTDRGL DNWMVKLIKL SNNKWRLKLA AIDNGLSFPW
KHPDEWRLYP YGWLYLPLQL LAKPFSEQMR SHFLPILTST NWWEESYQEF LALFSRDQDF
NVRMWKKQWA VLKGQAFNVV ETLKDPRQGP LELVRRTRCQ VIDEKMQVPC CPPPVSIFKN
AIDEPIGSYS TSPMVLPSTP STIPFHAHNQ SNSNPVYYDS TLHPFANKTV IAERLQIVNS
TPVFTWC
