LSB6_SCHPO
ID LSB6_SCHPO Reviewed; 624 AA.
AC Q9UT42; Q9UT71;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Phosphatidylinositol 4-kinase lsb6;
DE Short=PI4-kinase;
DE Short=PtdIns-4-kinase;
DE EC=2.7.1.67;
GN Name=lsb6; ORFNames=SPAC343.19, SPAC824.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: May play a role in endocytic and/or exocytic pathways.
CC {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Vacuole membrane {ECO:0000269|PubMed:16823372};
CC Peripheral membrane protein {ECO:0000269|PubMed:16823372}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane
CC protein {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB52282.1; -; Genomic_DNA.
DR PIR; T39102; T39102.
DR RefSeq; XP_001713056.1; XM_001713004.2.
DR AlphaFoldDB; Q9UT42; -.
DR SMR; Q9UT42; -.
DR BioGRID; 280607; 2.
DR STRING; 4896.SPAC343.19.1; -.
DR iPTMnet; Q9UT42; -.
DR MaxQB; Q9UT42; -.
DR PaxDb; Q9UT42; -.
DR PRIDE; Q9UT42; -.
DR EnsemblFungi; SPAC343.19.1; SPAC343.19.1:pep; SPAC343.19.
DR PomBase; SPAC343.19; lsb6.
DR VEuPathDB; FungiDB:SPAC343.19; -.
DR eggNOG; KOG2381; Eukaryota.
DR HOGENOM; CLU_009049_1_0_1; -.
DR InParanoid; Q9UT42; -.
DR OMA; PTFNYDY; -.
DR PhylomeDB; Q9UT42; -.
DR Reactome; R-SPO-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-SPO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-SPO-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-SPO-1660516; Synthesis of PIPs at the early endosome membrane.
DR PRO; PR:Q9UT42; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; ISO:PomBase.
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; ISO:PomBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
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 3: Inferred from homology;
KW ATP-binding; Cell membrane; Golgi apparatus; Kinase; Magnesium; Manganese;
KW Membrane; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Vacuole.
FT CHAIN 1..624
FT /note="Phosphatidylinositol 4-kinase lsb6"
FT /id="PRO_0000088849"
FT DOMAIN 145..520
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..157
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 346..354
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 409..429
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ SEQUENCE 624 AA; 71857 MW; 3DC401D41E3EAC68 CRC64;
MESTFHSDTL DSFPNYQENS LNTNEEQTNP LESLRDGWAS SNSSSSSSLL LPDENEGNEV
FGSLKGLVTQ SKFGQWANKL SKSLQARRRK SESISKPRVY YSVFMAPSWV LHAEKHWEEY
PHYAGYDYKD YVRLLDATKE AIAHGVFPVL ISKGSSGSYF VKNKVQKNIA VFKPKDEEPY
GKLNPKWTKW FHRNLFPCFF GRSCLIPNTS YLSEAAACVL DRGLGLYLVP YTSVASISSP
TFNYDYFARK AFLTRNKPLP EKTGSFQQFL DGFVVASKFF AQHPWPGTRH RETREYTESV
ASSEDFDIFD PFLAENEIET EFWTEELRLK FRFEFEKLVL LDYLMRNTDR NLDNWMIKIC
YEPCDNEEYY KSINLLSTNL TPNMSANSVD PAISQTSDFW KGPHFQIGAI DNSLAFPYKH
PDSWRSFPYG WLSLPRSLFT QPFTEFTRQL FLHKLTSREW WEKLSDDLRN VFNQDLDFDE
KMFSRQLSLV KGQAYNIVEV LKNPLMNIYD LLELPNLYVV EDVVRIEVNE PTSANSEEAE
FGLPIKRDYG SILHPSCSQT FPPYPGSQLL QATPGRSFSS NAEALLPLNY ITLLSKDSSS
PKMLKDVIFE RLQCASSNAV FSTC
