STT4_YEAST
ID STT4_YEAST Reviewed; 1900 AA.
AC P37297; D6VYU8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Phosphatidylinositol 4-kinase STT4;
DE Short=PI4-kinase;
DE Short=PtdIns-4-kinase;
DE EC=2.7.1.67;
GN Name=STT4; OrderedLocusNames=YLR305C; ORFNames=L2142.4;
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 204508 / S288c;
RX PubMed=8288577; DOI=10.1016/s0021-9258(17)42237-x;
RA Yoshida S., Goebl M., Ohya Y., Nakano A., Anraku Y.;
RT "A novel gene, STT4, encodes a phosphatidylinositol 4-kinase in the PKC1
RT protein kinase pathway of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 269:1166-1172(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [5]
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Acts on phosphatidylinositol (PI) in the first committed step
CC in the production of the second messenger inositol 1,4,5,-
CC trisphosphate. STT4 functions in PKC1 protein kinase pathway.
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 -!- INTERACTION:
CC P37297; P46951: YPP1; NbExp=2; IntAct=EBI-18454, EBI-23455;
CC -!- MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; D13717; BAA02870.1; -; Genomic_DNA.
DR EMBL; U17247; AAB67358.1; -; Genomic_DNA.
DR EMBL; U17243; AAB67354.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09614.1; -; Genomic_DNA.
DR PIR; S45530; S45530.
DR RefSeq; NP_013408.1; NM_001182193.1.
DR AlphaFoldDB; P37297; -.
DR SMR; P37297; -.
DR BioGRID; 31570; 275.
DR DIP; DIP-1677N; -.
DR IntAct; P37297; 13.
DR MINT; P37297; -.
DR STRING; 4932.YLR305C; -.
DR CarbonylDB; P37297; -.
DR iPTMnet; P37297; -.
DR MaxQB; P37297; -.
DR PaxDb; P37297; -.
DR PRIDE; P37297; -.
DR EnsemblFungi; YLR305C_mRNA; YLR305C; YLR305C.
DR GeneID; 851014; -.
DR KEGG; sce:YLR305C; -.
DR SGD; S000004296; STT4.
DR VEuPathDB; FungiDB:YLR305C; -.
DR eggNOG; KOG0902; Eukaryota.
DR GeneTree; ENSGT00550000074798; -.
DR HOGENOM; CLU_000893_1_1_1; -.
DR InParanoid; P37297; -.
DR OMA; QEYRYSE; -.
DR BioCyc; YEAST:MON3O-365; -.
DR Reactome; R-SCE-1483248; Synthesis of PIPs at the ER membrane.
DR Reactome; R-SCE-1660514; Synthesis of PIPs at the Golgi membrane.
DR PRO; PR:P37297; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P37297; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
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:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0061909; P:autophagosome-lysosome fusion; IMP:SGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:CACAO.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0140504; P:microlipophagy; IMP:SGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:SGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IMP:CACAO.
DR Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
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; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR045495; PI4K_N.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048; PTHR10048; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF19274; PI4K_N; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..1900
FT /note="Phosphatidylinositol 4-kinase STT4"
FT /id="PRO_0000088835"
FT DOMAIN 1345..1530
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 1617..1884
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1531..1648
FT /note="Pleckstrin homology (PH) domain conferring
FT phosphoinositide binding specificity"
FT /evidence="ECO:0000250"
FT REGION 1623..1629
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1751..1759
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1770..1794
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1900 AA; 214607 MW; F210BAF987BA276A CRC64;
MRFTRGLKAS SSLRAKAIGR LTKLSTGAPN DQNSNGTTLD LITHTLPIFY STNTSKIYTI
PLTLSEWEVL TSLCVAIPTT LDLVETMLKE IIAPYFLETP RQRISDVLSS KFKLEQMRNP
IELLTFQLTK FMIQACEQYP VLYENIGGII STYFERVLKI FTIKQSGLLS LVGFINAFIQ
FPNSTELTKF TWKKLAKLVL RGSFLNEVDK ILNSSATFTN DSIVQYYDAG NELSSAYLLE
LISRLQVSLI SHLLNTSHVG ANLSEFLLNQ QYQFYKFDQE VADENDDTKC IDDFFFNVRS
NKQFFTDMCK ISLQFCSESH ILDLSTDNRA RFSFDTRAHY LQTLCLIPFI EDTESELFES
FTNVVSESID KFFLSDVVTP SLIKAIVASA SLLNFFTEKL SLTLIRMFPL LVASPHITTE
TVNDVAKIFT TGLYPLNEDA IVSTIYSMNN LLAVSEDGSP VPVLRERQLT ITSGKNIEKD
YFPLRNSSAS LDGTGALLGN TTVGQLSSHD VNSGATMTYH ASLISNCVAA TTTIASYYNT
QSITALTISI LTQKVNSMSK ELDGVILNSL ARLAPNTSLT EFSLLLKFFK SRTVIATKID
DSALLKNIIK AKCVISKELL ARHFSSDLYF MYLHDLLDSI IASGEVERLE HHRPQTEISR
VADQIATYLE PLAALLPVPG DTPLDINKDE VTTNKFRNAW FNFVIHGYHL GGPIVKRNFS
FLLTIAYNSP PLASEFPANN KELSLEMNTI LRRGSSNENI KQQKQQITEY FNTNIVQYRT
TSSSKIMFLA AAVLLETIRC EAGDCSKTLL YFSDPSILSG SIEKCIAVLS VSMIRKYARL
IQKGNDAIFN SKMIAQQLNN LLLCLSHREP TLQDAAFHAC EIFIRSIPSS LCHHLSLYTL
LDMLTALFDS ILDSEAHKFE PRYEFKLKHS KTTILVPSSS SWRATTLSRL HKSAKEWVRI
LLNRSNQDTK ILLQSYISDL GEYSRLNSVE FGVSFAMDMA GLILPADKEL SRLTYYGPEK
PNTISGFISL HSWRSKYLFD TAITSSPEDI KRQIGISTQN IRKNLTLGNK IITKDVTDFL
DMATALLILG NGAPASLIYD IVHIPFEVFT SASLKIATNV WLTIITEKPE VAHLLLVEVC
YCWMRSIDDN IGLYSRDHDL KGEEYQKMEY SPYDKAGINR DAKNASQAMQ PHLHVIKFFA
SHFEGTLFQS DFLLKIFTKC ALYGIKNLYK ASLHPFARMI RHELLLFATL VLNASYKQGS
KYMGRLSQEI TNGALSWFKR PVAWPFGSNE LKIKADLSVT RDLFLQLNKL SSLMSRHCGK
DYKILNYFLA SEIQQIQTWL TPTEKIEGAD SNELTSDIVE ATFAKDPTLA INLLQRCYSK
KAEDVLVGLV AKHALMCVGS PSALDLFIKG SHLSSKKDLH ATLYWAPVSP LKSINLFLPE
WQGNSFILQF SIYSLESQDV NLAFFYVPQI VQCLRYDKTG YVERLILDTA KISVLFSHQI
IWNMLANCYK DDEGIQEDEI KPTLDRIRER MVSSFSQSHR DFYEREFEFF DEVTGISGKL
KPYIKKSKAE KKHKIDEEMS KIEVKPDVYL PSNPDGVVID IDRKSGKPLQ SHAKAPFMAT
FKIKKDVKDP LTGKNKEVEK WQAAIFKVGD DCRQDVLALQ LISLFRTIWS SIGLDVYVFP
YRVTATAPGC GVIDVLPNSV SRDMLGREAV NGLYEYFTSK FGNESTIEFQ NARNNFVKSL
AGYSVISYLL QFKDRHNGNI MYDDQGHCLH IDFGFIFDIV PGGIKFEAVP FKLTKEMVKV
MGGSPQTPAY LDFEELCIKA YLAARPHVEA IIECVNPMLG SGLPCFKGHK TIRNLRARFQ
PQKTDHEAAL YMKALIRKSY ESIFTKGYDE FQRLTNGIPY
