MSS4_YEAST
ID MSS4_YEAST Reviewed; 779 AA.
AC P38994; D6VSI9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase MSS4;
DE EC=2.7.1.68 {ECO:0000269|PubMed:9624178};
DE AltName: Full=1-phosphatidylinositol 4-phosphate kinase;
DE AltName: Full=Diphosphoinositide kinase;
DE AltName: Full=PIP5K;
GN Name=MSS4 {ECO:0000303|PubMed:8152413}; OrderedLocusNames=YDR208W;
GN ORFNames=YD8142A.05;
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], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8152413; DOI=10.1007/bf00283416;
RA Yoshida S., Ohya Y., Nakano A., Anraku Y.;
RT "Genetic interactions among genes involved in the STT4-PKC1 pathway of
RT Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 242:631-640(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9624178; DOI=10.1074/jbc.273.25.15787;
RA Desrivieres S., Cooke F.T., Parker P.J., Hall M.N.;
RT "MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for
RT organization of the actin cytoskeleton in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:15787-15793(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-222, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-659 AND SER-661, AND
RP IDENTIFICATION BY 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).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; THR-222; SER-225;
RP THR-659 AND SER-661, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-
CC phosphate on the fifth hydroxyl of the myo-inositol ring, to form
CC phosphatidylinositol 4,5-bisphosphate (PubMed:9624178). Acts downstream
CC of STT4, but in a pathway that does not involve PKC1. May be involved
CC in the organization of the actin cytoskeleton (PubMed:8152413).
CC {ECO:0000269|PubMed:8152413, ECO:0000269|PubMed:9624178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68;
CC Evidence={ECO:0000269|PubMed:9624178};
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DR EMBL; D13716; BAA02869.1; -; Genomic_DNA.
DR EMBL; Z68194; CAA92347.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12049.1; -; Genomic_DNA.
DR PIR; S61571; S61571.
DR RefSeq; NP_010494.1; NM_001180516.1.
DR AlphaFoldDB; P38994; -.
DR SMR; P38994; -.
DR BioGRID; 32258; 318.
DR IntAct; P38994; 3.
DR MINT; P38994; -.
DR STRING; 4932.YDR208W; -.
DR iPTMnet; P38994; -.
DR MaxQB; P38994; -.
DR PaxDb; P38994; -.
DR PRIDE; P38994; -.
DR EnsemblFungi; YDR208W_mRNA; YDR208W; YDR208W.
DR GeneID; 851789; -.
DR KEGG; sce:YDR208W; -.
DR SGD; S000002616; MSS4.
DR VEuPathDB; FungiDB:YDR208W; -.
DR eggNOG; KOG0229; Eukaryota.
DR HOGENOM; CLU_004312_4_1_1; -.
DR InParanoid; P38994; -.
DR OMA; HKREMKR; -.
DR BioCyc; YEAST:YDR208W-MON; -.
DR Reactome; R-SCE-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-SCE-6811555; PI5P Regulates TP53 Acetylation.
DR Reactome; R-SCE-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-SCE-8847453; Synthesis of PIPs in the nucleus.
DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P38994; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P38994; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR GO; GO:0031321; P:ascospore-type prospore assembly; IGI:SGD.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:CACAO.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.800.10; -; 1.
DR InterPro; IPR023610; PInositol-4-P-5-kinase.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR PANTHER; PTHR23086; PTHR23086; 1.
DR Pfam; PF01504; PIP5K; 1.
DR SMART; SM00330; PIPKc; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..779
FT /note="Phosphatidylinositol 4-phosphate 5-kinase MSS4"
FT /id="PRO_0000185455"
FT DOMAIN 376..756
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 659
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 610
FT /note="F -> L (in Ref. 1; BAA02869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 779 AA; 89320 MW; F66B796229CFB8F6 CRC64;
MSVLRSQPPS VVPLHLTTST SRKTEQEPSL LHSAIIERHQ DRSVPNSNSN PDSNHRIKKD
RNNHTSYHSS SNSESNMESP RLSDGESSTP TSIEELNPTI NNSRLVKRNY SISIDPLHDN
SNNNTDDDHP NTITSPRPNS TSNKEMQKYS FPEGKESKKI TTPSLNSNNC LDLDNSSLVH
TDSYIQDLND DHILLNKRVS RRSSRISAVT ATSTTIKQRR NTQDSNLPNI PFHASKHSQI
LPMDDSDVIK LANGDTSMKP NSATKISHSM TSLPLHPLPQ PSQKSKQYHM ISKSTTSLPP
ENDHYYQHSR GTNHNHAANA AAVNNNTTTT TAATGLKRSE SATAEIKKMR QSLLHKREMK
RKRKTFLVDD DRVLIGNKVS EGHVNFIIAY NMLTGIRVAV SRCSGIMKPL TPADFRFTKK
LAFDYHGNEL TPSSQYAFKF KDYCPEVFRE LRALFGLDPA DYLVSLTSKY ILSELNSPGK
SGSFFYYSRD YKYIIKTIHH SEHIHLRKHI QEYYNHVRDN PNTLICQFYG LHRVKMPISF
QNKIKHRKIY FLVMNNLFPP HLDIHITYDL KGSTWGRFTN LDKERLAKDR SYRPVMKDLN
WLEEGQKIKF GPLKKKTFLT QLKKDVELLA KLNTMDYSLL IGIHDINKAK EDDLQLADTA
SIEEQPQTQG PIRTGTGTVV RHFFREFEGG IRASDQFNND VDLIYYVGII DFLTNYSVMK
KLETFWRSLR HDTKLVSAIP PRDYANRFYE FIEDSVDPLP QKKTQSSYRD DPNQKNYKD
