IPT1_YEAST
ID IPT1_YEAST Reviewed; 527 AA.
AC P38954; D6VS58;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Inositolphosphotransferase 1 {ECO:0000303|PubMed:9368028};
DE EC=2.7.1.228 {ECO:0000269|PubMed:9368028};
DE AltName: Full=Mannosyl diphosphorylinositol ceramide synthase {ECO:0000303|PubMed:9368028};
GN Name=IPT1 {ECO:0000303|PubMed:9368028}; Synonyms=SYR4;
GN OrderedLocusNames=YDR072C; ORFNames=D4405, YD8554.05C;
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].
RA Stock S.D., Takemoto J.Y.;
RT "SYR4: a syringomycin action gene required for mannosyl
RT diphosphorylinositol ceramide synthesis in Saccharomyces cerevisiae.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7483840; DOI=10.1002/yea.320110708;
RA Coster F., Jonniaux J.-L., Goffeau A.;
RT "Analysis of a 32.8 kb segment of yeast chromosome IV reveals 21 open
RT reading frames, including TPS2, PPH3, RAD55, SED1, PDC2, AFR1, SSS1, SLU7
RT and a tRNA for arginine.";
RL Yeast 11:673-679(1995).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=9368028; DOI=10.1074/jbc.272.47.29620;
RA Dickson R.C., Nagiec E.E., Wells G.B., Nagiec M.M., Lester R.L.;
RT "Synthesis of mannose-(inositol-P)2-ceramide, the major sphingolipid in
RT Saccharomyces cerevisiae, requires the IPT1 (YDR072c) gene.";
RL J. Biol. Chem. 272:29620-29625(1997).
RN [7]
RP FUNCTION.
RX PubMed=10931938; DOI=10.1073/pnas.160077797;
RA Thevissen K., Cammue B.P., Lemaire K., Winderickx J., Dickson R.C.,
RA Lester R.L., Ferket K.K., Van Even F., Parret A.H., Broekaert W.F.;
RT "A gene encoding a sphingolipid biosynthesis enzyme determines the
RT sensitivity of Saccharomyces cerevisiae to an antifungal plant defensin
RT from dahlia (Dahlia merckii).";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9531-9536(2000).
RN [8]
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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=14583628; DOI=10.1074/jbc.m306119200;
RA Lisman Q., Pomorski T., Vogelzangs C., Urli-Stam D.,
RA de Cocq van Delwijnen W., Holthuis J.C.;
RT "Protein sorting in the late Golgi of Saccharomyces cerevisiae does not
RT require mannosylated sphingolipids.";
RL J. Biol. Chem. 279:1020-1029(2004).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
RN [13]
RP FUNCTION.
RX PubMed=22322963; DOI=10.1099/mic.0.056184-0;
RA Nakase M., Tani M., Takegawa K.;
RT "Expression of budding yeast IPT1 produces mannosyldiinositol
RT phosphorylceramide in fission yeast and inhibits cell growth.";
RL Microbiology 158:1219-1228(2012).
CC -!- FUNCTION: Catalyzes the addition of a phosphorylinositol group onto
CC mannosyl phosphorylinositol ceramide (MIPC) to form mannosyl
CC diphosphorylinositol ceramide (M(IP)2C), the major sphingolipid in
CC membranes of S.cerevisiae. {ECO:0000269|PubMed:10931938,
CC ECO:0000269|PubMed:22322963, ECO:0000269|PubMed:9368028}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + an
CC alpha-D-mannosyl-(1<->6)-1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-
CC very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base = a 1,2-
CC diacyl-sn-glycerol + an alpha-D-mannosyl-6-(1D-myo-inositol phospho)-
CC (1<->6)-1D-myo-inositol-1-phospho-N-[(R)-2-hydroxy-very-long-chain
CC fatty acyl]-(R)-4-hydroxysphingoid base; Xref=Rhea:RHEA:64540,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:57880, ChEBI:CHEBI:155884,
CC ChEBI:CHEBI:155885; EC=2.7.1.228;
CC Evidence={ECO:0000269|PubMed:9368028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64541;
CC Evidence={ECO:0000269|PubMed:9368028};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + a
CC mannosylinositol-1-phospho-N-acyl-sphingoid base = a 1,2-diacyl-sn-
CC glycerol + an inositol phosphomannosylnositol-1-phospho-N-
CC acylsphingoid base; Xref=Rhea:RHEA:55604, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:64997, ChEBI:CHEBI:74997;
CC Evidence={ECO:0000269|PubMed:10931938, ECO:0000269|PubMed:22322963};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55605;
CC Evidence={ECO:0000305|PubMed:10931938, ECO:0000305|PubMed:22322963};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + a
CC mannosylinositol-1-phospho-N-(2-hydroxyacyl)-4R-hydroxysphingoid base
CC = a 1,2-diacyl-sn-glycerol + an inositol phosphomannosylnositol-1-
CC phospho-N-(2-hydroxyacyl)-4R-hydroxysphingoid base;
CC Xref=Rhea:RHEA:55608, ChEBI:CHEBI:17815, ChEBI:CHEBI:57880,
CC ChEBI:CHEBI:74994, ChEBI:CHEBI:75023;
CC Evidence={ECO:0000269|PubMed:9368028};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55609;
CC Evidence={ECO:0000305|PubMed:9368028};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:14583628}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Fails to accumulate M(IP)2C and instead
CC accumulates increased amounts of the precursor mannose-inositol-P-
CC ceramide. {ECO:0000269|PubMed:9368028}.
CC -!- MISCELLANEOUS: Present with 606 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; AF022365; AAB72226.1; -; Genomic_DNA.
DR EMBL; X82086; CAA57599.1; -; Genomic_DNA.
DR EMBL; Z46796; CAA86794.1; -; Genomic_DNA.
DR EMBL; Z74368; CAA98890.1; -; Genomic_DNA.
DR EMBL; Z74369; CAA98892.1; -; Genomic_DNA.
DR EMBL; AY723772; AAU09689.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11918.1; -; Genomic_DNA.
DR PIR; S49827; S49827.
DR RefSeq; NP_010357.3; NM_001180380.3.
DR AlphaFoldDB; P38954; -.
DR BioGRID; 32127; 229.
DR DIP; DIP-5200N; -.
DR IntAct; P38954; 4.
DR MINT; P38954; -.
DR STRING; 4932.YDR072C; -.
DR SwissLipids; SLP:000001852; -.
DR iPTMnet; P38954; -.
DR PaxDb; P38954; -.
DR PRIDE; P38954; -.
DR TopDownProteomics; P38954; -.
DR EnsemblFungi; YDR072C_mRNA; YDR072C; YDR072C.
DR GeneID; 851644; -.
DR KEGG; sce:YDR072C; -.
DR SGD; S000002479; IPT1.
DR VEuPathDB; FungiDB:YDR072C; -.
DR eggNOG; ENOG502QPKA; Eukaryota.
DR GeneTree; ENSGT00940000176762; -.
DR HOGENOM; CLU_047580_1_0_1; -.
DR InParanoid; P38954; -.
DR OMA; PMAPPWF; -.
DR BioCyc; MetaCyc:YDR072C-MON; -.
DR BioCyc; YEAST:YDR072C-MON; -.
DR BRENDA; 2.7.1.228; 984.
DR PRO; PR:P38954; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P38954; protein.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070916; C:inositol phosphoceramide synthase complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045140; F:inositol phosphoceramide synthase activity; IBA:GO_Central.
DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IDA:SGD.
DR GO; GO:0006673; P:inositol phosphoceramide metabolic process; IBA:GO_Central.
DR GO; GO:0006676; P:mannosyl diphosphorylinositol ceramide metabolic process; IDA:SGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IGI:SGD.
DR InterPro; IPR026841; Aur1/Ipt1.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR Pfam; PF14378; PAP2_3; 1.
PE 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..527
FT /note="Inositolphosphotransferase 1"
FT /id="PRO_0000084224"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..99
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..190
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241..288
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..461
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT REGION 331..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 60873 MW; 0792FE736A560BAE CRC64;
MNVIFSLASF VKNMYNASLN QRNLISLPFN FMLNFAPVFI WLSIFKRAGL IPIRLRPDIH
SKFAFFADQF LFGDYWHELT VQLPDNTSKL FFWSFISSSA FLLVFLICIP FAIWYYIYYI
KHVNYNLLEW FANIFHYPCK RKQRPIQKRF RTIFIPFALP LFTFVILNID HFFAYQSDAN
FTKTKDLLAW FSYVILHLTA PILTAVYLYV FQPPGTLKCF SFALGLQNIA GVLTHLLVPM
ASPWFTHLYG IDDTEHVNYT QEGFAAGLIR VDSHLGTHLN TKGFHMSPIV FGAVPSLHSA
IAFQCFLFLV SRSTSLKHRF SNAGGFTMHN NDSSTFKLSE EDSEDEGDNS IPPTIGPNDL
EMEPLGTVEP VDISNERSSS PSSSFTVSSN ERSTGGGDGS IINSNGNKKP LQFVHLYDED
TNFTNKWIFK IVNDGFIPKF WAILYIILQW WATMYLDHHY RFDLFVGVLY AMTSFIIINW
FVLQPKVLKK WIHIRLGDKV DTRNEARTFG MRVFCGTKME WFFDPLA
