PIS_YEAST
ID PIS_YEAST Reviewed; 220 AA.
AC P06197; D6W4B2;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=CDP-diacylglycerol--inositol 3-phosphatidyltransferase;
DE EC=2.7.8.11;
DE AltName: Full=Phosphatidylinositol synthase;
DE Short=PI synthase;
DE Short=PtdIns synthase;
GN Name=PIS1; Synonyms=PIS; OrderedLocusNames=YPR113W; ORFNames=P8283.5;
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].
RX PubMed=3031032; DOI=10.1016/s0021-9258(18)61277-3;
RA Nikawa J., Kodaki T., Yamashita S.;
RT "Primary structure and disruption of the phosphatidylinositol synthase gene
RT of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 262:4876-4881(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [6]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) + CMP + H(+);
CC Xref=Rhea:RHEA:11580, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.11;
CC -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane; Multi-pass membrane protein.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:16823961}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:16823961}.
CC -!- MISCELLANEOUS: Myo-inositol-containing phospholipids are of crucial
CC importance in the control of cellular functions.
CC -!- MISCELLANEOUS: Present with 3810 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; J02697; AAA34876.1; -; Genomic_DNA.
DR EMBL; U32445; AAB68083.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11528.1; -; Genomic_DNA.
DR PIR; A27409; A27409.
DR RefSeq; NP_015438.1; NM_001184210.1.
DR AlphaFoldDB; P06197; -.
DR SMR; P06197; -.
DR BioGRID; 36280; 56.
DR DIP; DIP-3815N; -.
DR IntAct; P06197; 33.
DR MINT; P06197; -.
DR STRING; 4932.YPR113W; -.
DR MaxQB; P06197; -.
DR PaxDb; P06197; -.
DR PRIDE; P06197; -.
DR EnsemblFungi; YPR113W_mRNA; YPR113W; YPR113W.
DR GeneID; 856229; -.
DR KEGG; sce:YPR113W; -.
DR SGD; S000006317; PIS1.
DR VEuPathDB; FungiDB:YPR113W; -.
DR eggNOG; KOG3240; Eukaryota.
DR GeneTree; ENSGT00940000154169; -.
DR HOGENOM; CLU_067602_0_0_1; -.
DR InParanoid; P06197; -.
DR OMA; AQTYSEN; -.
DR BioCyc; MetaCyc:YPR113W-MON; -.
DR BioCyc; YEAST:YPR113W-MON; -.
DR BRENDA; 2.7.8.11; 984.
DR Reactome; R-SCE-1483226; Synthesis of PI.
DR PRO; PR:P06197; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P06197; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; IDA:SGD.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:SGD.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR InterPro; IPR014387; CDP_diag_ino_3_P_euk.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
DR PIRSF; PIRSF000848; CDP_diag_ino_3_P; 1.
DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Microsome; Mitochondrion; Mitochondrion outer membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..220
FT /note="CDP-diacylglycerol--inositol 3-
FT phosphatidyltransferase"
FT /id="PRO_0000056807"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..45
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..98
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..170
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
SQ SEQUENCE 220 AA; 24824 MW; 6E2E62252B3CB5E2 CRC64;
MSSNSTPEKV TAEHVLWYIP NKIGYVRVIT AALSFFVMKN HPTAFTWLYS TSCLLDALDG
TMARKYNQVS SLGAVLDMVT DRSSTAGLMC FLCVQYPQWC VFFQLMLGLD ITSHYMHMYA
SLSAGKTSHK SVGEGESRLL HLYYTRRDVL FTICAFNELF YAGLYLQLFS NSATFGKWTT
IISFPGYVFK QTANVVQLKR AALILADNDA KNANEKNKTY
