PIS_SCHPO
ID PIS_SCHPO Reviewed; 237 AA.
AC Q10153;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 25-MAY-2022, entry version 132.
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; ORFNames=SPAC1D4.08;
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 GENE MODEL REVISION.
RX PubMed=24929437; DOI=10.1038/nsmb.2843;
RA Duncan C.D., Mata J.;
RT "The translational landscape of fission-yeast meiosis and sporulation.";
RL Nat. Struct. Mol. Biol. 21:641-647(2014).
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
CC {ECO:0000250|UniProtKB:P06197}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P06197}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P06197}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA93217.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA93217.1; ALT_SEQ; Genomic_DNA.
DR PIR; T38049; T38049.
DR RefSeq; NP_593021.1; NM_001018420.2.
DR AlphaFoldDB; Q10153; -.
DR SMR; Q10153; -.
DR BioGRID; 278946; 3.
DR STRING; 4896.SPAC1D4.08.1; -.
DR PaxDb; Q10153; -.
DR EnsemblFungi; SPAC1D4.08.1; SPAC1D4.08.1:pep; SPAC1D4.08.
DR GeneID; 2542487; -.
DR KEGG; spo:SPAC1D4.08; -.
DR PomBase; SPAC1D4.08; pis1.
DR VEuPathDB; FungiDB:SPAC1D4.08; -.
DR eggNOG; KOG3240; Eukaryota.
DR InParanoid; Q10153; -.
DR Reactome; R-SPO-1483226; Synthesis of PI.
DR PRO; PR:Q10153; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; NAS:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; EXP:PomBase.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; EXP:PomBase.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISO:PomBase.
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 3: Inferred from homology;
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..237
FT /note="CDP-diacylglycerol--inositol 3-
FT phosphatidyltransferase"
FT /id="PRO_0000056823"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P06197"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..41
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P06197"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P06197"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..94
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P06197"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P06197"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..185
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:P06197"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P06197"
SQ SEQUENCE 237 AA; 26924 MW; 5E88E32FA35EE64D CRC64;
MGKNEQKDPN VYFFVPNLIG FTRVFLVLIS LYFMSWHPNY CTIVYLYSSL LDAFDGWAAR
KLHQATNFGA ILDMVTDRCA TSCLLCFLCA AYPKYAIIFQ LLVSLDLASH YMHMYSTLHQ
GASSHKTVTK KHNWMLRLYY GNNKVLFIFC AANEMFFVAL YLLSFTPRTP PKLGYLPVPS
FIYSTGELPL SYPTLLAVLC GPICLAKQII NVVQLVNAAN ALVKMDVEQR RAAKKLQ
