PIS1_ARATH
ID PIS1_ARATH Reviewed; 227 AA.
AC Q8LBA6; O81846;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1;
DE EC=2.7.8.11;
DE AltName: Full=Phosphatidylinositol synthase 1;
DE Short=AtPIS1;
DE Short=PI synthase 1;
DE Short=PtdIns synthase 1;
GN Name=PIS1; OrderedLocusNames=At1g68000; ORFNames=T23K23.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=10411624; DOI=10.1046/j.1432-1327.1999.00378.x;
RA Collin S., Justin A.-M., Cantrel C., Arondel V., Kader J.-C.;
RT "Identification of AtPIS, a phosphatidylinositol synthase from
RT Arabidopsis.";
RL Eur. J. Biochem. 262:652-658(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, COFACTOR, AND TISSUE SPECIFICITY.
RX PubMed=10809447; DOI=10.1023/a:1006308909105;
RA Xue H.-W., Hosaka K., Plesch G., Mueller-Roeber B.;
RT "Cloning of Arabidopsis thaliana phosphatidylinositol synthase and
RT functional expression in the yeast pis mutant.";
RL Plant Mol. Biol. 42:757-764(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=11985617; DOI=10.1046/j.1432-1033.2002.02893.x;
RA Justin A.-M., Kader J.-C., Collin S.;
RT "Phosphatidylinositol synthesis and exchange of the inositol head are
RT catalysed by the single phosphatidylinositol synthase 1 from Arabidopsis.";
RL Eur. J. Biochem. 269:2347-2352(2002).
RN [8]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14563413; DOI=10.1016/j.bbalip.2003.08.006;
RA Justin A.-M., Kader J.-C., Collin S.;
RT "Synthetic capacity of Arabidopsis phosphatidylinositol synthase 1
RT expressed in Escherichia coli.";
RL Biochim. Biophys. Acta 1634:52-60(2003).
CC -!- FUNCTION: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns)
CC as well as PtdIns:inositol exchange reaction. May thus act to reduce an
CC excessive cellular PtdIns content. The exchange activity is due to the
CC reverse reaction of PtdIns synthase and is dependent on CMP, which is
CC tightly bound to the enzyme. {ECO:0000269|PubMed:10411624,
CC ECO:0000269|PubMed:10809447, ECO:0000269|PubMed:11985617,
CC ECO:0000269|PubMed:14563413}.
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 Evidence={ECO:0000269|PubMed:10411624};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10411624, ECO:0000269|PubMed:10809447};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10411624, ECO:0000269|PubMed:10809447};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=400 uM for myo-inositol {ECO:0000269|PubMed:14563413};
CC KM=10 uM for CDP-diacylglycerol {ECO:0000269|PubMed:14563413};
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in stems, flowers, shoots and roots.
CC Present in epidermal tissues. {ECO:0000269|PubMed:10809447}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {ECO:0000305}.
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DR EMBL; AJ000539; CAA04172.1; -; mRNA.
DR EMBL; AC012563; AAG52009.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34734.1; -; Genomic_DNA.
DR EMBL; AY140047; AAM98188.1; -; mRNA.
DR EMBL; AY087327; AAM64877.1; -; mRNA.
DR PIR; T52643; T52643.
DR RefSeq; NP_176967.1; NM_105470.3.
DR AlphaFoldDB; Q8LBA6; -.
DR SMR; Q8LBA6; -.
DR STRING; 3702.AT1G68000.1; -.
DR PaxDb; Q8LBA6; -.
DR PRIDE; Q8LBA6; -.
DR ProteomicsDB; 235089; -.
DR EnsemblPlants; AT1G68000.1; AT1G68000.1; AT1G68000.
DR GeneID; 843128; -.
DR Gramene; AT1G68000.1; AT1G68000.1; AT1G68000.
DR KEGG; ath:AT1G68000; -.
DR Araport; AT1G68000; -.
DR TAIR; locus:2200241; AT1G68000.
DR eggNOG; KOG3240; Eukaryota.
DR HOGENOM; CLU_067602_2_1_1; -.
DR InParanoid; Q8LBA6; -.
DR OMA; QEFAYIF; -.
DR OrthoDB; 1615564at2759; -.
DR PhylomeDB; Q8LBA6; -.
DR BRENDA; 2.7.8.11; 399.
DR SABIO-RK; Q8LBA6; -.
DR PRO; PR:Q8LBA6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LBA6; baseline and differential.
DR Genevisible; Q8LBA6; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IDA:TAIR.
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 Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese; Membrane;
KW Metal-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..227
FT /note="CDP-diacylglycerol--inositol 3-
FT phosphatidyltransferase 1"
FT /id="PRO_0000056805"
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 221
FT /note="I -> L (in Ref. 6; AAM64877)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25861 MW; 6109A184A4E03DDE CRC64;
MAKKERPRPE KLSVYLYIPN IVGYMRVLLN CVAFAVCFSN KPLFSVLYFF SFCCDAVDGW
VARRFNQVST FGAVLDMVTD RVSTACLLVI LSQIYRPSLV FLSLLALDIA SHWLQMYSTF
LAGKSSHKDV KDSTSWLFRL YYGNRIFMCY CCVSCEVLYI ILLLIAKNQS ENLLNVVVAT
LTQISPLSFL LALTLFGWSM KQTINVIQMK TAADVCVLYD IEKQQKP
