PIS2_ARATH
ID PIS2_ARATH Reviewed; 225 AA.
AC Q8GUK6; Q9SZN6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable CDP-diacylglycerol--inositol 3-phosphatidyltransferase 2;
DE EC=2.7.8.11;
DE AltName: Full=Phosphatidylinositol synthase 2;
DE Short=AtPIS2;
DE Short=PI synthase 2;
DE Short=PtdIns synthase 2;
GN Name=PIS2; OrderedLocusNames=At4g38570; ORFNames=F20M13.130;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
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 [4]
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.
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 (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8GUK6-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC family. {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; AL035540; CAB37513.1; -; Genomic_DNA.
DR EMBL; AL161593; CAB80521.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86948.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66702.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66703.1; -; Genomic_DNA.
DR EMBL; BT002432; AAO00792.1; -; mRNA.
DR EMBL; AY086801; AAM63850.1; -; mRNA.
DR PIR; T05685; T05685.
DR RefSeq; NP_001328583.1; NM_001342506.1. [Q8GUK6-1]
DR RefSeq; NP_001328584.1; NM_001342505.1. [Q8GUK6-1]
DR RefSeq; NP_195569.1; NM_120018.4. [Q8GUK6-1]
DR AlphaFoldDB; Q8GUK6; -.
DR SMR; Q8GUK6; -.
DR STRING; 3702.AT4G38570.1; -.
DR iPTMnet; Q8GUK6; -.
DR PaxDb; Q8GUK6; -.
DR PRIDE; Q8GUK6; -.
DR ProteomicsDB; 236759; -. [Q8GUK6-1]
DR EnsemblPlants; AT4G38570.1; AT4G38570.1; AT4G38570. [Q8GUK6-1]
DR EnsemblPlants; AT4G38570.3; AT4G38570.3; AT4G38570. [Q8GUK6-1]
DR EnsemblPlants; AT4G38570.4; AT4G38570.4; AT4G38570. [Q8GUK6-1]
DR GeneID; 830014; -.
DR Gramene; AT4G38570.1; AT4G38570.1; AT4G38570. [Q8GUK6-1]
DR Gramene; AT4G38570.3; AT4G38570.3; AT4G38570. [Q8GUK6-1]
DR Gramene; AT4G38570.4; AT4G38570.4; AT4G38570. [Q8GUK6-1]
DR KEGG; ath:AT4G38570; -.
DR Araport; AT4G38570; -.
DR TAIR; locus:2121184; AT4G38570.
DR eggNOG; KOG3240; Eukaryota.
DR InParanoid; Q8GUK6; -.
DR PhylomeDB; Q8GUK6; -.
DR BioCyc; ARA:AT4G38570-MON; -.
DR BRENDA; 2.7.8.11; 399.
DR PRO; PR:Q8GUK6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GUK6; baseline and differential.
DR Genevisible; Q8GUK6; 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:0003881; F:CDP-diacylglycerol-inositol 3-phosphatidyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Manganese; Membrane; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..225
FT /note="Probable CDP-diacylglycerol--inositol 3-
FT phosphatidyltransferase 2"
FT /id="PRO_0000056806"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 148
FT /note="C -> S (in Ref. 3; AAO00792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 25580 MW; A5E395A81A50B4BB CRC64;
MAKQRPATLS VYLYIPNIVG YMRVLLNCIA FSVCFSNKTL FSLLYFFSFC CDAVDGWCAR
KFNQVSTFGA VLDMVTDRVS TACLLVILSQ IYRPSLVFLS LLALDIASHW LQMYSTFLSG
KTSHKDVKDS TSWLFRLYYG NRMFMGYCCV SCEVLYIILL LIATNQTENL MNVVVKSLMQ
ISPLSLLLAL SIFGWSIKQI INVIQMKTAA DVCVLYDIEK QHKKP
