HPT1_ARATH
ID HPT1_ARATH Reviewed; 393 AA.
AC Q8VWJ1; O64625;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Homogentisate phytyltransferase 1, chloroplastic;
DE Short=AtHPT1;
DE EC=2.5.1.115;
DE AltName: Full=Tocopherol polyprenyltransferase 1;
DE AltName: Full=Vitamin E pathway gene 2-1 protein;
DE Short=AtVTE2-1;
DE Flags: Precursor;
GN Name=HPT1; Synonyms=TPT1, VTE2-1; OrderedLocusNames=At2g18950;
GN ORFNames=F19F24.15;
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], AND FUNCTION.
RX PubMed=11706191; DOI=10.1104/pp.010421;
RA Collakova E., DellaPenna D.;
RT "Isolation and functional analysis of homogentisate phytyltransferase from
RT Synechocystis sp. PCC 6803 and Arabidopsis.";
RL Plant Physiol. 127:1113-1124(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. No-0;
RX PubMed=12011362; DOI=10.1104/pp.010747;
RA Savidge B., Weiss J.D., Wong Y.H.H., Lassner M.W., Mitsky T.A.,
RA Shewmaker C.K., Post-Beittenmiller D., Valentin H.E.;
RT "Isolation and characterization of homogentisate phytyltransferase genes
RT from Synechocystis sp. PCC 6803 and Arabidopsis.";
RL Plant Physiol. 129:321-332(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Gururani M.A., Upadhyaya C.P., Nookaraju A., Kim D.H., Chul S.C.,
RA Park S.W.;
RT "Vitamin E metabolic engineering in potato.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
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 [6]
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12586887; DOI=10.1104/pp.015222;
RA Collakova E., DellaPenna D.;
RT "Homogentisate phytyltransferase activity is limiting for tocopherol
RT biosynthesis in Arabidopsis.";
RL Plant Physiol. 131:632-642(2003).
RN [8]
RP FUNCTION.
RX PubMed=16258032; DOI=10.1105/tpc.105.037036;
RA Havaux M., Eymery F., Porfirova S., Rey P., Doermann P.;
RT "Vitamin E protects against photoinhibition and photooxidative stress in
RT Arabidopsis thaliana.";
RL Plant Cell 17:3451-3469(2005).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16989822; DOI=10.1016/j.febslet.2006.09.002;
RA Sadre R., Gruber J., Frentzen M.;
RT "Characterization of homogentisate prenyltransferases involved in
RT plastoquinone-9 and tocochromanol biosynthesis.";
RL FEBS Lett. 580:5357-5362(2006).
RN [10]
RP NOMENCLATURE.
RX PubMed=16408209; DOI=10.1007/s00425-005-0180-1;
RA Venkatesh T.V., Karunanandaa B., Free D.L., Rottnek J.M., Baszis S.R.,
RA Valentin H.E.;
RT "Identification and characterization of an Arabidopsis homogentisate
RT phytyltransferase paralog.";
RL Planta 223:1134-1144(2006).
RN [11]
RP FUNCTION.
RX PubMed=17012603; DOI=10.1105/tpc.105.039404;
RA Maeda H., Song W., Sage T.L., DellaPenna D.;
RT "Tocopherols play a crucial role in low-temperature adaptation and phloem
RT loading in Arabidopsis.";
RL Plant Cell 18:2710-2732(2006).
RN [12]
RP FUNCTION.
RX PubMed=18314499; DOI=10.1105/tpc.107.054718;
RA Maeda H., Sage T.L., Isaac G., Welti R., Dellapenna D.;
RT "Tocopherols modulate extraplastidic polyunsaturated fatty acid metabolism
RT in Arabidopsis at low temperature.";
RL Plant Cell 20:452-470(2008).
RN [13]
RP FUNCTION.
RX PubMed=20691023; DOI=10.1111/j.1467-7652.2010.00509.x;
RA Xi D.M., Liu W.S., Yang G.D., Wu C.A., Zheng C.C.;
RT "Seed-specific overexpression of antioxidant genes in Arabidopsis enhances
RT oxidative stress tolerance during germination and early seedling growth.";
RL Plant Biotechnol. J. 8:796-806(2010).
RN [14]
RP FUNCTION.
RX PubMed=20837525; DOI=10.1073/pnas.1006971107;
RA Mene-Saffrane L., Jones A.D., DellaPenna D.;
RT "Plastochromanol-8 and tocopherols are essential lipid-soluble antioxidants
RT during seed desiccation and quiescence in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17815-17820(2010).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21223386; DOI=10.1111/j.1365-313x.2010.04417.x;
RA Yang W., Cahoon R.E., Hunter S.C., Zhang C., Han J., Borgschulte T.,
RA Cahoon E.B.;
RT "Vitamin E biosynthesis: functional characterization of the monocot
RT homogentisate geranylgeranyl transferase.";
RL Plant J. 65:206-217(2011).
CC -!- FUNCTION: Involved in the synthesis of tocopherol (vitamin E).
CC Catalyzes the condensation of homogentisate and phytyl diphosphate to
CC form dimethylphytylhydrquinone. Low activity with geranylgeranyl
CC diphosphate as substrate, but no activity with farnesyl diphosphate or
CC solanesyl diphosphate. Tocopherol functions to limit lipid oxidation
CC during seed desiccation, quiescence and germination and early seedling
CC development. Protects thylakoid membrane lipids from photooxidation and
CC is required for low-temperature adaptation.
CC {ECO:0000269|PubMed:11706191, ECO:0000269|PubMed:12011362,
CC ECO:0000269|PubMed:12586887, ECO:0000269|PubMed:16258032,
CC ECO:0000269|PubMed:16989822, ECO:0000269|PubMed:17012603,
CC ECO:0000269|PubMed:18314499, ECO:0000269|PubMed:20691023,
CC ECO:0000269|PubMed:20837525, ECO:0000269|PubMed:21223386}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + homogentisate + phytyl diphosphate = 2-methyl-6-phytyl-
CC 1,4-benzene-1,4-diol + CO2 + diphosphate; Xref=Rhea:RHEA:37975,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16169, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:75434, ChEBI:CHEBI:75920;
CC EC=2.5.1.115; Evidence={ECO:0000269|PubMed:16989822};
CC -!- PATHWAY: Cofactor biosynthesis; tocopherol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:21223386}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Reduced seed longevity, severe seedling growth
CC defects during germination and high levels of lipid hydroperoxides and
CC hydroxy fatty acids. {ECO:0000269|PubMed:12586887}.
CC -!- MISCELLANEOUS: Seeds and plants overexpressing HPT1 accumulate
CC increased levels of tocopherol.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC09029.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF324344; AAL35412.1; -; mRNA.
DR EMBL; AY089963; AAM10489.1; -; mRNA.
DR EMBL; GU198365; ADA57641.1; -; mRNA.
DR EMBL; AC003673; AAC09029.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06831.1; -; Genomic_DNA.
DR EMBL; AY063893; AAL36249.1; -; mRNA.
DR EMBL; AY113993; AAM45041.1; -; mRNA.
DR PIR; T01623; T01623.
DR RefSeq; NP_849984.1; NM_179653.4.
DR AlphaFoldDB; Q8VWJ1; -.
DR SMR; Q8VWJ1; -.
DR STRING; 3702.AT2G18950.1; -.
DR SwissLipids; SLP:000001495; -.
DR iPTMnet; Q8VWJ1; -.
DR PaxDb; Q8VWJ1; -.
DR PRIDE; Q8VWJ1; -.
DR ProteomicsDB; 228744; -.
DR EnsemblPlants; AT2G18950.1; AT2G18950.1; AT2G18950.
DR GeneID; 816412; -.
DR Gramene; AT2G18950.1; AT2G18950.1; AT2G18950.
DR KEGG; ath:AT2G18950; -.
DR Araport; AT2G18950; -.
DR TAIR; locus:2044440; AT2G18950.
DR eggNOG; ENOG502R0I3; Eukaryota.
DR HOGENOM; CLU_048963_0_0_1; -.
DR InParanoid; Q8VWJ1; -.
DR OMA; FYQFIWK; -.
DR OrthoDB; 1231215at2759; -.
DR PhylomeDB; Q8VWJ1; -.
DR BRENDA; 2.5.1.115; 399.
DR UniPathway; UPA00160; -.
DR PRO; PR:Q8VWJ1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VWJ1; baseline and differential.
DR Genevisible; Q8VWJ1; AT.
DR GO; GO:0009507; C:chloroplast; ISS:TAIR.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0010176; F:homogentisate phytyltransferase activity; IDA:TAIR.
DR GO; GO:0071555; P:cell wall organization; IMP:TAIR.
DR GO; GO:0009915; P:phloem sucrose loading; IMP:TAIR.
DR GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:TAIR.
DR GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; IMP:TAIR.
DR GO; GO:0010189; P:vitamin E biosynthetic process; IMP:TAIR.
DR CDD; cd13960; PT_UbiA_HPT1; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR InterPro; IPR044502; AtHST-like.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR044878; UbiA_sf.
DR Pfam; PF01040; UbiA; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Reference proteome; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..393
FT /note="Homogentisate phytyltransferase 1, chloroplastic"
FT /id="PRO_0000409868"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 393 AA; 43909 MW; 6C585625394FF6AC CRC64;
MESLLSSSSL VSAAGGFCWK KQNLKLHSLS EIRVLRCDSS KVVAKPKFRN NLVRPDGQGS
SLLLYPKHKS RFRVNATAGQ PEAFDSNSKQ KSFRDSLDAF YRFSRPHTVI GTVLSILSVS
FLAVEKVSDI SPLLFTGILE AVVAALMMNI YIVGLNQLSD VEIDKVNKPY LPLASGEYSV
NTGIAIVASF SIMSFWLGWI VGSWPLFWAL FVSFMLGTAY SINLPLLRWK RFALVAAMCI
LAVRAIIVQI AFYLHIQTHV FGRPILFTRP LIFATAFMSF FSVVIALFKD IPDIEGDKIF
GIRSFSVTLG QKRVFWTCVT LLQMAYAVAI LVGATSPFIW SKVISVVGHV ILATTLWARA
KSVDLSSKTE ITSCYMFIWK LFYAEYLLLP FLK
