PP264_ARATH
ID PP264_ARATH Reviewed; 665 AA.
AC Q9SNB7;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein LOW PHOTOSYNTHETIC EFFICIENCY 1, chloroplastic {ECO:0000303|PubMed:29891689};
DE Flags: Precursor;
GN Name=LPE1 {ECO:0000303|PubMed:29891689};
GN OrderedLocusNames=At3g46610 {ECO:0000312|Araport:AT3G46610};
GN ORFNames=F12A12.130 {ECO:0000312|EMBL:CAB62331.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP GENE FAMILY.
RX PubMed=15269332; DOI=10.1105/tpc.104.022236;
RA Lurin C., Andres C., Aubourg S., Bellaoui M., Bitton F., Bruyere C.,
RA Caboche M., Debast C., Gualberto J., Hoffmann B., Lecharny A., Le Ret M.,
RA Martin-Magniette M.-L., Mireau H., Peeters N., Renou J.-P., Szurek B.,
RA Taconnat L., Small I.;
RT "Genome-wide analysis of Arabidopsis pentatricopeptide repeat proteins
RT reveals their essential role in organelle biogenesis.";
RL Plant Cell 16:2089-2103(2004).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH HCF173, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=29891689; DOI=10.1073/pnas.1807364115;
RA Jin H., Fu M., Duan Z., Duan S., Li M., Dong X., Liu B., Feng D., Wang J.,
RA Peng L., Wang H.-B.;
RT "LOW PHOTOSYNTHETIC EFFICIENCY 1 is required for light-regulated
RT photosystem II biogenesis in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E6075-E6084(2018).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=30844105; DOI=10.1111/tpj.14308;
RA Williams-Carrier R., Brewster C., Belcher S.E., Rojas M.,
RA Chotewutmontri P., Ljungdahl S., Barkan A.;
RT "The Arabidopsis pentatricopeptide repeat protein LPE1 and its maize
RT ortholog are required for translation of the chloroplast psbJ RNA.";
RL Plant J. 99:56-66(2019).
CC -!- FUNCTION: Required for light-regulated photosystem II (PSII) biogenesis
CC and grana thylakoids formation by binding to the 5' UTR of PSII subunit
CC mRNAs (e.g. psbJ, psbN and psbA) in a light-dependent manner through a
CC redox-based mechanism, and facilitating the association of HCF173 with
CC target mRNAs, which encodes PSII reaction center proteins (e.g. J, N
CC and D1), thus regulating its expression by modulating ribosome loading.
CC {ECO:0000269|PubMed:29891689, ECO:0000269|PubMed:30844105}.
CC -!- SUBUNIT: Interacts with HCF173. {ECO:0000269|PubMed:29891689}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:29891689}; Peripheral membrane protein
CC {ECO:0000269|PubMed:29891689}; Stromal side
CC {ECO:0000269|PubMed:29891689}. Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:29891689}. Note=Predominantly present at thylakoid
CC membranes. {ECO:0000269|PubMed:29891689}.
CC -!- DISRUPTION PHENOTYPE: Retardation of photoautotrophic growth
CC (PubMed:29891689). Reduced efficiency of photosystem II (PSII) subunit
CC mRNAs (e.g. psbJ, psbN and psbA) ribosome loading and impaired
CC synthesis of PSII reaction center proteins (e.g. J, N and D1) leading
CC to reduced PSII activity and biogenesis, as well as reduced grana
CC thylakoid formation (PubMed:29891689, PubMed:30844105). Reduced
CC production of PSII subunits D1, D2, CP43, CP47, PsbE, PsbF, and PsbO,
CC and, to a lower extent, of PSI subunits PsaA and PsaB (PubMed:29891689,
CC PubMed:30844105). High levels of nonphotochemical quenching (NPQ)
CC (PubMed:29891689). {ECO:0000269|PubMed:29891689,
CC ECO:0000269|PubMed:30844105}.
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX825001; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Pentatricopeptide repeat proteins;
CC URL="https://ppr.plantenergy.uwa.edu.au";
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DR EMBL; AL133314; CAB62331.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78181.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65376.1; -; Genomic_DNA.
DR EMBL; BX825001; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T45598; T45598.
DR RefSeq; NP_001319696.1; NM_001339269.1.
DR RefSeq; NP_190245.1; NM_114528.2.
DR AlphaFoldDB; Q9SNB7; -.
DR SMR; Q9SNB7; -.
DR STRING; 3702.AT3G46610.1; -.
DR PaxDb; Q9SNB7; -.
DR PRIDE; Q9SNB7; -.
DR ProteomicsDB; 248954; -.
DR EnsemblPlants; AT3G46610.1; AT3G46610.1; AT3G46610.
DR EnsemblPlants; AT3G46610.2; AT3G46610.2; AT3G46610.
DR GeneID; 823814; -.
DR Gramene; AT3G46610.1; AT3G46610.1; AT3G46610.
DR Gramene; AT3G46610.2; AT3G46610.2; AT3G46610.
DR KEGG; ath:AT3G46610; -.
DR Araport; AT3G46610; -.
DR TAIR; locus:2075165; AT3G46610.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_021023_0_0_1; -.
DR InParanoid; Q9SNB7; -.
DR OMA; LAYEMYM; -.
DR OrthoDB; 1344243at2759; -.
DR PhylomeDB; Q9SNB7; -.
DR PRO; PR:Q9SNB7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SNB7; baseline and differential.
DR Genevisible; Q9SNB7; AT.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0043022; F:ribosome binding; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0008494; F:translation activator activity; IMP:TAIR.
DR GO; GO:0010207; P:photosystem II assembly; IMP:UniProtKB.
DR GO; GO:0032544; P:plastid translation; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IDA:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR033443; PPR_long.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF01535; PPR; 1.
DR Pfam; PF13812; PPR_3; 1.
DR Pfam; PF17177; PPR_long; 1.
DR TIGRFAMs; TIGR00756; PPR; 5.
DR PROSITE; PS51375; PPR; 12.
PE 1: Evidence at protein level;
KW Chloroplast; Membrane; Plastid; Reference proteome; Repeat; RNA-binding;
KW Thylakoid; Transit peptide.
FT TRANSIT 1..68
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 69..665
FT /note="Protein LOW PHOTOSYNTHETIC EFFICIENCY 1,
FT chloroplastic"
FT /id="PRO_0000356123"
FT REPEAT 145..179
FT /note="PPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 181..217
FT /note="PPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 218..252
FT /note="PPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 253..283
FT /note="PPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 309..344
FT /note="PPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 345..375
FT /note="PPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 380..414
FT /note="PPR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 422..456
FT /note="PPR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 457..491
FT /note="PPR 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 492..526
FT /note="PPR 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 527..561
FT /note="PPR 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 562..596
FT /note="PPR 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 597..631
FT /note="PPR 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
SQ SEQUENCE 665 AA; 75175 MW; D2D9172C819596D9 CRC64;
MQALSILPLK SGLLVGSRLE FELDCSCFVV SPKTTRKRLC FLEQACFGSS SSISSFIFVS
SNRKVLFLCE PKRSLLGSSF GVGWATEQRE LELGEEEVST EDLSSANGGE KNNLRVDVRE
LAFSLRAAKT ADDVDAVLKD KGELPLQVFC AMIKGFGKDK RLKPAVAVVD WLKRKKSESG
GVIGPNLFIY NSLLGAMRGF GEAEKILKDM EEEGIVPNIV TYNTLMVIYM EEGEFLKALG
ILDLTKEKGF EPNPITYSTA LLVYRRMEDG MGALEFFVEL REKYAKREIG NDVGYDWEFE
FVKLENFIGR ICYQVMRRWL VKDDNWTTRV LKLLNAMDSA GVRPSREEHE RLIWACTREE
HYIVGKELYK RIRERFSEIS LSVCNHLIWL MGKAKKWWAA LEIYEDLLDE GPEPNNLSYE
LVVSHFNILL SAASKRGIWR WGVRLLNKME DKGLKPQRRH WNAVLVACSK ASETTAAIQI
FKAMVDNGEK PTVISYGALL SALEKGKLYD EAFRVWNHMI KVGIEPNLYA YTTMASVLTG
QQKFNLLDTL LKEMASKGIE PSVVTFNAVI SGCARNGLSG VAYEWFHRMK SENVEPNEIT
YEMLIEALAN DAKPRLAYEL HVKAQNEGLK LSSKPYDAVV KSAETYGATI DLNLLGPRPD
KKNRP
