PP314_ARATH
ID PP314_ARATH Reviewed; 702 AA.
AC Q8GWE0; F4JLT2; O23484; Q9LF83;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 3.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Pentatricopeptide repeat-containing protein At4g16390, chloroplastic {ECO:0000305};
DE AltName: Full=Chloroplastic RNA-binding protein P67 {ECO:0000303|PubMed:11034340};
DE AltName: Full=Protein SUPPRESSOR OF VARIEGATION 7 {ECO:0000303|PubMed:20935174};
DE Flags: Precursor;
GN Name=P67 {ECO:0000303|PubMed:11034340};
GN Synonyms=SVR7 {ECO:0000303|PubMed:20935174}; OrderedLocusNames=At4g16390;
GN ORFNames=dl4225w, FCAALL.354;
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 [GENOMIC DNA], RNA-BINDING, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11034340; DOI=10.1016/s0014-5793(00)01935-9;
RA Lahmy S., Barneche F., Derancourt J., Filipowicz W., Delseny M.,
RA Echeverria M.;
RT "A chloroplastic RNA-binding protein is a new member of the PPR family.";
RL FEBS Lett. 480:255-260(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=18431481; DOI=10.1371/journal.pone.0001994;
RA Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q.,
RA van Wijk K.J.;
RT "Sorting signals, N-terminal modifications and abundance of the chloroplast
RT proteome.";
RL PLoS ONE 3:E1994-E1994(2008).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21187014; DOI=10.1186/1471-2229-10-287;
RA Liu X., Rodermel S.R., Yu F.;
RT "A var2 leaf variegation suppressor locus, SUPPRESSOR OF VARIEGATION3,
RT encodes a putative chloroplast translation elongation factor that is
RT important for chloroplast development in the cold.";
RL BMC Plant Biol. 10:287-287(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20935174; DOI=10.1104/pp.110.164111;
RA Liu X., Yu F., Rodermel S.;
RT "An Arabidopsis pentatricopeptide repeat protein, SUPPRESSOR OF
RT VARIEGATION7, is required for FtsH-mediated chloroplast biogenesis.";
RL Plant Physiol. 154:1588-1601(2010).
RN [10]
RP FUNCTION.
RX PubMed=23076438; DOI=10.1007/s10265-012-0527-1;
RA Zoschke R., Qu Y., Zubo Y.O., Boerner T., Schmitz-Linneweber C.;
RT "Mutation of the pentatricopeptide repeat-SMR protein SVR7 impairs
RT accumulation and translation of chloroplast ATP synthase subunits in
RT Arabidopsis thaliana.";
RL J. Plant Res. 126:403-414(2013).
CC -!- FUNCTION: Involved in chloroplast RNA processing. Can bind RNA
CC (PubMed:11034340). Involved in chloroplast development
CC (PubMed:21187014). Involved in chloroplast ribosomal RNA (rRNA)
CC processing and/or translation. Required for FtsH-mediated chloroplast
CC biogenesis (PubMed:20935174). Involved in translation and accumulation
CC of chloroplast ATP synthase subunits (PubMed:23076438).
CC {ECO:0000269|PubMed:11034340, ECO:0000269|PubMed:20935174,
CC ECO:0000269|PubMed:21187014, ECO:0000269|PubMed:23076438}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:11034340, ECO:0000269|PubMed:18431481,
CC ECO:0000269|PubMed:20935174}. Note=Accumulates in discrete foci within
CC the chloroplast. {ECO:0000269|PubMed:20935174}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers and at lower levels
CC in stems and flower buds. {ECO:0000269|PubMed:11034340}.
CC -!- DISRUPTION PHENOTYPE: Reduced plant size and pale-green leaf phenotype.
CC {ECO:0000269|PubMed:20935174, ECO:0000269|PubMed:21187014}.
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10416.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB78681.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Pentatricopeptide repeat proteins;
CC URL="https://ppr.plantenergy.uwa.edu.au";
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DR EMBL; AJ243545; CAC01928.1; -; Genomic_DNA.
DR EMBL; Z97341; CAB10416.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL161543; CAB78681.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP002687; AEE83741.1; -; Genomic_DNA.
DR EMBL; AK118908; BAC43491.1; -; mRNA.
DR PIR; F71430; F71430.
DR RefSeq; NP_193372.6; NM_117734.8.
DR AlphaFoldDB; Q8GWE0; -.
DR SMR; Q8GWE0; -.
DR BioGRID; 12626; 1.
DR IntAct; Q8GWE0; 1.
DR STRING; 3702.AT4G16390.1; -.
DR PaxDb; Q8GWE0; -.
DR PRIDE; Q8GWE0; -.
DR ProteomicsDB; 248981; -.
DR EnsemblPlants; AT4G16390.1; AT4G16390.1; AT4G16390.
DR GeneID; 827333; -.
DR Gramene; AT4G16390.1; AT4G16390.1; AT4G16390.
DR KEGG; ath:AT4G16390; -.
DR Araport; AT4G16390; -.
DR TAIR; locus:2130549; AT4G16390.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_018319_0_0_1; -.
DR InParanoid; Q8GWE0; -.
DR OMA; RPWQAKK; -.
DR OrthoDB; 1344243at2759; -.
DR PRO; PR:Q8GWE0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GWE0; baseline and differential.
DR Genevisible; Q8GWE0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0031425; P:chloroplast RNA processing; IMP:TAIR.
DR GO; GO:0045727; P:positive regulation of translation; IMP:TAIR.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR033443; PPR_long.
DR InterPro; IPR002625; Smr_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF01535; PPR; 1.
DR Pfam; PF13041; PPR_2; 1.
DR Pfam; PF13812; PPR_3; 1.
DR Pfam; PF17177; PPR_long; 1.
DR SMART; SM00463; SMR; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR TIGRFAMs; TIGR00756; PPR; 8.
DR PROSITE; PS51375; PPR; 10.
DR PROSITE; PS50828; SMR; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Nucleotide-binding; Plastid; Reference proteome; Repeat;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..702
FT /note="Pentatricopeptide repeat-containing protein
FT At4g16390, chloroplastic"
FT /id="PRO_0000363432"
FT REPEAT 174..208
FT /note="PPR 1"
FT REPEAT 209..243
FT /note="PPR 2"
FT REPEAT 244..278
FT /note="PPR 3"
FT REPEAT 279..313
FT /note="PPR 4"
FT REPEAT 314..348
FT /note="PPR 5"
FT REPEAT 349..383
FT /note="PPR 6"
FT REPEAT 384..414
FT /note="PPR 7"
FT REPEAT 420..454
FT /note="PPR 8"
FT REPEAT 455..489
FT /note="PPR 9"
FT DOMAIN 603..688
FT /note="Smr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00321"
FT CONFLICT 398..399
FT /note="NR -> IG (in Ref. 1; CAC01928 and 5; BAC43491)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="Y -> H (in Ref. 2; CAB10416 and 3; CAB78681)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="E -> K (in Ref. 2; CAB10416 and 3; CAB78681)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="M -> I (in Ref. 2; CAB10416 and 3; CAB78681)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="S -> F (in Ref. 1; CAC01928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 702 AA; 78243 MW; 04529D5A9B655972 CRC64;
MSFHHLCSSP SSLLHDPLPL CNLLSVYPKS TPRSFLSSYN PNSSHFHSRN LLQATHVSVQ
EAIPQSEKSK LVDVDLPIPE PTASKSYVWV NPKSPRASQL RRKSYDSRYS SLIKLAESLD
ACKPNEADVC DVITGFGGKL FEQDAVVTLN NMTNPETAPL VLNNLLETMK PSREVILYNV
TMKVFRKSKD LEKSEKLFDE MLERGIKPDN ATFTTIISCA RQNGVPKRAV EWFEKMSSFG
CEPDNVTMAA MIDAYGRAGN VDMALSLYDR ARTEKWRIDA VTFSTLIRIY GVSGNYDGCL
NIYEEMKALG VKPNLVIYNR LIDSMGRAKR PWQAKIIYKD LITNGFTPNW STYAALVRAY
GRARYGDDAL AIYREMKEKG LSLTVILYNT LLSMCADNRY VDEAFEIFQD MKNCETCDPD
SWTFSSLITV YACSGRVSEA EAALLQMREA GFEPTLFVLT SVIQCYGKAK QVDDVVRTFD
QVLELGITPD DRFCGCLLNV MTQTPSEEIG KLIGCVEKAK PKLGQVVKML VEEQNCEEGV
FKKEASELID SIGSDVKKAY LNCLIDLCVN LNKLERACEI LQLGLEYDIY TGLQSKSATQ
WSLHLKSLSL GAALTALHVW MNDLSEAALE SGEEFPPLLG INTGHGKHKY SDKGLAAVFE
SHLKELNAPF HEAPDKVGWF LTTSVAAKAW LESRRSAGGV SA
