PPR10_MAIZE
ID PPR10_MAIZE Reviewed; 786 AA.
AC B8Y6I0;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Pentatricopeptide repeat-containing protein 10, chloroplastic {ECO:0000303|PubMed:19424177};
DE Short=ZmPPR10 {ECO:0000303|PubMed:25609698};
DE Flags: Precursor;
GN Name=PPR10 {ECO:0000303|PubMed:19424177};
GN ORFNames=ZEAMMB73_Zm00001d036698 {ECO:0000312|EMBL:AQK81740.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19424177; DOI=10.1038/emboj.2009.121;
RA Pfalz J., Bayraktar O.A., Prikryl J., Barkan A.;
RT "Site-specific binding of a PPR protein defines and stabilizes 5' and 3'
RT mRNA termini in chloroplasts.";
RL EMBO J. 28:2042-2052(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [4]
RP FUNCTION.
RX PubMed=21173259; DOI=10.1073/pnas.1012076108;
RA Prikryl J., Rojas M., Schuster G., Barkan A.;
RT "Mechanism of RNA stabilization and translational activation by a
RT pentatricopeptide repeat protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:415-420(2011).
RN [5]
RP FUNCTION.
RX PubMed=22156165; DOI=10.1093/nar/gkr1137;
RA Zhelyazkova P., Hammani K., Rojas M., Voelker R., Vargas-Suarez M.,
RA Boerner T., Barkan A.;
RT "Protein-mediated protection as the predominant mechanism for defining
RT processed mRNA termini in land plant chloroplasts.";
RL Nucleic Acids Res. 40:3092-3105(2012).
RN [6]
RP FUNCTION.
RX PubMed=25609698; DOI=10.1093/nar/gkv027;
RA Gully B.S., Cowieson N., Stanley W.A., Shearston K., Small I.D., Barkan A.,
RA Bond C.S.;
RT "The solution structure of the pentatricopeptide repeat protein PPR10 upon
RT binding atpH RNA.";
RL Nucleic Acids Res. 43:1918-1926(2015).
RN [7]
RP FUNCTION.
RX PubMed=30125002; DOI=10.1093/nar/gky737;
RA Rojas M., Ruwe H., Miranda R.G., Zoschke R., Hase N.,
RA Schmitz-Linneweber C., Barkan A.;
RT "Unexpected functional versatility of the pentatricopeptide repeat proteins
RT PGR3, PPR5 and PPR10.";
RL Nucleic Acids Res. 46:10448-10459(2018).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF 61-786 IN COMPLEX WITH RNA, AND
RP HOMODIMER.
RX PubMed=24162847; DOI=10.1038/nature12651;
RA Yin P., Li Q., Yan C., Liu Y., Liu J., Yu F., Wang Z., Long J., He J.,
RA Wang H.W., Wang J., Zhu J.K., Shi Y., Yan N.;
RT "Structural basis for the modular recognition of single-stranded RNA by PPR
RT proteins.";
RL Nature 504:168-171(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 69-786 IN COMPLEX WITH RNA, AND
RP HOMODIMER.
RX PubMed=25231995; DOI=10.1074/jbc.m114.575472;
RA Li Q., Yan C., Xu H., Wang Z., Long J., Li W., Wu J., Yin P., Yan N.;
RT "Examination of the dimerization states of the single-stranded RNA
RT recognition protein pentatricopeptide repeat 10 (PPR10).";
RL J. Biol. Chem. 289:31503-31512(2014).
CC -!- FUNCTION: Involved in chloroplast mRNA stability (PubMed:19424177,
CC PubMed:21173259, PubMed:22156165). Binds specifically to two intergenic
CC RNA regions of similar sequence located in the chloroplast atpH 5'-UTR
CC and psaJ 3'-UTR, and serves as a barrier to RNA decay
CC (PubMed:19424177). Binding to a specific site in the intergenic region
CC of the chloroplast atpH is sufficient to block 5'-3' and 3'-5'
CC exonucleases (PubMed:21173259). Acts as protein barrier to block mRNA
CC degradation by exonucleases, and defines processed mRNA termini in
CC chloroplasts (PubMed:22156165). Remodels the structure of the atpH
CC ribosome-binding site in a manner that can account for its ability to
CC enhance translation (PubMed:21173259). Stabilizes a RNA 3'-end
CC downstream from psaI (PubMed:30125002). Binds atpH RNA as a monomer
CC (PubMed:25609698). {ECO:0000269|PubMed:19424177,
CC ECO:0000269|PubMed:21173259, ECO:0000269|PubMed:22156165,
CC ECO:0000269|PubMed:25609698, ECO:0000269|PubMed:30125002}.
CC -!- SUBUNIT: Forms homodimers. {ECO:0000269|PubMed:24162847,
CC ECO:0000269|PubMed:25231995}.
CC -!- INTERACTION:
CC B8Y6I0; B8Y6I0: PPR10; NbExp=3; IntAct=EBI-16079897, EBI-16079897;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19424177}.
CC -!- DISRUPTION PHENOTYPE: Yellow-green seedling phenotype
CC (PubMed:19424177). Seedling lethality after the development of three
CC leaves (PubMed:19424177). Defects in plastid mRNA metabolism and
CC reduced levels of subunits of several photosynthetic enzyme complexes
CC (PubMed:19424177). {ECO:0000269|PubMed:19424177}.
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
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DR EMBL; FJ490677; ACL01094.1; -; mRNA.
DR EMBL; CM000782; AQK81740.1; -; Genomic_DNA.
DR EMBL; BT063468; ACN28165.1; -; mRNA.
DR RefSeq; NP_001157212.1; NM_001163740.1.
DR PDB; 4M57; X-ray; 2.86 A; A=61-786.
DR PDB; 4M59; X-ray; 2.46 A; A/B=69-786.
DR PDB; 4OE1; X-ray; 2.80 A; A/B=69-786.
DR PDBsum; 4M57; -.
DR PDBsum; 4M59; -.
DR PDBsum; 4OE1; -.
DR AlphaFoldDB; B8Y6I0; -.
DR SMR; B8Y6I0; -.
DR DIP; DIP-60592N; -.
DR STRING; 4577.GRMZM2G177169_P01; -.
DR PaxDb; B8Y6I0; -.
DR PRIDE; B8Y6I0; -.
DR EnsemblPlants; Zm00001eb274840_T001; Zm00001eb274840_P001; Zm00001eb274840.
DR GeneID; 100302579; -.
DR Gramene; Zm00001eb274840_T001; Zm00001eb274840_P001; Zm00001eb274840.
DR KEGG; zma:100302579; -.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_002706_49_8_1; -.
DR OMA; HKYVNRV; -.
DR OrthoDB; 1344243at2759; -.
DR Proteomes; UP000007305; Chromosome 6.
DR ExpressionAtlas; B8Y6I0; baseline and differential.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048255; P:mRNA stabilization; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 7.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF01535; PPR; 3.
DR Pfam; PF12854; PPR_1; 2.
DR Pfam; PF13041; PPR_2; 4.
DR Pfam; PF13812; PPR_3; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR TIGRFAMs; TIGR00756; PPR; 13.
DR PROSITE; PS51375; PPR; 18.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; mRNA processing; Plastid; Reference proteome;
KW Repeat; RNA-binding; Transit peptide.
FT TRANSIT 1..95
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 96..786
FT /note="Pentatricopeptide repeat-containing protein 10,
FT chloroplastic"
FT /id="PRO_0000446264"
FT REPEAT 137..167
FT /note="PPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 173..207
FT /note="PPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 208..243
FT /note="PPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 244..278
FT /note="PPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 279..313
FT /note="PPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 314..348
FT /note="PPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 349..383
FT /note="PPR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 384..418
FT /note="PPR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 419..453
FT /note="PPR 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 454..488
FT /note="PPR 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 489..523
FT /note="PPR 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 524..558
FT /note="PPR 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 560..594
FT /note="PPR 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 595..629
FT /note="PPR 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 630..664
FT /note="PPR 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 666..700
FT /note="PPR 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 701..735
FT /note="PPR 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 736..770
FT /note="PPR 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:4M57"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 261..272
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 280..292
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 296..308
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 350..363
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 366..378
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 385..396
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 401..414
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 420..427
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 435..448
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 455..468
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 471..481
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 482..485
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 490..503
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 506..517
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 526..536
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 537..539
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 541..551
FT /evidence="ECO:0007829|PDB:4M59"
FT STRAND 554..557
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 561..572
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 577..587
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 588..591
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 596..607
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 608..610
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 612..623
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 631..643
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 648..658
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 667..680
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 683..695
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 702..713
FT /evidence="ECO:0007829|PDB:4M59"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:4M59"
FT TURN 719..724
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 725..727
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 729..731
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 737..747
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 754..761
FT /evidence="ECO:0007829|PDB:4M59"
FT HELIX 778..781
FT /evidence="ECO:0007829|PDB:4M59"
SQ SEQUENCE 786 AA; 86224 MW; 3B2DD7F3FE777F1B CRC64;
MEATGRGLFP NKPTLPAGPR KRGPLLPAAP PPPSPSSLPL DSLLLHLTAP APAPAPAPRR
SHQTPTPPHS FLSPDAQVLV LAISSHPLPT LAAFLASRRD ELLRADITSL LKALELSGHW
EWALALLRWA GKEGAADASA LEMVVRALGR EGQHDAVCAL LDETPLPPGS RLDVRAYTTV
LHALSRAGRY ERALELFAEL RRQGVAPTLV TYNVVLDVYG RMGRSWPRIV ALLDEMRAAG
VEPDGFTAST VIAACCRDGL VDEAVAFFED LKARGHAPCV VTYNALLQVF GKAGNYTEAL
RVLGEMEQNG CQPDAVTYNE LAGTYARAGF FEEAARCLDT MASKGLLPNA FTYNTVMTAY
GNVGKVDEAL ALFDQMKKTG FVPNVNTYNL VLGMLGKKSR FTVMLEMLGE MSRSGCTPNR
VTWNTMLAVC GKRGMEDYVT RVLEGMRSCG VELSRDTYNT LIAAYGRCGS RTNAFKMYNE
MTSAGFTPCI TTYNALLNVL SRQGDWSTAQ SIVSKMRTKG FKPNEQSYSL LLQCYAKGGN
VAGIAAIENE VYGSGAVFPS WVILRTLVIA NFKCRRLDGM ETAFQEVKAR GYNPDLVIFN
SMLSIYAKNG MYSKATEVFD SIKRSGLSPD LITYNSLMDM YAKCSESWEA EKILNQLKCS
QTMKPDVVSY NTVINGFCKQ GLVKEAQRVL SEMVADGMAP CAVTYHTLVG GYSSLEMFSE
AREVIGYMVQ HGLKPMELTY RRVVESYCRA KRFEEARGFL SEVSETDLDF DKKALEAYIE
DAQFGR
