ATP4_MAIZE
ID ATP4_MAIZE Reviewed; 691 AA.
AC B4F8Z1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Pentatricopeptide repeat-containing protein ATP4, chloroplastic {ECO:0000305};
DE AltName: Full=ATP synthase 4 {ECO:0000303|PubMed:22708543};
DE Flags: Precursor;
GN Name=ATP4 {ECO:0000303|PubMed:22708543};
GN ORFNames=ZEAMMB73_Zm00001d028221 {ECO:0000312|EMBL:ONL95104.1};
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 [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 [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22708543; DOI=10.1111/j.1365-313x.2012.05081.x;
RA Zoschke R., Kroeger T., Belcher S., Schoettler M.A., Barkan A.,
RA Schmitz-Linneweber C.;
RT "The pentatricopeptide repeat-SMR protein ATP4 promotes translation of the
RT chloroplast atpB/E mRNA.";
RL Plant J. 72:547-558(2012).
RN [4]
RP FUNCTION.
RX PubMed=23735295; DOI=10.1105/tpc.113.111567;
RA Zoschke R., Watkins K.P., Barkan A.;
RT "A rapid ribosome profiling method elucidates chloroplast ribosome behavior
RT in vivo.";
RL Plant Cell 25:2265-2275(2013).
CC -!- FUNCTION: Involved in translation and accumulation of chloroplast ATP
CC synthase subunits. Interacts with the 5'-UTR of the chloroplast
CC bicistronic atpB and atpE mRNA and activates its translation by
CC facilitating ribosome association with the mRNA (PubMed:22708543).
CC Required for accumulation and activity of the chloroplast ATP synthase.
CC Enhances atpA translation and is required for accumulation of specific
CC processed atpF and psaJ transcripts (PubMed:22708543, PubMed:23735295).
CC Required for the stabilization of bicistronic rpl16 and rpl14 mRNAs
CC (PubMed:23735295). {ECO:0000269|PubMed:22708543,
CC ECO:0000269|PubMed:23735295}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:22708543}.
CC -!- DISRUPTION PHENOTYPE: Pale green leaf phenotype.
CC {ECO:0000269|PubMed:22708543}.
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
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DR EMBL; CM007647; ONL95104.1; -; Genomic_DNA.
DR EMBL; BT033579; ACF78584.1; -; mRNA.
DR RefSeq; NP_001130387.1; NM_001136915.1.
DR AlphaFoldDB; B4F8Z1; -.
DR SMR; B4F8Z1; -.
DR STRING; 4577.GRMZM2G128665_P01; -.
DR PaxDb; B4F8Z1; -.
DR PRIDE; B4F8Z1; -.
DR EnsemblPlants; Zm00001eb008730_T001; Zm00001eb008730_P001; Zm00001eb008730.
DR GeneID; 100191483; -.
DR Gramene; Zm00001eb008730_T001; Zm00001eb008730_P001; Zm00001eb008730.
DR KEGG; zma:100191483; -.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_018319_0_0_1; -.
DR OMA; RPWQAKK; -.
DR OrthoDB; 1344243at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; B4F8Z1; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
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; 2.
DR Pfam; PF17177; PPR_long; 1.
DR SMART; SM00463; SMR; 1.
DR TIGRFAMs; TIGR00756; PPR; 8.
DR PROSITE; PS51375; PPR; 10.
DR PROSITE; PS50828; SMR; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; mRNA processing; Plastid; Reference proteome; Repeat;
KW RNA-binding; Transit peptide; Translation regulation.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..691
FT /note="Pentatricopeptide repeat-containing protein ATP4,
FT chloroplastic"
FT /id="PRO_0000441904"
FT REPEAT 163..197
FT /note="PPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 198..232
FT /note="PPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 233..267
FT /note="PPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 268..302
FT /note="PPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 303..337
FT /note="PPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 338..372
FT /note="PPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 373..403
FT /note="PPR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 411..445
FT /note="PPR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 446..480
FT /note="PPR 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 546..580
FT /note="PPR 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT DOMAIN 592..677
FT /note="Smr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00321"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 75581 MW; C7F82CF9BC2BF6CA CRC64;
MASLPLCRSP SSLLPSWPHR PISASFNPKN PSSPVAAHVS VQETPPQPQD PSPPSDSNPN
GTRPSSSSNT RFLWVNPNSP RAADVARARA GSGRRARLAS AAAALGACET TESAVEAALQ
AAFPEPPSEQ DAVIVLNTAA ATRAETAVLA LRWFLGNAKV RKKVILYNVV LKLLRKKRLW
SETEALWAEM LRDGVQPDNA TFSTVISCAR ACGLHSKAVE WFDKMPEFGC SPDMLTYSAV
IDAYGHAGNS EAALRLYDRA RAEKWQLDPV ICSTVIKVHS TSGNFDGALN VFEEMKAIGV
RPNLVVYNTM LDAMGRALRP WVVKTIHREM VDQQVQPSRA TYCCLLHAYT RARYGEDAMA
VYRLMKDEAM GIDVMLYNML LSMCADIGYV DEAEEIFRDM KASMGAHSKP DSWSYSSMVT
LYSSTANVLS AEGILNEMVE AGFKPNIFVL TSLIRCYGKV GRTDDVVRSF GMLQDLGIIP
DDRFCGCLLS VAANTPAEEL GKVISCIERS NVQLGAVVKL LVDRSSSESF REAARELLRS
SRGVVKMPYC NCLMDLCVNL NQMEKACALL DAAQQLGIYA NIQTRTQTQW SLHLRGLSVG
AALTTLHVWM NDLYTSLQTG NEGLPPLLGI HTGQGKNTYS DRGLAAMFEA HLKELDAPFH
EAPDKAGWFL TTNVAAKQWL ESKAASELVT V
