PPR45_ARATH
ID PPR45_ARATH Reviewed; 866 AA.
AC Q9M9E2; E2FJQ9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Pentatricopeptide repeat-containing protein At1g15510, chloroplastic;
DE AltName: Full=Protein EARLY CHLOROPLAST BIOGENESIS 2 {ECO:0000303|PubMed:19500301};
DE Short=AtECB2 {ECO:0000303|PubMed:19500301};
DE AltName: Full=Protein VANILLA CREAM 1 {ECO:0000303|PubMed:20143129};
DE Flags: Precursor;
GN Name=PCMP-H73;
GN Synonyms=ECB2 {ECO:0000303|PubMed:19500301},
GN VAC1 {ECO:0000303|PubMed:20143129}; OrderedLocusNames=At1g15510;
GN ORFNames=T16N11.2;
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=20143129; DOI=10.1007/s11103-010-9616-5;
RA Tseng C.C., Sung T.Y., Li Y.C., Hsu S.J., Lin C.L., Hsieh M.H.;
RT "Editing of accD and ndhF chloroplast transcripts is partially affected in
RT the Arabidopsis vanilla cream1 mutant.";
RL Plant Mol. Biol. 73:309-323(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [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, AND DISRUPTION PHENOTYPE.
RX PubMed=19500301; DOI=10.1111/j.1365-313x.2009.03930.x;
RA Yu Q.B., Jiang Y., Chong K., Yang Z.N.;
RT "AtECB2, a pentatricopeptide repeat protein, is required for chloroplast
RT transcript accD RNA editing and early chloroplast biogenesis in Arabidopsis
RT thaliana.";
RL Plant J. 59:1011-1023(2009).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF THR-500.
RX PubMed=21294841; DOI=10.1111/j.1744-7909.2011.01030.x;
RA Cao Z.L., Yu Q.B., Sun Y., Lu Y., Cui Y.L., Yang Z.N.;
RT "A point mutation in the pentatricopeptide repeat motif of the AtECB2
RT protein causes delayed chloroplast development.";
RL J. Integr. Plant Biol. 53:258-269(2011).
CC -!- FUNCTION: Regulates the RNA editing of the chloroplast transcript accD,
CC and is essential for the early stages of chloroplast biogenesis
CC (PubMed:20143129, PubMed:19500301, PubMed:21294841). Required for the
CC RNA editing of the chloroplast transcript ndhF (PubMed:20143129,
CC PubMed:21294841). {ECO:0000269|PubMed:19500301,
CC ECO:0000269|PubMed:20143129, ECO:0000269|PubMed:21294841}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Albino cotyledons without primary leaf and
CC seedling lethality under autotrophic growth conditions.
CC {ECO:0000269|PubMed:19500301}.
CC -!- SIMILARITY: Belongs to the PPR family. PCMP-H subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Pentatricopeptide repeat proteins;
CC URL="https://ppr.plantenergy.uwa.edu.au";
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DR EMBL; HM157284; ADK35876.1; -; mRNA.
DR EMBL; AC013453; AAF71977.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29331.1; -; Genomic_DNA.
DR PIR; H86288; H86288.
DR RefSeq; NP_173004.1; NM_101420.2.
DR AlphaFoldDB; Q9M9E2; -.
DR SMR; Q9M9E2; -.
DR STRING; 3702.AT1G15510.1; -.
DR PaxDb; Q9M9E2; -.
DR PRIDE; Q9M9E2; -.
DR ProteomicsDB; 226405; -.
DR EnsemblPlants; AT1G15510.1; AT1G15510.1; AT1G15510.
DR GeneID; 838121; -.
DR Gramene; AT1G15510.1; AT1G15510.1; AT1G15510.
DR KEGG; ath:AT1G15510; -.
DR Araport; AT1G15510; -.
DR TAIR; locus:2196583; AT1G15510.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_002706_15_1_1; -.
DR InParanoid; Q9M9E2; -.
DR OMA; RINNRCF; -.
DR OrthoDB; 1344243at2759; -.
DR PhylomeDB; Q9M9E2; -.
DR PRO; PR:Q9M9E2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9E2; baseline and differential.
DR Genevisible; Q9M9E2; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR GO; GO:0009451; P:RNA modification; IMP:TAIR.
DR Gene3D; 1.25.40.10; -; 6.
DR InterPro; IPR032867; DYW_dom.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF14432; DYW_deaminase; 1.
DR Pfam; PF01535; PPR; 3.
DR Pfam; PF13041; PPR_2; 4.
DR TIGRFAMs; TIGR00756; PPR; 8.
DR PROSITE; PS51375; PPR; 16.
PE 1: Evidence at protein level;
KW Chloroplast; Plastid; Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..866
FT /note="Pentatricopeptide repeat-containing protein
FT At1g15510, chloroplastic"
FT /id="PRO_0000342786"
FT REPEAT 58..92
FT /note="PPR 1"
FT REPEAT 93..123
FT /note="PPR 2"
FT REPEAT 128..158
FT /note="PPR 3"
FT REPEAT 159..194
FT /note="PPR 4"
FT REPEAT 195..229
FT /note="PPR 5"
FT REPEAT 230..260
FT /note="PPR 6"
FT REPEAT 261..295
FT /note="PPR 7"
FT REPEAT 296..330
FT /note="PPR 8"
FT REPEAT 331..365
FT /note="PPR 9"
FT REPEAT 366..396
FT /note="PPR 10"
FT REPEAT 397..431
FT /note="PPR 11"
FT REPEAT 432..466
FT /note="PPR 12"
FT REPEAT 467..493
FT /note="PPR 13"
FT REPEAT 497..531
FT /note="PPR 14"
FT REPEAT 532..561
FT /note="PPR 15"
FT REPEAT 562..596
FT /note="PPR 16"
FT REPEAT 597..631
FT /note="PPR 17"
FT REPEAT 632..662
FT /note="PPR 18"
FT REGION 667..742
FT /note="Type E motif"
FT REGION 743..773
FT /note="Type E(+) motif"
FT REGION 774..866
FT /note="Type DYW motif"
FT MUTAGEN 500
FT /note="T->I: In ecb2-2; delayed chloroplast development and
FT plant greening."
FT /evidence="ECO:0000269|PubMed:21294841"
SQ SEQUENCE 866 AA; 97697 MW; 41238CF8CB57F5D6 CRC64;
MASSAQSPHF YLNPGKSNSF QSKAYKQRNV NFYWNFGIRR LFLRKSQGLS VLSSSSSSTH
FSNSQLHGLC ANGKLEEAMK LLNSMQELRV AVDEDVFVAL VRLCEWKRAQ EEGSKVYSIA
LSSMSSLGVE LGNAFLAMFV RFGNLVDAWY VFGKMSERNL FSWNVLVGGY AKQGYFDEAM
CLYHRMLWVG GVKPDVYTFP CVLRTCGGIP DLARGKEVHV HVVRYGYELD IDVVNALITM
YVKCGDVKSA RLLFDRMPRR DIISWNAMIS GYFENGMCHE GLELFFAMRG LSVDPDLMTL
TSVISACELL GDRRLGRDIH AYVITTGFAV DISVCNSLTQ MYLNAGSWRE AEKLFSRMER
KDIVSWTTMI SGYEYNFLPD KAIDTYRMMD QDSVKPDEIT VAAVLSACAT LGDLDTGVEL
HKLAIKARLI SYVIVANNLI NMYSKCKCID KALDIFHNIP RKNVISWTSI IAGLRLNNRC
FEALIFLRQM KMTLQPNAIT LTAALAACAR IGALMCGKEI HAHVLRTGVG LDDFLPNALL
DMYVRCGRMN TAWSQFNSQK KDVTSWNILL TGYSERGQGS MVVELFDRMV KSRVRPDEIT
FISLLCGCSK SQMVRQGLMY FSKMEDYGVT PNLKHYACVV DLLGRAGELQ EAHKFIQKMP
VTPDPAVWGA LLNACRIHHK IDLGELSAQH IFELDKKSVG YYILLCNLYA DCGKWREVAK
VRRMMKENGL TVDAGCSWVE VKGKVHAFLS DDKYHPQTKE INTVLEGFYE KMSEVGLTKI
SESSSMDETE ISRDEIFCGH SERKAIAFGL INTVPGMPIW VTKNLSMCEN CHDTVKFISK
TVRREISVRD AEHFHHFKDG ECSCGD
