PP202_ARATH
ID PP202_ARATH Reviewed; 613 AA.
AC O22137;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Pentatricopeptide repeat-containing protein At2g45350, chloroplastic;
DE AltName: Full=Protein CHLORORESPIRATORY REDUCTION 4;
DE Flags: Precursor;
GN Name=CRR4; Synonyms=PCMP-E11; OrderedLocusNames=At2g45350;
GN ORFNames=F4L23.14;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 GENE FAMILY.
RX PubMed=10809006; DOI=10.1023/a:1006352315928;
RA Aubourg S., Boudet N., Kreis M., Lecharny A.;
RT "In Arabidopsis thaliana, 1% of the genome codes for a novel protein family
RT unique to plants.";
RL Plant Mol. Biol. 42:603-613(2000).
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.
RX PubMed=15662426; DOI=10.1038/nature03229;
RA Kotera E., Tasaka M., Shikanai T.;
RT "A pentatricopeptide repeat protein is essential for RNA editing in
RT chloroplasts.";
RL Nature 433:326-330(2005).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17015439; DOI=10.1074/jbc.m608184200;
RA Okuda K., Nakamura T., Sugita M., Shimizu T., Shikanai T.;
RT "A pentatricopeptide repeat protein is a site recognition factor in
RT chloroplast RNA editing.";
RL J. Biol. Chem. 281:37661-37667(2006).
RN [7]
RP FUNCTION, INTERACTION WITH DYW1, AND SUBCELLULAR LOCATION.
RX PubMed=23001034; DOI=10.1105/tpc.112.099507;
RA Boussardon C., Salone V., Avon A., Berthome R., Hammani K., Okuda K.,
RA Shikanai T., Small I., Lurin C.;
RT "Two interacting proteins are necessary for the editing of the NdhD-1 site
RT in Arabidopsis plastids.";
RL Plant Cell 24:3684-3694(2012).
CC -!- FUNCTION: Plays a major role in chloroplast RNA editing. Acts as a
CC site-recognition transacting factor to recruit C-deaminase
CC (PubMed:15662426, PubMed:17015439). Involved in single RNA editing
CC events. Required for the edition of the site 1 of ndhD (ndhD-1 site
CC corresponding to cytidine-2), which is a plastid-encoded subunit of the
CC NADH-plastoquinone oxidoreductase. The interaction with DYW1 is
CC required for its function in editing the ndhD-1 site (PubMed:23001034).
CC {ECO:0000269|PubMed:15662426, ECO:0000269|PubMed:17015439,
CC ECO:0000269|PubMed:23001034}.
CC -!- SUBUNIT: Interacts with DYW1. {ECO:0000269|PubMed:23001034}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:17015439, ECO:0000269|PubMed:23001034}.
CC -!- MISCELLANEOUS: Unlike other RNA editing factors, CCR4 does not contain
CC identifiable E(+) and DYW motifs but does contain PPR repeats.
CC Therefore its association with DYW1, which lacks PPR repeats, but does
CC contain E(+) and DYW motifs, is required for its function in RNA
CC editing. {ECO:0000305|PubMed:23001034}.
CC -!- SIMILARITY: Belongs to the PPR family. PCMP-E subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB82628.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Pentatricopeptide repeat proteins;
CC URL="https://ppr.plantenergy.uwa.edu.au";
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DR EMBL; AC002387; AAB82628.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC10542.1; -; Genomic_DNA.
DR PIR; E84889; E84889.
DR RefSeq; NP_182060.2; NM_130098.3.
DR AlphaFoldDB; O22137; -.
DR SMR; O22137; -.
DR BioGRID; 4479; 1.
DR STRING; 3702.AT2G45350.1; -.
DR PaxDb; O22137; -.
DR PRIDE; O22137; -.
DR EnsemblPlants; AT2G45350.1; AT2G45350.1; AT2G45350.
DR GeneID; 819143; -.
DR Gramene; AT2G45350.1; AT2G45350.1; AT2G45350.
DR KEGG; ath:AT2G45350; -.
DR Araport; AT2G45350; -.
DR TAIR; locus:2050857; AT2G45350.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_002706_37_2_1; -.
DR InParanoid; O22137; -.
DR OMA; SVDHWNA; -.
DR OrthoDB; 1344243at2759; -.
DR PhylomeDB; O22137; -.
DR PRO; PR:O22137; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22137; baseline and differential.
DR Genevisible; O22137; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:1900865; P:chloroplast RNA modification; IMP:UniProtKB.
DR GO; GO:0016556; P:mRNA modification; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF01535; PPR; 9.
DR Pfam; PF13041; PPR_2; 1.
DR TIGRFAMs; TIGR00756; PPR; 5.
DR PROSITE; PS51375; PPR; 14.
PE 1: Evidence at protein level;
KW Chloroplast; mRNA processing; Plastid; Reference proteome; Repeat;
KW RNA-binding; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..613
FT /note="Pentatricopeptide repeat-containing protein
FT At2g45350, chloroplastic"
FT /id="PRO_0000356061"
FT REPEAT 85..119
FT /note="PPR 1"
FT REPEAT 120..154
FT /note="PPR 2"
FT REPEAT 155..185
FT /note="PPR 3"
FT REPEAT 186..216
FT /note="PPR 4"
FT REPEAT 219..250
FT /note="PPR 5"
FT REPEAT 251..285
FT /note="PPR 6"
FT REPEAT 286..312
FT /note="PPR 7"
FT REPEAT 313..347
FT /note="PPR 8"
FT REPEAT 349..383
FT /note="PPR 9"
FT REPEAT 384..414
FT /note="PPR 10"
FT REPEAT 415..449
FT /note="PPR 11"
FT REPEAT 450..480
FT /note="PPR 12"
FT REPEAT 486..516
FT /note="PPR 13"
FT REGION 521..596
FT /note="Type E motif"
SQ SEQUENCE 613 AA; 69186 MW; E0A51EDB553E6DA6 CRC64;
MLVFKSTMEC SISSTIHVLG SCKTSDDVNQ IHGRLIKTGI IKNSNLTTRI VLAFASSRRP
YLADFARCVF HEYHVCSFSF GEVEDPFLWN AVIKSHSHGK DPRQALLLLC LMLENGVSVD
KFSLSLVLKA CSRLGFVKGG MQIHGFLKKT GLWSDLFLQN CLIGLYLKCG CLGLSRQMFD
RMPKRDSVSY NSMIDGYVKC GLIVSARELF DLMPMEMKNL ISWNSMISGY AQTSDGVDIA
SKLFADMPEK DLISWNSMID GYVKHGRIED AKGLFDVMPR RDVVTWATMI DGYAKLGFVH
HAKTLFDQMP HRDVVAYNSM MAGYVQNKYH MEALEIFSDM EKESHLLPDD TTLVIVLPAI
AQLGRLSKAI DMHLYIVEKQ FYLGGKLGVA LIDMYSKCGS IQHAMLVFEG IENKSIDHWN
AMIGGLAIHG LGESAFDMLL QIERLSLKPD DITFVGVLNA CSHSGLVKEG LLCFELMRRK
HKIEPRLQHY GCMVDILSRS GSIELAKNLI EEMPVEPNDV IWRTFLTACS HHKEFETGEL
VAKHLILQAG YNPSSYVLLS NMYASFGMWK DVRRVRTMMK ERKIEKIPGC SWIELDGRVH
EFFVDSIEVS STL
