PP438_ARATH
ID PP438_ARATH Reviewed; 521 AA.
AC Q9FME4; Q8LCR2;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Pentatricopeptide repeat-containing protein PNM1, mitochondrial;
DE AltName: Full=PPR PROTEIN LOCALIZED TO THE NUCLEUS AND MITOCHONDRIA 1;
DE Flags: Precursor;
GN Name=PNM1; OrderedLocusNames=At5g60960; ORFNames=MSL3.8;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 SUBCELLULAR LOCATION, INTERACTION WITH NAP1;1 AND TCP8, DISRUPTION
RP PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND RNA-BINDING.
RX PubMed=21297037; DOI=10.1105/tpc.110.081638;
RA Hammani K., Gobert A., Hleibieh K., Choulier L., Small I., Giege P.;
RT "An Arabidopsis dual-localized pentatricopeptide repeat protein interacts
RT with nuclear proteins involved in gene expression regulation.";
RL Plant Cell 23:730-740(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-59.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
CC -!- FUNCTION: RNA-binding protein that functions in both mitochondrion and
CC nucleus. In mitochondrion, it is associated with polysomes and may play
CC a role in translation. Required during embryogenesis. In nucleus, might
CC be involved in the regulation of its own gene expression.
CC {ECO:0000269|PubMed:21297037}.
CC -!- SUBUNIT: Interacts with NAP1;1 and TCP8. Able to bind mitochondrial RNA
CC in vitro. {ECO:0000269|PubMed:21297037}.
CC -!- INTERACTION:
CC Q9FME4; Q9SZI2: NAP1;1; NbExp=4; IntAct=EBI-6913662, EBI-4424361;
CC Q9FME4; Q9C518: TCP8; NbExp=4; IntAct=EBI-6913662, EBI-3134124;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:21297037, ECO:0000305|PubMed:25732537}. Nucleus
CC {ECO:0000269|PubMed:21297037}. Note=Can localize to both mitochondrion
CC and nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, lateral root primordia and
CC leaf primordia. Highly detected in the mature pollen grains.
CC {ECO:0000269|PubMed:21297037}.
CC -!- DISRUPTION PHENOTYPE: Embryo-lethal at a early stage of development.
CC {ECO:0000269|PubMed:21297037}.
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Pentatricopeptide repeat proteins;
CC URL="https://ppr.plantenergy.uwa.edu.au";
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DR EMBL; AB008269; BAB10645.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97403.1; -; Genomic_DNA.
DR EMBL; AY086450; AAM63453.1; -; mRNA.
DR RefSeq; NP_200904.1; NM_125489.3.
DR PDB; 6XYW; EM; 3.86 A; AQ=1-521.
DR PDBsum; 6XYW; -.
DR AlphaFoldDB; Q9FME4; -.
DR SMR; Q9FME4; -.
DR BioGRID; 21461; 5.
DR IntAct; Q9FME4; 5.
DR STRING; 3702.AT5G60960.1; -.
DR iPTMnet; Q9FME4; -.
DR PaxDb; Q9FME4; -.
DR PRIDE; Q9FME4; -.
DR ProteomicsDB; 249319; -.
DR EnsemblPlants; AT5G60960.1; AT5G60960.1; AT5G60960.
DR GeneID; 836217; -.
DR Gramene; AT5G60960.1; AT5G60960.1; AT5G60960.
DR KEGG; ath:AT5G60960; -.
DR Araport; AT5G60960; -.
DR TAIR; locus:2173552; AT5G60960.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_041224_0_0_1; -.
DR InParanoid; Q9FME4; -.
DR OMA; CICRLCR; -.
DR OrthoDB; 1344243at2759; -.
DR PhylomeDB; Q9FME4; -.
DR PRO; PR:Q9FME4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FME4; baseline and differential.
DR Genevisible; Q9FME4; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IDA:TAIR.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
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 TIGRFAMs; TIGR00756; PPR; 2.
DR PROSITE; PS51375; PPR; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Nucleus; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation; Transit peptide;
KW Translation regulation.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 60..521
FT /note="Pentatricopeptide repeat-containing protein PNM1,
FT mitochondrial"
FT /id="PRO_0000363575"
FT REPEAT 174..204
FT /note="PPR 1"
FT REPEAT 210..240
FT /note="PPR 2"
FT REPEAT 244..278
FT /note="PPR 3"
FT REPEAT 279..313
FT /note="PPR 4"
FT REPEAT 321..355
FT /note="PPR 5"
FT REPEAT 356..390
FT /note="PPR 6"
FT REPEAT 393..427
FT /note="PPR 7"
FT REPEAT 428..462
FT /note="PPR 8"
FT REGION 480..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 486..503
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 480..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 164
FT /note="E -> G (in Ref. 3; AAM63453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 521 AA; 59143 MW; 53CEED0D7D208E2D CRC64;
MPPSLPSLQL RRLLLRSFIS SSSVNTLQSQ PRIISSKPLF SPLPPSRSSI FSTFPSRFFS
SETNAESESL DSNEIALSFS KELTGNPDAE SQTISQRFNL SFSHITPNPD LILQTLNLSP
EAGRAALGFN EWLDSNSNFS HTDETVSFFV DYFGRRKDFK GMLEIISKYK GIAGGKTLES
AIDRLVRAGR PKQVTDFFEK MENDYGLKRD KESLTLVVKK LCEKGHASIA EKMVKNTANE
IFPDENICDL LISGWCIAEK LDEATRLAGE MSRGGFEIGT KAYNMMLDCV CKLCRKKDPF
KLQPEVEKVL LEMEFRGVPR NTETFNVLIN NLCKIRRTEE AMTLFGRMGE WGCQPDAETY
LVLIRSLYQA ARIGEGDEMI DKMKSAGYGE LLNKKEYYGF LKILCGIERL EHAMSVFKSM
KANGCKPGIK TYDLLMGKMC ANNQLTRANG LYKEAAKKGI AVSPKEYRVD PRFMKKKTKE
VDSNVKKRET LPEKTARKKK RLKQINMSFV KKPHNKMRRR M
