MORF8_ARATH
ID MORF8_ARATH Reviewed; 395 AA.
AC Q9LKA5; Q5XEU8;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Multiple organellar RNA editing factor 8, chloroplastic/mitochondrial {ECO:0000305};
DE AltName: Full=RNA editing-interacting protein 1 {ECO:0000303|PubMed:22566615};
DE Flags: Precursor;
GN Name=MORF8 {ECO:0000303|PubMed:22411807};
GN Synonyms=RIP1 {ECO:0000303|PubMed:22566615}; OrderedLocusNames=At3g15000;
GN ORFNames=K15M2.14;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2] {ECO:0000305}
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP PROTEIN SEQUENCE OF 169-179, AND SUBCELLULAR LOCATION.
RC TISSUE=Leaf, and Stem;
RX PubMed=11743114; DOI=10.1104/pp.010474;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22411807; DOI=10.1073/pnas.1202452109;
RA Takenaka M., Zehrmann A., Verbitskiy D., Kugelmann M., Hartel B.,
RA Brennicke A.;
RT "Multiple organellar RNA editing factor (MORF) family proteins are required
RT for RNA editing in mitochondria and plastids of plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5104-5109(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22566615; DOI=10.1073/pnas.1121465109;
RA Bentolila S., Heller W.P., Sun T., Babina A.M., Friso G., van Wijk K.J.,
RA Hanson M.R.;
RT "RIP1, a member of an Arabidopsis protein family, interacts with the
RT protein RARE1 and broadly affects RNA editing.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E1453-E1461(2012).
RN [10]
RP INTERACTION WITH PCMP-H52/MEF10.
RX PubMed=23288601; DOI=10.1007/s11103-012-0003-2;
RA Haertel B., Zehrmann A., Verbitskiy D., van der Merwe J.A., Brennicke A.,
RA Takenaka M.;
RT "MEF10 is required for RNA editing at nad2-842 in mitochondria of
RT Arabidopsis thaliana and interacts with MORF8.";
RL Plant Mol. Biol. 81:337-346(2013).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23818871; DOI=10.1371/journal.pgen.1003584;
RA Bentolila S., Oh J., Hanson M.R., Bukowski R.;
RT "Comprehensive high-resolution analysis of the role of an Arabidopsis gene
RT family in RNA editing.";
RL PLoS Genet. 9:E1003584-E1003584(2013).
RN [12]
RP INTERACTION WITH PPOX1.
RX PubMed=24497494; DOI=10.1073/pnas.1316183111;
RA Zhang F., Tang W., Hedtke B., Zhong L., Liu L., Peng L., Lu C., Grimm B.,
RA Lin R.;
RT "Tetrapyrrole biosynthetic enzyme protoporphyrinogen IX oxidase 1 is
RT required for plastid RNA editing.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2023-2028(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, HOMODIMERIZATION, INTERACTION WITH
RP MORF1/RIP8; MORF2/RIP2; MORF3/RIP3; MORF4/RIP4; MORF5/RIP5; MORF6/RIP6 AND
RP MORF7/RIP7, AND SUBCELLULAR LOCATION.
RX PubMed=25583991; DOI=10.1074/jbc.m114.602086;
RA Zehrmann A., Haertel B., Glass F., Bayer-Csaszar E., Obata T., Meyer E.,
RA Brennicke A., Takenaka M.;
RT "Selective homo- and heteromer interactions between the multiple organellar
RT RNA editing factor (MORF) proteins in Arabidopsis thaliana.";
RL J. Biol. Chem. 290:6445-6456(2015).
RN [14]
RP INTERACTION WITH RBG3/ORRM3.
RX PubMed=25800738; DOI=10.1093/nar/gkv245;
RA Shi X., Hanson M.R., Bentolila S.;
RT "Two RNA recognition motif-containing proteins are plant mitochondrial
RT editing factors.";
RL Nucleic Acids Res. 43:3814-3825(2015).
RN [15]
RP INTERACTION WITH PCMP-A2/PMD1.
RX PubMed=26123918; DOI=10.1007/s11120-015-0171-4;
RA Zhang H.D., Cui Y.L., Huang C., Yin Q.Q., Qin X.M., Xu T., He X.F.,
RA Zhang Y., Li Z.R., Yang Z.N.;
RT "PPR protein PDM1/SEL1 is involved in RNA editing and splicing of plastid
RT genes in Arabidopsis thaliana.";
RL Photosyn. Res. 126:311-321(2015).
RN [16]
RP INTERACTION WITH ORRM1 AND VAT3/OZ1.
RX PubMed=25768119; DOI=10.1371/journal.pgen.1005028;
RA Sun T., Shi X., Friso G., Van Wijk K., Bentolila S., Hanson M.R.;
RT "A zinc finger motif-containing protein is essential for chloroplast RNA
RT editing.";
RL PLoS Genet. 11:E1005028-E1005028(2015).
RN [17]
RP INTERACTION WITH PCMP-H13/MEF35.
RX PubMed=26470017; DOI=10.1371/journal.pone.0140680;
RA Brehme N., Bayer-Csaszar E., Glass F., Takenaka M.;
RT "The DYW subgroup PPR protein MEF35 targets RNA editing sites in the
RT mitochondrial rpl16, nad4 and cob mRNAs in Arabidopsis thaliana.";
RL PLoS ONE 10:E0140680-E0140680(2015).
RN [18]
RP INTERACTION WITH RBG5/ORRM4, AND SUBCELLULAR LOCATION.
RX PubMed=26578708; DOI=10.1104/pp.15.01280;
RA Shi X., Germain A., Hanson M.R., Bentolila S.;
RT "RNA recognition motif-containing protein ORRM4 broadly affects
RT mitochondrial RNA editing and impacts plant development and flowering.";
RL Plant Physiol. 170:294-309(2016).
RN [19]
RP INTERACTION WITH ORRM6, AND SUBCELLULAR LOCATION.
RX PubMed=28213559; DOI=10.1104/pp.16.01623;
RA Hackett J.B., Shi X., Kobylarz A.T., Lucas M.K., Wessendorf R.L.,
RA Hines K.M., Bentolila S., Hanson M.R., Lu Y.;
RT "An organelle RNA recognition motif protein is required for photosynthetic
RT subunit psbF transcript editing.";
RL Plant Physiol. 173:2278-2293(2017).
CC -!- FUNCTION: Involved in organellar RNA editing. Required for the
CC processing of numerous RNA editing sites in mitochondria and plastids
CC (PubMed:22566615, PubMed:23818871). Binds to the plastid RARE1 factor,
CC a pentatricopeptide repeat-containing protein involved in RNA editing
CC (PubMed:22566615). {ECO:0000269|PubMed:22566615,
CC ECO:0000269|PubMed:23818871}.
CC -!- SUBUNIT: Interacts with protoporphyrinogen oxidase 1 PPOX1
CC (PubMed:24497494). Interacts with PCMP-H52/MEF10 (PubMed:23288601).
CC Homodimer and heterodimers with MORF1/RIP8, MORF2/RIP2, MORF3/RIP3,
CC MORF4/RIP4, MORF5/RIP5, MORF6/RIP6 and MORF7/RIP7 (PubMed:25583991).
CC Interacts with RBG3/ORRM3 (PubMed:25800738). Interacts with PCMP-
CC A2/PMD1 (PubMed:26123918). Interacts with ORRM1 and VAT3/OZ1
CC (PubMed:25768119). Interacts with PCMP-H13/MEF35 (PubMed:26470017).
CC Interacts with RBG5/ORRM4 (PubMed:26578708). Interacts with ORRM6
CC (PubMed:28213559). {ECO:0000269|PubMed:23288601,
CC ECO:0000269|PubMed:24497494, ECO:0000269|PubMed:25583991,
CC ECO:0000269|PubMed:25768119, ECO:0000269|PubMed:25800738,
CC ECO:0000269|PubMed:26123918, ECO:0000269|PubMed:26470017,
CC ECO:0000269|PubMed:26578708, ECO:0000269|PubMed:28213559}.
CC -!- INTERACTION:
CC Q9LKA5; Q9LFT8: CDKC-1; NbExp=2; IntAct=EBI-2025869, EBI-2025736;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11743114,
CC ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:22566615,
CC ECO:0000269|PubMed:25583991, ECO:0000269|PubMed:26578708}. Plastid,
CC chloroplast {ECO:0000269|PubMed:22566615, ECO:0000269|PubMed:25583991,
CC ECO:0000269|PubMed:28213559}. Note=Dual targeting to mitochondria and
CC chloroplasts. {ECO:0000269|PubMed:22566615,
CC ECO:0000269|PubMed:25583991}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants. {ECO:0000269|PubMed:22566615,
CC ECO:0000269|PubMed:23818871}.
CC -!- SIMILARITY: Belongs to the MORF family.
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DR EMBL; AP000370; BAA97063.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75601.1; -; Genomic_DNA.
DR EMBL; AF428427; AAL16196.1; -; mRNA.
DR EMBL; BT015868; AAU94431.1; -; mRNA.
DR EMBL; AK226420; BAE98564.1; -; mRNA.
DR RefSeq; NP_566496.1; NM_112362.4.
DR AlphaFoldDB; Q9LKA5; -.
DR SMR; Q9LKA5; -.
DR BioGRID; 6063; 16.
DR IntAct; Q9LKA5; 5.
DR STRING; 3702.AT3G15000.1; -.
DR MetOSite; Q9LKA5; -.
DR SwissPalm; Q9LKA5; -.
DR PaxDb; Q9LKA5; -.
DR PRIDE; Q9LKA5; -.
DR ProteomicsDB; 250938; -.
DR EnsemblPlants; AT3G15000.1; AT3G15000.1; AT3G15000.
DR GeneID; 820729; -.
DR Gramene; AT3G15000.1; AT3G15000.1; AT3G15000.
DR KEGG; ath:AT3G15000; -.
DR Araport; AT3G15000; -.
DR TAIR; locus:2086310; AT3G15000.
DR eggNOG; ENOG502QS63; Eukaryota.
DR HOGENOM; CLU_046201_0_0_1; -.
DR InParanoid; Q9LKA5; -.
DR OMA; GYAPPNN; -.
DR OrthoDB; 1318902at2759; -.
DR PhylomeDB; Q9LKA5; -.
DR PRO; PR:Q9LKA5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LKA5; baseline and differential.
DR Genevisible; Q9LKA5; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0046983; F:protein dimerization activity; IPI:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:TAIR.
DR GO; GO:0016554; P:cytidine to uridine editing; IMP:TAIR.
DR GO; GO:0080156; P:mitochondrial mRNA modification; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0009451; P:RNA modification; IMP:TAIR.
DR InterPro; IPR039206; MORF/ORRM1/DAG-like.
DR PANTHER; PTHR31346; PTHR31346; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Direct protein sequencing; Mitochondrion; mRNA processing;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast and mitochondrion"
FT CHAIN 57..395
FT /note="Multiple organellar RNA editing factor 8,
FT chloroplastic/mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000220586"
FT REGION 211..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 42870 MW; D15E5CCC89E2A33C CRC64;
MATHTISRSI LCRPAKSLSF LFTRSFASSA PLAKSPASSL LSRSRPLVAA FSSVFRGGLV
SVKGLSTQAT SSSLNDPNPN WSNRPPKETI LLDGCDFEHW LVVVEPPQGE PTRDEIIDSY
IKTLAQIVGS EDEARMKIYS VSTRCYYAFG ALVSEDLSHK LKELSNVRWV LPDSYLDVRN
KDYGGEPFID GKAVPYDPKY HEEWIRNNAR ANERNRRNDR PRNNDRSRNF ERRRENMAGG
PPPQRPPMGG PPPPPHIGGS APPPPHMGGS APPPPHMGQN YGPPPPNNMG GPRHPPPYGA
PPQNNMGGPR PPQNYGGTPP PNYGGAPPAN NMGGAPPPNY GGGPPPQYGA VPPPQYGGAP
PQNNNYQQQG SGMQQPQYQN NYPPNRDGSG NPYQG
