MORF1_ARATH
ID MORF1_ARATH Reviewed; 419 AA.
AC O49429; F4JU25;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Multiple organellar RNA editing factor 1, mitochondrial {ECO:0000305};
DE AltName: Full=RNA editing-interacting protein 8 {ECO:0000303|PubMed:23818871};
DE Flags: Precursor;
GN Name=MORF1 {ECO:0000303|PubMed:22411807};
GN Synonyms=RIP8 {ECO:0000303|PubMed:23818871};
GN OrderedLocusNames=At4g20020 {ECO:0000312|Araport:AT4G20020};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP FUNCTION, INTERACTION WITH MORF3, GENE FAMILY, NOMENCLATURE, AND DISRUPTION
RP PHENOTYPE.
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 [6]
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 [7]
RP HOMODIMERIZATION, INTERACTION WITH MORF8/RIP1; MORF3/RIP3; MORF4/RIP4 AND
RP MORF6/RIP6, 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 [8]
RP INTERACTION WITH PCMP-E90/MEF13.
RX PubMed=26048647; DOI=10.1016/j.molp.2015.05.008;
RA Glass F., Haertel B., Zehrmann A., Verbitskiy D., Takenaka M.;
RT "MEF13 requires MORF3 and MORF8 for RNA editing at eight targets in
RT mitochondrial mRNAs in Arabidopsis thaliana.";
RL Mol. Plant 8:1466-1477(2015).
RN [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 79-190.
RX PubMed=28201607; DOI=10.1093/nar/gkx099;
RA Haag S., Schindler M., Berndt L., Brennicke A., Takenaka M., Weber G.;
RT "Crystal structures of the Arabidopsis thaliana organellar RNA editing
RT factors MORF1 and MORF9.";
RL Nucleic Acids Res. 45:4915-4928(2017).
CC -!- FUNCTION: Involved in organellar RNA editing. Required for the
CC processing of numerous RNA editing sites in mitochondria
CC (PubMed:22411807, PubMed:23818871). Binds to the mitochondrial MEF19
CC and MEF21 factors, two pentatricopeptide repeat-containing proteins
CC involved in RNA editing (PubMed:22411807).
CC {ECO:0000269|PubMed:22411807, ECO:0000269|PubMed:23818871}.
CC -!- SUBUNIT: Homodimer and heterodimer with MORF3 (PubMed:22411807,
CC PubMed:25583991). Heterodimers with MORF8/RIP1, MORF4/RIP4 and
CC MORF6/RIP6 (PubMed:25583991). Interacts with PCMP-E90/MEF13
CC (PubMed:26048647). Interacts with PCMP-H13/MEF35 (PubMed:26470017).
CC {ECO:0000269|PubMed:22411807, ECO:0000269|PubMed:25583991,
CC ECO:0000269|PubMed:26048647, ECO:0000269|PubMed:26470017}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25583991}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O49429-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O49429-2; Sequence=VSP_057525, VSP_057526;
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when homozygous.
CC {ECO:0000269|PubMed:22411807, ECO:0000269|PubMed:23818871}.
CC -!- SIMILARITY: Belongs to the MORF family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX826898; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AL021637; CAA16610.1; -; Genomic_DNA.
DR EMBL; AL161552; CAB79002.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84262.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84263.1; -; Genomic_DNA.
DR EMBL; BT002761; AAO22589.1; -; mRNA.
DR EMBL; BX826898; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T04886; T04886.
DR RefSeq; NP_193735.1; NM_118121.4. [O49429-1]
DR RefSeq; NP_974579.1; NM_202850.3. [O49429-2]
DR PDB; 5MPW; X-ray; 1.50 A; A/B/C/D=79-190.
DR PDB; 5MPX; X-ray; 1.94 A; A/B/C/D=79-190.
DR PDBsum; 5MPW; -.
DR PDBsum; 5MPX; -.
DR AlphaFoldDB; O49429; -.
DR SMR; O49429; -.
DR STRING; 3702.AT4G20020.1; -.
DR SwissPalm; O49429; -.
DR PaxDb; O49429; -.
DR PRIDE; O49429; -.
DR ProteomicsDB; 238303; -. [O49429-1]
DR EnsemblPlants; AT4G20020.1; AT4G20020.1; AT4G20020. [O49429-1]
DR EnsemblPlants; AT4G20020.2; AT4G20020.2; AT4G20020. [O49429-2]
DR GeneID; 827747; -.
DR Gramene; AT4G20020.1; AT4G20020.1; AT4G20020. [O49429-1]
DR Gramene; AT4G20020.2; AT4G20020.2; AT4G20020. [O49429-2]
DR KEGG; ath:AT4G20020; -.
DR Araport; AT4G20020; -.
DR TAIR; locus:2119782; AT4G20020.
DR eggNOG; ENOG502QUVM; Eukaryota.
DR InParanoid; O49429; -.
DR OMA; QNYGPPR; -.
DR OrthoDB; 1266828at2759; -.
DR PhylomeDB; O49429; -.
DR PRO; PR:O49429; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49429; baseline and differential.
DR Genevisible; O49429; AT.
DR GO; GO:0009507; C:chloroplast; IEA:GOC.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0046983; F:protein dimerization activity; IPI:TAIR.
DR GO; GO:1900865; P:chloroplast RNA modification; IMP:TAIR.
DR GO; GO:0016554; P:cytidine to uridine editing; IEA:InterPro.
DR GO; GO:0080156; P:mitochondrial mRNA modification; IBA:GO_Central.
DR GO; GO:1900864; P:mitochondrial RNA modification; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.80; -; 1.
DR InterPro; IPR039206; MORF/ORRM1/DAG-like.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR31346; PTHR31346; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Mitochondrion; mRNA processing;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..60
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 61..419
FT /note="Multiple organellar RNA editing factor 1,
FT mitochondrial"
FT /id="PRO_0000432524"
FT REGION 174..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 400..406
FT /note="VRSRSIM -> FPQGRRY (in isoform 2)"
FT /id="VSP_057525"
FT VAR_SEQ 407..419
FT /note="Missing (in isoform 2)"
FT /id="VSP_057526"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:5MPW"
FT HELIX 105..120
FT /evidence="ECO:0007829|PDB:5MPW"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:5MPW"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:5MPW"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:5MPW"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:5MPW"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:5MPW"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:5MPW"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:5MPW"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:5MPW"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:5MPW"
SQ SEQUENCE 419 AA; 45157 MW; 2C1204736AED291A CRC64;
MAMISHRLRR ALLTATSYVN RSISSSITPA SDFPSVSAAV LKRSVIGRST EVATRAPARL
FSTRQYKLYK EGDEITEDTV LFEGCDYNHW LITMDFSKEE TPKSPEEMVA AYEETCAQGL
GISVEEAKQR MYACSTTTYQ GFQAIMTEQE SEKFKDLPGV VFILPDSYID PQNKEYGGDK
YENGVITHRP PPIQSGRARP RPRFDRSGGG SGGPQNFQRN TQYGQQPPMQ GGGGSYGPQQ
GYATPGQGQG TQAPPPFQGG YNQGPRSPPP PYQAGYNQGQ GSPVPPYQAG YNQVQGSPVP
PYQGTQSSYG QGGSGNYSQG PQGGYNQGGP RNYNPQGAGN FGPASGAGNL GPAPGAGNPG
YGQGYSGPGQ EQNQTFPQAD QRNRDWNNNN PAGQPGSDQV RSRSIMNLAS FFFDILIRH
