MORF3_ARATH
ID MORF3_ARATH Reviewed; 244 AA.
AC Q84JZ6; Q9M7Y5;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Multiple organellar RNA editing factor 3, mitochondrial {ECO:0000305};
DE AltName: Full=RNA editing-interacting protein 3 {ECO:0000303|PubMed:23818871};
DE Flags: Precursor;
GN Name=MORF3 {ECO:0000303|PubMed:22411807};
GN Synonyms=RIP3 {ECO:0000303|PubMed:23818871};
GN OrderedLocusNames=At3g06790 {ECO:0000312|Araport:AT3G06790};
GN ORFNames=F3E22.7 {ECO:0000312|EMBL:AAF63819.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 FUNCTION, INTERACTION WITH MORF1, 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 [5]
RP FUNCTION, GENE FAMILY, 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 [6]
RP HOMODIMERIZATION, INTERACTION WITH MORF8/RIP1; MORF1/RIP8; MORF4/RIP4 AND
RP MORF5/RIP5, 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).
CC -!- FUNCTION: Involved in organellar RNA editing. Required for the
CC processing of RNA editing sites in mitochondria.
CC {ECO:0000269|PubMed:22411807, ECO:0000269|PubMed:23818871}.
CC -!- SUBUNIT: Heterodimer with MORF1 (PubMed:22411807, PubMed:25583991).
CC Homodimer and heterodimers with MORF8/RIP1, MORF4/RIP4 and MORF5/RIP5
CC (PubMed:25583991). {ECO:0000269|PubMed:22411807,
CC ECO:0000269|PubMed:25583991}.
CC -!- INTERACTION:
CC Q84JZ6; Q9ATB4: ADA2B; NbExp=3; IntAct=EBI-4465639, EBI-979237;
CC Q84JZ6; Q9FDW1: MYB44; NbExp=3; IntAct=EBI-4465639, EBI-15192813;
CC Q84JZ6; Q9LF53: RGL3; NbExp=3; IntAct=EBI-4465639, EBI-15681313;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25583991}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84JZ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84JZ6-2; Sequence=VSP_057527;
CC -!- DISRUPTION PHENOTYPE: Retarded growth. {ECO:0000269|PubMed:22411807,
CC ECO:0000269|PubMed:23818871}.
CC -!- SIMILARITY: Belongs to the MORF family.
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DR EMBL; AC023912; AAF63819.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74459.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74460.1; -; Genomic_DNA.
DR EMBL; BT002982; AAO22791.1; -; mRNA.
DR EMBL; BT004451; AAO42445.1; -; mRNA.
DR RefSeq; NP_187335.1; NM_111559.3. [Q84JZ6-2]
DR RefSeq; NP_974243.1; NM_202514.3. [Q84JZ6-1]
DR AlphaFoldDB; Q84JZ6; -.
DR SMR; Q84JZ6; -.
DR IntAct; Q84JZ6; 6.
DR STRING; 3702.AT3G06790.1; -.
DR iPTMnet; Q84JZ6; -.
DR PaxDb; Q84JZ6; -.
DR PRIDE; Q84JZ6; -.
DR ProteomicsDB; 238304; -. [Q84JZ6-1]
DR EnsemblPlants; AT3G06790.1; AT3G06790.1; AT3G06790. [Q84JZ6-2]
DR EnsemblPlants; AT3G06790.2; AT3G06790.2; AT3G06790. [Q84JZ6-1]
DR GeneID; 819864; -.
DR Gramene; AT3G06790.1; AT3G06790.1; AT3G06790. [Q84JZ6-2]
DR Gramene; AT3G06790.2; AT3G06790.2; AT3G06790. [Q84JZ6-1]
DR KEGG; ath:AT3G06790; -.
DR Araport; AT3G06790; -.
DR TAIR; locus:2083348; AT3G06790.
DR eggNOG; ENOG502QSEB; Eukaryota.
DR HOGENOM; CLU_073703_2_0_1; -.
DR InParanoid; Q84JZ6; -.
DR OMA; DMINAYV; -.
DR PhylomeDB; Q84JZ6; -.
DR PRO; PR:Q84JZ6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84JZ6; baseline and differential.
DR Genevisible; Q84JZ6; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0046983; F:protein dimerization activity; IPI:TAIR.
DR GO; GO:0016554; P:cytidine to uridine editing; IEA:InterPro.
DR GO; GO:0080156; P:mitochondrial mRNA modification; IMP:UniProtKB.
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 Alternative splicing; Mitochondrion; mRNA processing; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..62
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 63..244
FT /note="Multiple organellar RNA editing factor 3,
FT mitochondrial"
FT /id="PRO_0000432526"
FT REGION 59..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 127..128
FT /note="CE -> WQ (in isoform 2)"
FT /id="VSP_057527"
SQ SEQUENCE 244 AA; 27558 MW; 4886E4C8E24C323A CRC64;
MALISTRRTL STLLNKTLSS STSYSSSFPT LSSRSRFAMP LIEKVSSSRT SLGPCYISTR
PKTSGSGYSP LNDPSPNWSN RPPKETILLD GCDYEHWLIV MEFTDPKPTE EEMINSYVKT
LTSVLGCEEE AKKKIYSVCT STYTGFGALI SEELSCKVKA LPGVLWVLPD SYLDVPNKDY
GGDLYVEGKV IPRPQYRFTE QRHTRPRPRP RYDRRRETMQ VERREPSMGL HSPVNPGEFN
KPSA
