MORF2_ARATH
ID MORF2_ARATH Reviewed; 219 AA.
AC O22793; O24657; Q7DLI5; Q8L949;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Multiple organellar RNA editing factor 2, chloroplastic {ECO:0000305};
DE AltName: Full=Protein DIFFERENTIATION AND GREENING-like 1 {ECO:0000303|PubMed:12678554};
DE Short=Protein DAG-like 1 {ECO:0000305};
DE AltName: Full=RNA editing-interacting protein 2 {ECO:0000303|PubMed:23818871};
DE Flags: Precursor;
GN Name=MORF2 {ECO:0000303|PubMed:22411807};
GN Synonyms=DAL1 {ECO:0000303|PubMed:12678554},
GN RIP2 {ECO:0000303|PubMed:23818871};
GN OrderedLocusNames=At2g33430 {ECO:0000312|Araport:AT2G33430};
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 [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC TISSUE=Leaf;
RX PubMed=9356517; DOI=10.1073/pnas.94.23.12722;
RA Babiychuk E., Fuangthong M., Van Montagu M., Inze D., Kushnir S.;
RT "Efficient gene tagging in Arabidopsis thaliana using a gene trap
RT approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:12722-12727(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=12678554; DOI=10.1023/a:1022557825768;
RA Bisanz C., Begot L., Carol P., Perez P., Bligny M., Pesey H., Gallois J.L.,
RA Lerbs-Mache S., Mache R.;
RT "The Arabidopsis nuclear DAL gene encodes a chloroplast protein which is
RT required for the maturation of the plastid ribosomal RNAs and is essential
RT for chloroplast differentiation.";
RL Plant Mol. Biol. 51:651-663(2003).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, INTERACTION WITH MORF9, 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 [9]
RP FUNCTION, AND GENE FAMILY.
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 [10]
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 [11]
RP HOMODIMERIZATION, INTERACTION WITH MORF8/RIP1 AND MORF9/RIP9, AND
RP 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 [12]
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 [13]
RP INTERACTION WITH ORRM1.
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 [14]
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 plastid rRNA processing and consequently in
CC translation and early chloroplast differentiation (PubMed:12678554).
CC Involved in organellar RNA editing. Required for the processing of
CC multiple editing sites in plastids (PubMed:22411807, PubMed:23818871).
CC {ECO:0000269|PubMed:12678554, ECO:0000269|PubMed:22411807,
CC ECO:0000269|PubMed:23818871}.
CC -!- SUBUNIT: Homodimer and heterodimer with MORF9 (PubMed:22411807,
CC PubMed:25583991). Interacts with protoporphyrinogen oxidase 1 PPOX1
CC (PubMed:24497494). Heterodimers with MORF8/RIP1 and MORF9/RIP9
CC (PubMed:25583991). Interacts with PCMP-A2/PMD1 (PubMed:26123918).
CC Interacts with ORRM1 (PubMed:25768119). Interacts with ORRM6
CC (PubMed:28213559). {ECO:0000269|PubMed:22411807,
CC ECO:0000269|PubMed:24497494, ECO:0000269|PubMed:25583991,
CC ECO:0000269|PubMed:25768119, ECO:0000269|PubMed:26123918,
CC ECO:0000269|PubMed:28213559}.
CC -!- INTERACTION:
CC O22793; Q9FYK5: ESR2; NbExp=3; IntAct=EBI-1998046, EBI-1536925;
CC O22793; O23160: MYB73; NbExp=3; IntAct=EBI-1998046, EBI-25506855;
CC O22793; P49598: PP2CA; NbExp=3; IntAct=EBI-1998046, EBI-1764934;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:12678554, ECO:0000269|PubMed:25583991,
CC ECO:0000269|PubMed:28213559}.
CC -!- DISRUPTION PHENOTYPE: Small plants with white leaves that do not
CC contain chlorophyll. Mutant plants are unable to grow autotrophically
CC on soil and flowers are sterile. {ECO:0000269|PubMed:12678554,
CC ECO:0000269|PubMed:22411807}.
CC -!- SIMILARITY: Belongs to the MORF family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB06698.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z86094; CAB06698.1; ALT_FRAME; mRNA.
DR EMBL; Y14850; CAA75115.1; -; mRNA.
DR EMBL; Y14851; CAA75116.1; -; Genomic_DNA.
DR EMBL; AC002332; AAB80660.1; -; Genomic_DNA.
DR EMBL; CP002685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF446351; AAL48226.1; -; mRNA.
DR EMBL; AY097425; AAM19941.1; -; mRNA.
DR EMBL; AK228465; BAF00392.1; -; mRNA.
DR EMBL; AY088637; AAM66959.1; -; mRNA.
DR PIR; D84745; D84745.
DR PIR; T52623; T52623.
DR PDB; 5YDG; X-ray; 2.40 A; A/B=79-194.
DR PDBsum; 5YDG; -.
DR AlphaFoldDB; O22793; -.
DR SMR; O22793; -.
DR IntAct; O22793; 4.
DR STRING; 3702.AT2G33430.1; -.
DR PaxDb; O22793; -.
DR PeptideAtlas; O22793; -.
DR PRIDE; O22793; -.
DR Araport; AT2G33430; -.
DR TAIR; locus:2051003; AT2G33430.
DR eggNOG; ENOG502QPXC; Eukaryota.
DR HOGENOM; CLU_073703_1_0_1; -.
DR InParanoid; O22793; -.
DR PhylomeDB; O22793; -.
DR PRO; PR:O22793; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22793; baseline and differential.
DR Genevisible; O22793; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IEA:InterPro.
DR GO; GO:0002103; P:endonucleolytic cleavage of tetracistronic rRNA transcript (SSU-rRNA, LSU-rRNA, 4.5S-rRNA, 5S-rRNA); IMP:TAIR.
DR GO; GO:0080156; P:mitochondrial mRNA modification; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0009657; P:plastid organization; IMP:TAIR.
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; Chloroplast; mRNA processing; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..219
FT /note="Multiple organellar RNA editing factor 2,
FT chloroplastic"
FT /id="PRO_0000432525"
FT REGION 182..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 102..103
FT /note="QQ -> HE (in Ref. 2; CAA75115/CAA75116)"
FT /evidence="ECO:0000305"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:5YDG"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:5YDG"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:5YDG"
FT STRAND 126..140
FT /evidence="ECO:0007829|PDB:5YDG"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:5YDG"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:5YDG"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:5YDG"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:5YDG"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:5YDG"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:5YDG"
SQ SEQUENCE 219 AA; 24715 MW; AD8CB0EAD343B638 CRC64;
MALPLSGTRH LTRALLSNVT LMAPPRIPSS VHYGGSRLGC STRFFSIRCG ANRSGSTYSP
LNSGSNFSDR PPTEMAPLFP GCDYEHWLIV MDKPGGEGAT KQQMIDCYIQ TLAKVVGSEE
EAKKRIYNVS CERYLGFGCE IDEETSTKLE GLPGVLFVLP DSYVDPENKD YGAELFVNGE
IVQRSPERQR RVEPQPQRAQ DRPRYNDRTR YSRRRENTR
