MORF9_ARATH
ID MORF9_ARATH Reviewed; 232 AA.
AC Q9LPZ1; Q8LB30;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Multiple organellar RNA editing factor 9, chloroplastic {ECO:0000305};
DE AltName: Full=RNA editing-interacting protein 9 {ECO:0000303|PubMed:23818871};
DE Flags: Precursor;
GN Name=MORF9 {ECO:0000303|PubMed:22411807};
GN Synonyms=RIP9 {ECO:0000303|PubMed:23818871};
GN OrderedLocusNames=At1g11430 {ECO:0000312|Araport:AT1G11430};
GN ORFNames=T23J18.10 {ECO:0000312|EMBL:AAF16628.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
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 [6]
RP FUNCTION, INTERACTION WITH MORF2, 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 [7]
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 [8]
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 [9]
RP HOMODIMERIZATION, INTERACTION WITH MORF2/RIP2 AND MORF5/RIP5, 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 [10]
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 [11]
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).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 86-186.
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 multiple editing sites in plastids.
CC {ECO:0000269|PubMed:22411807, ECO:0000269|PubMed:23818871}.
CC -!- SUBUNIT: Homodimer and heterodimer with MORF2 (PubMed:22411807,
CC PubMed:25583991). Interacts with protoporphyrinogen oxidase 1 PPOX1
CC (PubMed:24497494). Heterodimer with MORF5/RIP5 (PubMed:25583991).
CC Interacts with PCMP-A2/PMD1 (PubMed:26123918). Interacts with ORRM6
CC (PubMed:28213559). {ECO:0000269|PubMed:22411807,
CC ECO:0000269|PubMed:24497494, ECO:0000269|PubMed:25583991,
CC ECO:0000269|PubMed:26123918, ECO:0000269|PubMed:28213559}.
CC -!- INTERACTION:
CC Q9LPZ1; Q38845: PP2AA1; NbExp=3; IntAct=EBI-4424647, EBI-1645478;
CC Q9LPZ1; Q9LF53: RGL3; NbExp=3; IntAct=EBI-4424647, EBI-15681313;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:25583991, ECO:0000269|PubMed:28213559}.
CC -!- DISRUPTION PHENOTYPE: White leaves with green islands, giving a
CC variegated appearance. Mutant plants can grow autotrophically on soil.
CC {ECO:0000269|PubMed:22411807}.
CC -!- SIMILARITY: Belongs to the MORF family.
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DR EMBL; AC011661; AAF16628.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28735.1; -; Genomic_DNA.
DR EMBL; AK117508; BAC42171.1; -; mRNA.
DR EMBL; BT005071; AAO50604.1; -; mRNA.
DR EMBL; AY087455; AAM65001.1; -; mRNA.
DR RefSeq; NP_172610.1; NM_101016.4.
DR PDB; 5GI0; X-ray; 2.04 A; A=75-196.
DR PDB; 5IWB; X-ray; 1.76 A; A=75-196.
DR PDB; 5IWW; X-ray; 2.65 A; A/B/C=75-196.
DR PDB; 5MPY; X-ray; 2.25 A; A/B=86-186.
DR PDBsum; 5GI0; -.
DR PDBsum; 5IWB; -.
DR PDBsum; 5IWW; -.
DR PDBsum; 5MPY; -.
DR AlphaFoldDB; Q9LPZ1; -.
DR SMR; Q9LPZ1; -.
DR IntAct; Q9LPZ1; 3.
DR STRING; 3702.AT1G11430.1; -.
DR PaxDb; Q9LPZ1; -.
DR PRIDE; Q9LPZ1; -.
DR ProMEX; Q9LPZ1; -.
DR ProteomicsDB; 250939; -.
DR EnsemblPlants; AT1G11430.1; AT1G11430.1; AT1G11430.
DR GeneID; 837685; -.
DR Gramene; AT1G11430.1; AT1G11430.1; AT1G11430.
DR KEGG; ath:AT1G11430; -.
DR Araport; AT1G11430; -.
DR TAIR; locus:2200131; AT1G11430.
DR eggNOG; ENOG502QVUD; Eukaryota.
DR HOGENOM; CLU_073703_0_0_1; -.
DR InParanoid; Q9LPZ1; -.
DR OMA; YRSPNAP; -.
DR OrthoDB; 1367806at2759; -.
DR PhylomeDB; Q9LPZ1; -.
DR PRO; PR:Q9LPZ1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPZ1; baseline and differential.
DR Genevisible; Q9LPZ1; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; 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:1900865; P:chloroplast RNA modification; IMP:TAIR.
DR GO; GO:0016554; P:cytidine to uridine editing; IEA:InterPro.
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; Chloroplast; mRNA processing; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 59..232
FT /note="Multiple organellar RNA editing factor 9,
FT chloroplastic"
FT /id="PRO_0000432531"
FT REGION 190..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 44
FT /note="N -> S (in Ref. 5; AAM65001)"
FT /evidence="ECO:0000305"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:5IWB"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5GI0"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:5IWB"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:5IWB"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:5IWB"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:5IWB"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:5IWB"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:5IWB"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:5IWB"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:5IWB"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5IWB"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5IWB"
SQ SEQUENCE 232 AA; 26201 MW; 7E26445D058C24EC CRC64;
MASFTTTSSS SLLLKTLLPV SHLNRFSTLS GIRVGDSWTP LLRNISTAGS RRRVAIVKAA
TVDSDYSSKR SNSNEQRETI MLPGCDYNHW LIVMEFPKDP APSRDQMIDT YLNTLATVLG
SMEEAKKNMY AFSTTTYTGF QCTIDEETSE KFKGLPGVLW VLPDSYIDVK NKDYGGDKYI
NGEIIPCTYP TYQPKQRNNT KYQSKRYERK RDGPPPPEQR KPRQEPAASD SS
