ORRM1_ARATH
ID ORRM1_ARATH Reviewed; 374 AA.
AC Q8L440; Q9LIH1;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Organelle RRM domain-containing protein 1, chloroplastic {ECO:0000303|PubMed:23487777};
DE Flags: Precursor;
GN Name=ORRM1 {ECO:0000303|PubMed:23487777};
GN OrderedLocusNames=At3g20930 {ECO:0000312|Araport:AT3G20930};
GN ORFNames=MFD22.4 {ECO:0000312|EMBL:BAB01902.1};
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=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]
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 [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 [5]
RP FUNCTION, INTERACTION WITH PCMP-H51/CRR28 AND PCMP-H12/OTP82, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23487777; DOI=10.1073/pnas.1220162110;
RA Sun T., Germain A., Giloteaux L., Hammani K., Barkan A., Hanson M.R.,
RA Bentolila S.;
RT "An RNA recognition motif-containing protein is required for plastid RNA
RT editing in Arabidopsis and maize.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E1169-E1178(2013).
RN [6]
RP INTERACTION WITH MORF8/RIP1; MORF2/RIP2 AND VAR3/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).
CC -!- FUNCTION: Involved in C-to-U editing of chloroplastic RNA. Functions as
CC major chloroplastic editing factor. Controls 62 percent of the
CC chloroplastic editing sites. Binds RNA close to ORRM1-dependent editing
CC sites in vitro. Binds the editing recognition trans-factors PCMP-
CC H51/CRR28 and PCMP-H12/OTP82. {ECO:0000269|PubMed:23487777}.
CC -!- SUBUNIT: Interacts with PCMP-H51/CRR28 and PCMP-H12/OTP82
CC (PubMed:23487777). Interacts with MORF8/RIP1, MORF2/RIP2 and VAR3/OZ1
CC (PubMed:25768119). {ECO:0000269|PubMed:23487777,
CC ECO:0000269|PubMed:25768119}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit severe editing defects in
CC chloroplastic transcripts. {ECO:0000269|PubMed:23487777}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01902.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP001304; BAB01902.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76442.1; -; Genomic_DNA.
DR EMBL; AY099828; AAM20679.1; -; mRNA.
DR EMBL; BT002195; AAN72206.1; -; mRNA.
DR EMBL; AY084565; AAM61131.1; -; mRNA.
DR RefSeq; NP_566672.1; NM_112985.5.
DR AlphaFoldDB; Q8L440; -.
DR SMR; Q8L440; -.
DR STRING; 3702.AT3G20930.1; -.
DR PaxDb; Q8L440; -.
DR PRIDE; Q8L440; -.
DR ProteomicsDB; 248825; -.
DR EnsemblPlants; AT3G20930.1; AT3G20930.1; AT3G20930.
DR GeneID; 821642; -.
DR Gramene; AT3G20930.1; AT3G20930.1; AT3G20930.
DR KEGG; ath:AT3G20930; -.
DR Araport; AT3G20930; -.
DR TAIR; locus:2088756; AT3G20930.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_056098_0_0_1; -.
DR InParanoid; Q8L440; -.
DR OMA; DEDCAQE; -.
DR PhylomeDB; Q8L440; -.
DR PRO; PR:Q8L440; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L440; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IDA:TAIR.
DR GO; GO:1900871; P:chloroplast mRNA 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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.30.70.80; -; 2.
DR InterPro; IPR039206; MORF/ORRM1/DAG-like.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR31346; PTHR31346; 2.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Chloroplast; mRNA processing; Plastid; Reference proteome; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..54
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 55..374
FT /note="Organelle RRM domain-containing protein 1,
FT chloroplastic"
FT /id="PRO_0000439868"
FT DOMAIN 282..360
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 258..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 41610 MW; B7EEBEBB26203E00 CRC64;
MEALIASTSF FVPISNSSSS HIINNRFFPS FYSPNLNFGT FRKTSLSSSH LVFSSSAISA
PPSSTVLTRN SYWMVLLDKP PHWVSSKSAM VDYYVEILAK VLGNEKDAQV SIYDASFDTH
FGFCCHIDED ASRQLASLPG VVSIRPEQDY SSEKKNYGIG SHKGVSLFDH GTVKHWMVRI
DKPGVGIVTK AQMVDHCVQL LSKVLWNEKD AQMCLYHVSW QSDFGFCCDL DERSAVELAG
VPGVLAVVPD NSFESLNKDY EGDSTQDSRD QDDSESPPVK TKKLFITGLS FYTSEKTLRA
AFEGFGELVE VKIIMDKISK RSKGYAFLEY TTEEAAGTAL KEMNGKIING WMIVVDVAKT
KPFRQNRSQP SFGL
