MORF4_ARATH
ID MORF4_ARATH Reviewed; 723 AA.
AC O48582;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Multiple organellar RNA editing factor 4, mitochondrial {ECO:0000305};
DE AltName: Full=RNA editing-interacting protein 4 {ECO:0000303|PubMed:23818871};
DE Flags: Precursor;
GN Name=MORF4 {ECO:0000303|PubMed:22411807};
GN Synonyms=RIP4 {ECO:0000303|PubMed:23818871};
GN OrderedLocusNames=At5g44780 {ECO:0000312|Araport:AT5G44780};
GN ORFNames=K23L20.12 {ECO:0000312|EMBL:BAB08831.1},
GN T19K24.11 {ECO:0000312|EMBL:AAC79143.1};
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, GENE FAMILY, AND NOMENCLATURE.
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, 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 [8]
RP INTERACTION WITH MORF8/RIP1; MORF1/RIP8 AND MORF3/RIP3, AND SUBCELLULAR
RP 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 few RNA editing site in mitochondria.
CC {ECO:0000269|PubMed:22411807, ECO:0000269|PubMed:23818871}.
CC -!- SUBUNIT: Heterodimers with MORF8/RIP1, MORF1/RIP8 and MORF3/RIP3.
CC {ECO:0000269|PubMed:25583991}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25583991}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:23818871}.
CC -!- SIMILARITY: Belongs to the MORF family.
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DR EMBL; AB016874; BAB08831.1; -; Genomic_DNA.
DR EMBL; AC002342; AAC79143.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95160.1; -; Genomic_DNA.
DR EMBL; BT012578; AAS99722.1; -; mRNA.
DR EMBL; AK221549; BAD94930.1; -; mRNA.
DR RefSeq; NP_199291.1; NM_123845.4.
DR AlphaFoldDB; O48582; -.
DR SMR; O48582; -.
DR STRING; 3702.AT5G44780.1; -.
DR PaxDb; O48582; -.
DR PRIDE; O48582; -.
DR ProteomicsDB; 250936; -.
DR EnsemblPlants; AT5G44780.1; AT5G44780.1; AT5G44780.
DR GeneID; 834507; -.
DR Gramene; AT5G44780.1; AT5G44780.1; AT5G44780.
DR KEGG; ath:AT5G44780; -.
DR Araport; AT5G44780; -.
DR TAIR; locus:2156344; AT5G44780.
DR eggNOG; ENOG502QUVM; Eukaryota.
DR HOGENOM; CLU_392989_0_0_1; -.
DR InParanoid; O48582; -.
DR OrthoDB; 659230at2759; -.
DR PhylomeDB; O48582; -.
DR PRO; PR:O48582; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O48582; baseline and differential.
DR Genevisible; O48582; AT.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; 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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR039206; MORF/ORRM1/DAG-like.
DR PANTHER; PTHR31346; PTHR31346; 3.
PE 1: Evidence at protein level;
KW Mitochondrion; mRNA processing; Reference proteome; Transit peptide.
FT TRANSIT 1..64
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 65..723
FT /note="Multiple organellar RNA editing factor 4,
FT mitochondrial"
FT /id="PRO_0000432527"
FT REGION 180..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 79034 MW; 0F840DE327A89228 CRC64;
MAMFSHRLRR IVVAAPSYFQ RFSTLSRPSD FTPVPSLLPR SVVKQSTAIN RSPARLFSTT
QYQYDPYTGE DSFMPDNEGC DFNHWLITMN FPKDNLPSRE EMISIFEQTC AKGLAISLEE
AKKKIYAICT TSYQGFQATM TIGEVEKFRD LPGVQYIIPD SYIDVENKVY GGDKYENGVI
TPGPVPVPTK EGFDSLKKES KPEQEEAEII LTPPDEGKTS GQVQGQGSLT LPDQRSVKER
QGTLALVQGQ GQRSGMSILG QGQGEGRRMS IPGQWQSRGQ GNSFQGSFKQ SQGTLPVRKG
QTQISDEIPS FQGNVKQRQE MPIHGQGQAQ RSQMPSSQGT LRQGQAQGSQ RPSNQVGYNQ
GQGAQTPPYH QGQGAQTPPY QESPNNYGQG AFVQYNQGPP QGNVVQTTQE KYNQMGQGNY
APQSGGNYSP AQGAGSPRFG YGQGQGGQLL SPYRGNYNQG QGTPLPGQGQ EGQPSYQMGF
SQGLGAPVPP NQVIPGNYGQ WAFVNYNQGP PQGNFLQGPQ QNHNQGGQWN YSPQNGGHYG
PAQFGQWYPG PPQGQGIQWP QYQLSYNQGQ GTPFSGQCRC PNCGMTSYQG YNNQGQGTHI
PEQWEGQDYA VLSYQASYNQ AHGAQAPPYH GNYNQATPGG YGQGTSANFN QRFPVNPANY
NMQNGGNYGP PHGLAGNPGF RQGFSGQGQN QTFQQDDQRN VAGDLRNNNP VDPTETRKPN
SRI
