RD521_ARATH
ID RD521_ARATH Reviewed; 176 AA.
AC Q9FVV7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=DNA repair RAD52-like protein 1, mitochondrial {ECO:0000305};
DE AltName: Full=Organellar DNA-binding protein 1 {ECO:0000303|PubMed:22762281};
DE Flags: Precursor;
GN Name=RAD52-1 {ECO:0000303|PubMed:22202891};
GN Synonyms=ODB1 {ECO:0000303|PubMed:22762281};
GN OrderedLocusNames=At1g71310 {ECO:0000312|Araport:AT1G71310};
GN ORFNames=F3I17.4 {ECO:0000312|EMBL:AAG51886.1};
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=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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22202891; DOI=10.1105/tpc.111.091744;
RA Samach A., Melamed-Bessudo C., Avivi-Ragolski N., Pietrokovski S.,
RA Levy A.A.;
RT "Identification of plant RAD52 homologs and characterization of the
RT Arabidopsis thaliana RAD52-like genes.";
RL Plant Cell 23:4266-4279(2011).
RN [5]
RP FUNCTION, INTERACTION WITH WHY2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=22762281; DOI=10.1111/j.1365-313x.2012.05097.x;
RA Janicka S., Kuehn K., Le Ret M., Bonnard G., Imbault P., Augustyniak H.,
RA Gualberto J.M.;
RT "A RAD52-like single-stranded DNA binding protein affects mitochondrial DNA
RT repair by recombination.";
RL Plant J. 72:423-435(2012).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26048959; DOI=10.1093/nar/gkv540;
RA Gualberto J.M., Le Ret M., Beator B., Kuehn K.;
RT "The RAD52-like protein ODB1 is required for the efficient excision of two
RT mitochondrial introns spliced via first-step hydrolysis.";
RL Nucleic Acids Res. 43:6500-6510(2015).
CC -!- FUNCTION: Plant-specific single-stranded DNA-binding protein required
CC for efficient heterologous recombination-dependent DNA repair in
CC nuclear and mitochondrial compartments. Forms large nucleo-protein
CC complexes with WHY2 in mitochondria. Binds ssDNA with high affinity,
CC but with little sequence specificity (PubMed:22762281). Involved in
CC double-stranded DNA break repair (PubMed:22202891). Involved in the
CC hydrolytic splicing pathway in mitochondrion. Facilitates the excision
CC of two cis-spliced group II introns, NAD1 intron 2 and NAD2 intron 1
CC (PubMed:26048959). {ECO:0000269|PubMed:22202891,
CC ECO:0000269|PubMed:22762281, ECO:0000269|PubMed:26048959}.
CC -!- SUBUNIT: Interacts with WHY2. {ECO:0000269|PubMed:22762281}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:22202891,
CC ECO:0000269|PubMed:22762281, ECO:0000269|PubMed:26048959}. Nucleus
CC {ECO:0000269|PubMed:22202891}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q9FVV7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in root vascular tissue, tips of primary
CC and secondary roots, young leaves, hydathodes, stomatal guard cells,
CC cauline leaves, flower buds, stipules, carpels, pistils and anther
CC filaments. {ECO:0000269|PubMed:22762281}.
CC -!- DISRUPTION PHENOTYPE: Reduced fertility, increased sensitivity to
CC mitomycin C, and decreased levels of intrachromosomal recombination.
CC {ECO:0000269|PubMed:26048959}.
CC -!- SIMILARITY: Belongs to the RAD52 family. {ECO:0000305}.
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DR EMBL; AC016162; AAG51886.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35186.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35187.1; -; Genomic_DNA.
DR EMBL; AY128372; AAM91575.1; -; mRNA.
DR EMBL; BT000380; AAN15699.1; -; mRNA.
DR PIR; H96737; H96737.
DR RefSeq; NP_177287.1; NM_105800.2. [Q9FVV7-1]
DR RefSeq; NP_849876.1; NM_179545.3. [Q9FVV7-1]
DR AlphaFoldDB; Q9FVV7; -.
DR SMR; Q9FVV7; -.
DR STRING; 3702.AT1G71310.1; -.
DR PaxDb; Q9FVV7; -.
DR PRIDE; Q9FVV7; -.
DR ProteomicsDB; 225952; -. [Q9FVV7-1]
DR EnsemblPlants; AT1G71310.1; AT1G71310.1; AT1G71310. [Q9FVV7-1]
DR EnsemblPlants; AT1G71310.2; AT1G71310.2; AT1G71310. [Q9FVV7-1]
DR GeneID; 843472; -.
DR Gramene; AT1G71310.1; AT1G71310.1; AT1G71310. [Q9FVV7-1]
DR Gramene; AT1G71310.2; AT1G71310.2; AT1G71310. [Q9FVV7-1]
DR KEGG; ath:AT1G71310; -.
DR Araport; AT1G71310; -.
DR TAIR; locus:2032313; AT1G71310.
DR eggNOG; ENOG502RXQN; Eukaryota.
DR HOGENOM; CLU_095139_1_0_1; -.
DR InParanoid; Q9FVV7; -.
DR OMA; AIKYIPW; -.
DR PhylomeDB; Q9FVV7; -.
DR PRO; PR:Q9FVV7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FVV7; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:TAIR.
DR GO; GO:0000373; P:Group II intron splicing; IMP:UniProtKB.
DR Gene3D; 3.30.390.80; -; 1.
DR InterPro; IPR037489; RAD52-like.
DR InterPro; IPR042525; Rad52_Rad59_Rad22_sf.
DR PANTHER; PTHR34050; PTHR34050; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Mitochondrion; Nucleus; Reference proteome; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..176
FT /note="DNA repair RAD52-like protein 1, mitochondrial"
FT /id="PRO_0000438186"
SQ SEQUENCE 176 AA; 19484 MW; 5B98E14D48DDEB30 CRC64;
MAGLGLRLKA AKWTLRSGSG AVSREWSSEM GKGVRRFSTE TENDVPTSGI SRPLAEILKE
LNKKVPDSVI RTRVEDGCSI KYIPWHIVNR IMNMHAPEWS GEVRSVTYSP DGNTVTVAYR
VTLYGTDAEI FRESTGTTSV DDKGYGDAVQ KAEAMAFRRA CARFGLGLHL YHEDAL
