RUG3_ARATH
ID RUG3_ARATH Reviewed; 445 AA.
AC Q9FJG9; B3LF49; F4K0I4; Q56Y67;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=RCC1 domain-containing protein RUG3, mitochondrial {ECO:0000303|PubMed:21623974};
DE AltName: Full=RCC1/UVR8/GEF-like protein 3, mitochondrial {ECO:0000303|PubMed:21623974};
DE Flags: Precursor;
GN Name=RUG3 {ECO:0000303|PubMed:21623974};
GN OrderedLocusNames=At5g60870 {ECO:0000312|Araport:AT5G60870};
GN ORFNames=MAE1.11 {ECO:0000312|EMBL:BAB10107.1};
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-445 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA de los Reyes C., Quan R., Chen H., Bautista V., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21623974; DOI=10.1111/j.1365-313x.2011.04658.x;
RA Kuehn K., Carrie C., Giraud E., Wang Y., Meyer E.H., Narsai R.,
RA des Francs-Small C.C., Zhang B., Murcha M.W., Whelan J.;
RT "The RCC1 family protein RUG3 is required for splicing of nad2 and complex
RT I biogenesis in mitochondria of Arabidopsis thaliana.";
RL Plant J. 67:1067-1080(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28613105; DOI=10.1080/15592324.2017.1333217;
RA Su C., Yuan J., Zhao H., Zhao Y., Ji H., Wang Y., Li X.;
RT "RUG3 is a negative regulator of plant responses to ABA in Arabidopsis
RT thaliana.";
RL Plant Signal. Behav. 12:E1333217-E1333217(2017).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ATM, TISSUE SPECIFICITY,
RP REGULATION BY METHYL METHANESULFONATE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=28262819; DOI=10.1038/srep43897;
RA Su C., Zhao H., Zhao Y., Ji H., Wang Y., Zhi L., Li X.;
RT "RUG3 and ATM synergistically regulate the alternative splicing of
RT mitochondrial nad2 and the DNA damage response in Arabidopsis thaliana.";
RL Sci. Rep. 7:43897-43897(2017).
CC -!- FUNCTION: Regulates DNA damage response (DDR) synergistically with ATM
CC (PubMed:28262819). Together with ATM, involved in the splicing of the
CC ND2/NAD2 mRNA (PubMed:21623974, PubMed:28262819). Required for the
CC accumulation of mitochondrial respiratory chain complex I
CC (PubMed:21623974). Negative regulator of plant responses to abscisic
CC acid (ABA) (PubMed:28613105). May have a pivotal role in vegetative
CC growth and the phase transition from vegetative to reproductive growth
CC (PubMed:28262819). {ECO:0000269|PubMed:21623974,
CC ECO:0000269|PubMed:28262819, ECO:0000269|PubMed:28613105}.
CC -!- SUBUNIT: Interacts with ATM. {ECO:0000269|PubMed:28262819}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21623974,
CC ECO:0000269|PubMed:28262819}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9FJG9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FJG9-2; Sequence=VSP_059685;
CC Name=3;
CC IsoId=Q9FJG9-3; Sequence=VSP_059686;
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and rosette leaves of
CC young seedlings, and, to a lower extent, in the flowers and siliques of
CC mature plants. Preferentially expressed in the vascular tissues.
CC {ECO:0000269|PubMed:28262819}.
CC -!- INDUCTION: Reduced by methyl methanesulfonate (MMS) treatment.
CC {ECO:0000269|PubMed:28262819}.
CC -!- DISRUPTION PHENOTYPE: Delayed development including late seed
CC germination and cotyledon greening as well as delayed flowering time,
CC short roots and mildly curled rosette leaves in long-day conditions,
CC thus leading to extended life span (PubMed:21623974, PubMed:28262819).
CC Reduced root length is associated with a smaller size of the root
CC apical meristem (RAM) due to a decreased cortical cell number
CC (PubMed:28262819). Reduced mitochondrial complex I abundance and
CC activity. Lower levels of complex I subunits NAD9 and FRO1, but induced
CC expression of the alternative oxidase (AOX) (PubMed:21623974). Reduced
CC splicing efficiencies for both the trans-spliced intron 2 and the cis-
CC spliced intron 3 of ND2/NAD2 mRNA (PubMed:21623974, PubMed:28262819).
CC Increased capacities for import of nucleus-encoded mitochondrial
CC proteins into the organelle and moderately increased mitochondrial
CC transcript levels (PubMed:21623974). Increased plant responses to
CC abscisic acid (ABA) during seed germination and post-germinative growth
CC (PubMed:28613105). Augmented DNA damage response (DDR) associated with
CC increased intracellular reactive oxygen species (ROS) levels and cell
CC cycle arrest at the G2/M checkpoint in the root apical meristem (RAM),
CC thus leading to root growth retardation (PubMed:28262819).
CC {ECO:0000269|PubMed:21623974, ECO:0000269|PubMed:28262819,
CC ECO:0000269|PubMed:28613105}.
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DR EMBL; AB015472; BAB10107.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97388.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97389.2; -; Genomic_DNA.
DR EMBL; CP002688; AED97390.1; -; Genomic_DNA.
DR EMBL; AK221456; BAD94537.1; -; mRNA.
DR EMBL; BT033037; ACE79739.1; -; mRNA.
DR RefSeq; NP_001078775.1; NM_001085306.1. [Q9FJG9-2]
DR RefSeq; NP_200895.2; NM_125480.4. [Q9FJG9-1]
DR RefSeq; NP_974971.2; NM_203242.2. [Q9FJG9-3]
DR AlphaFoldDB; Q9FJG9; -.
DR SMR; Q9FJG9; -.
DR STRING; 3702.AT5G60870.1; -.
DR PaxDb; Q9FJG9; -.
DR PRIDE; Q9FJG9; -.
DR ProteomicsDB; 228057; -. [Q9FJG9-1]
DR EnsemblPlants; AT5G60870.1; AT5G60870.1; AT5G60870. [Q9FJG9-1]
DR EnsemblPlants; AT5G60870.2; AT5G60870.2; AT5G60870. [Q9FJG9-3]
DR EnsemblPlants; AT5G60870.3; AT5G60870.3; AT5G60870. [Q9FJG9-2]
DR GeneID; 836208; -.
DR Gramene; AT5G60870.1; AT5G60870.1; AT5G60870. [Q9FJG9-1]
DR Gramene; AT5G60870.2; AT5G60870.2; AT5G60870. [Q9FJG9-3]
DR Gramene; AT5G60870.3; AT5G60870.3; AT5G60870. [Q9FJG9-2]
DR KEGG; ath:AT5G60870; -.
DR Araport; AT5G60870; -.
DR TAIR; locus:2159295; AT5G60870.
DR eggNOG; KOG1426; Eukaryota.
DR HOGENOM; CLU_030760_1_0_1; -.
DR InParanoid; Q9FJG9; -.
DR OMA; KLWIWGK; -.
DR OrthoDB; 1062377at2759; -.
DR PhylomeDB; Q9FJG9; -.
DR PRO; PR:Q9FJG9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJG9; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0072702; P:response to methyl methanesulfonate; IEP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:UniProtKB.
DR Gene3D; 2.130.10.30; -; 2.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR Pfam; PF00415; RCC1; 7.
DR PRINTS; PR00633; RCCNDNSATION.
DR SUPFAM; SSF50985; SSF50985; 1.
DR PROSITE; PS00626; RCC1_2; 1.
DR PROSITE; PS50012; RCC1_3; 6.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; DNA damage;
KW Mitochondrion; mRNA processing; mRNA splicing; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..445
FT /note="RCC1 domain-containing protein RUG3, mitochondrial"
FT /id="PRO_0000445001"
FT REPEAT 47..101
FT /note="RCC1 1"
FT /evidence="ECO:0000255"
FT REPEAT 118..169
FT /note="RCC1 2"
FT /evidence="ECO:0000255"
FT REPEAT 171..221
FT /note="RCC1 3"
FT /evidence="ECO:0000255"
FT REPEAT 222..279
FT /note="RCC1 4"
FT /evidence="ECO:0000255"
FT REPEAT 280..331
FT /note="RCC1 5"
FT /evidence="ECO:0000255"
FT REPEAT 333..383
FT /note="RCC1 6"
FT /evidence="ECO:0000255"
FT REPEAT 385..442
FT /note="RCC1 7"
FT /evidence="ECO:0000255"
FT VAR_SEQ 2..176
FT /note="AALSHRLRSFTRRFSSTRTTQRSGGGANTKVPILYTSPDIDSDPVTLQLFSW
FT GRGASGQLGGGIEEIRMYPSPVANLLFRSDQSFSLAQTPGRIDADSSSFRIGISCGLFH
FT SGLTIDGDLWIWGKGDGGRLGFGQENSVFVPNLNPLFEEHSIRCIALGGLHSVALTHQG
FT DVFTW -> YSLVVR (in isoform 2)"
FT /id="VSP_059685"
FT VAR_SEQ 381
FT /note="I -> ITGWDWFL (in isoform 3)"
FT /id="VSP_059686"
SQ SEQUENCE 445 AA; 47331 MW; D7C93CF44087C594 CRC64;
MAALSHRLRS FTRRFSSTRT TQRSGGGANT KVPILYTSPD IDSDPVTLQL FSWGRGASGQ
LGGGIEEIRM YPSPVANLLF RSDQSFSLAQ TPGRIDADSS SFRIGISCGL FHSGLTIDGD
LWIWGKGDGG RLGFGQENSV FVPNLNPLFE EHSIRCIALG GLHSVALTHQ GDVFTWGYGG
FGALGHKVYT RELVPRRVDD SWDCKISAIA TSGTHTAAIT ESGELYMWGR EEGDGRLGLG
PGRGPNEGGG LSVPSKVKAL TVPVASVSCG GFFTMALTKE GQLWNWGANS NYELGRGDNL
GGWEPMPVPS LEGVRITQIA CGGYHSLALT EEGKVLSWGH GGHGQLGSSS LRNQKVPTEI
EALADKKIVF IASGGSSSAA ITDGGELWMW GNAKDFQLGV PGLPEIQTTP VEVNFLTEED
ECQPHKVISI SIGASHALCL VSRSP
