BOLA2_ARATH
ID BOLA2_ARATH Reviewed; 93 AA.
AC Q9FIC3;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Protein BOLA2 {ECO:0000303|PubMed:24203231};
GN Name=BOLA2 {ECO:0000303|PubMed:24203231};
GN OrderedLocusNames=At5g09830 {ECO:0000312|Araport:AT5G09830};
GN ORFNames=MYH9.4 {ECO:0000312|EMBL:BAB09404.1};
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 {ECO:0000312|Proteomes:UP000006548};
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 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].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 SUBCELLULAR LOCATION, INTERACTION WITH GRXC5; GRXS14; GRXS15; GRXS16 AND
RP GRXS17, GLUTATHIONYLATION AT CYS-29, SUBUNIT, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=24203231; DOI=10.1093/mp/sst156;
RA Couturier J., Wu H.C., Dhalleine T., Pegeot H., Sudre D., Gualberto J.M.,
RA Jacquot J.P., Gaymard F., Vignols F., Rouhier N.;
RT "Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis
RT thaliana BolA2 and SufE1.";
RL Mol. Plant 7:187-205(2014).
RN [7]
RP FUNCTION, AND INTERACTION WITH GRXS17.
RX PubMed=24714563; DOI=10.4161/psb.28564;
RA Dhalleine T., Rouhier N., Couturier J.;
RT "Putative roles of glutaredoxin-BolA holo-heterodimers in plants.";
RL Plant Signal. Behav. 9:E28564-E28564(2014).
RN [8]
RP STRUCTURE BY NMR IN COMPLEX WITH GRXS17, AND DOMAIN.
RX PubMed=25012657; DOI=10.1074/jbc.m114.572701;
RA Roret T., Tsan P., Couturier J., Zhang B., Johnson M.K., Rouhier N.,
RA Didierjean C.;
RT "Structural and spectroscopic insights into BolA-glutaredoxin complexes.";
RL J. Biol. Chem. 289:24588-24598(2014).
CC -!- FUNCTION: May act either alone or in interaction with glutaredoxin as a
CC redox-regulated transcriptional regulator, or as a factor regulating
CC Fe-S cluster biogenesis (Probable). The GRXS17-BOLA2 heterodimer binds
CC a labile, oxygen sensitive iron-sulfur cluster (PubMed:24714563).
CC {ECO:0000269|PubMed:24714563, ECO:0000305|PubMed:24203231}.
CC -!- SUBUNIT: Homodimer (PubMed:24203231). Interacts in vitro with GRXS14,
CC GRXS15, GRXS16 and GRXS17, but not with GRXC5 (PubMed:24203231).
CC Interacts in vivo only with GRXS17 (PubMed:24203231, PubMed:24714563).
CC {ECO:0000269|PubMed:24203231, ECO:0000269|PubMed:24714563}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24203231}. Nucleus
CC {ECO:0000269|PubMed:24203231}.
CC -!- DOMAIN: The putative nucleic acid binding region (34-77) coincides with
CC the interaction surface with glutaredoxin.
CC {ECO:0000269|PubMed:25012657}.
CC -!- PTM: Can be either glutathionylated or forming covalent homodimers,
CC depending on the oxidation state. {ECO:0000269|PubMed:24203231}.
CC -!- SIMILARITY: Belongs to the bolA/yrbA family.
CC {ECO:0000255|RuleBase:RU003860}.
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DR EMBL; AB016893; BAB09404.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91453.1; -; Genomic_DNA.
DR EMBL; BT003151; AAO24583.1; -; mRNA.
DR EMBL; AK228169; BAF00125.1; -; mRNA.
DR EMBL; AY087656; AAM65194.1; -; mRNA.
DR RefSeq; NP_568217.1; NM_121020.5.
DR PDB; 2MM9; NMR; -; A=1-93.
DR PDB; 2MMA; NMR; -; B=2-93.
DR PDB; 4PUH; X-ray; 1.90 A; A/B=1-93.
DR PDBsum; 2MM9; -.
DR PDBsum; 2MMA; -.
DR PDBsum; 4PUH; -.
DR AlphaFoldDB; Q9FIC3; -.
DR BMRB; Q9FIC3; -.
DR SMR; Q9FIC3; -.
DR IntAct; Q9FIC3; 3.
DR STRING; 3702.AT5G09830.1; -.
DR PaxDb; Q9FIC3; -.
DR PRIDE; Q9FIC3; -.
DR ProteomicsDB; 240671; -.
DR EnsemblPlants; AT5G09830.1; AT5G09830.1; AT5G09830.
DR GeneID; 830843; -.
DR Gramene; AT5G09830.1; AT5G09830.1; AT5G09830.
DR KEGG; ath:AT5G09830; -.
DR Araport; AT5G09830; -.
DR TAIR; locus:2178143; AT5G09830.
DR eggNOG; KOG3348; Eukaryota.
DR HOGENOM; CLU_109462_4_0_1; -.
DR InParanoid; Q9FIC3; -.
DR OMA; NCGSSFE; -.
DR OrthoDB; 1571278at2759; -.
DR PhylomeDB; Q9FIC3; -.
DR PRO; PR:Q9FIC3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIC3; baseline and differential.
DR Genevisible; Q9FIC3; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IEA:InterPro.
DR GO; GO:0010039; P:response to iron ion; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR Gene3D; 3.30.300.90; -; 1.
DR InterPro; IPR045115; BOL2.
DR InterPro; IPR002634; BolA.
DR InterPro; IPR036065; BolA-like_sf.
DR PANTHER; PTHR12735; PTHR12735; 1.
DR Pfam; PF01722; BolA; 1.
DR PIRSF; PIRSF003113; BolA; 1.
DR SUPFAM; SSF82657; SSF82657; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Glutathionylation; Nucleus;
KW Reference proteome.
FT CHAIN 1..93
FT /note="Protein BOLA2"
FT /id="PRO_0000432128"
FT REGION 72..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="S-glutathionyl cysteine; transient; alternate"
FT /evidence="ECO:0000305|PubMed:24203231"
FT DISULFID 29
FT /note="Interchain; alternate"
FT /evidence="ECO:0000305|PubMed:24203231"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:4PUH"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:4PUH"
FT STRAND 26..38
FT /evidence="ECO:0007829|PDB:4PUH"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4PUH"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:4PUH"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:4PUH"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:4PUH"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:4PUH"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:4PUH"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:2MM9"
SQ SEQUENCE 93 AA; 10375 MW; EF2734E5BBCE0412 CRC64;
MVTKEQVEAS LTSKLKPIHL EVIDISGGCG SSFEVEVVSE QFEGKRLLER HRMVNAALEE
EMKEIHALSI KKAQTPQQWK PPSQDSATLT KDA
