AKR2B_ARATH
ID AKR2B_ARATH Reviewed; 344 AA.
AC Q29Q26;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Ankyrin repeat domain-containing protein 2B {ECO:0000303|PubMed:20215589};
GN Name=AKR2B {ECO:0000303|PubMed:20215589};
GN OrderedLocusNames=At2g17390 {ECO:0000312|EMBL:AEC06620.1};
GN ORFNames=F5J6.15 {ECO:0000305};
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|EMBL:ABD59068.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH APX3; APX5 AND TOC34.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=20215589; DOI=10.1105/tpc.109.065979;
RA Shen G., Kuppu S., Venkataramani S., Wang J., Yan J., Qiu X., Zhang H.;
RT "ANKYRIN REPEAT-CONTAINING PROTEIN 2A is an essential molecular chaperone
RT for peroxisomal membrane-bound ASCORBATE PEROXIDASE3 in Arabidopsis.";
RL Plant Cell 22:811-831(2010).
CC -!- FUNCTION: Exhibits chaperone activity toward chloroplast outer envelope
CC membrane, mitochondrion outer membrane, endoplasmic reticulum membrane
CC and peroxisomal proteins, by recruiting specific proteins containing a
CC single transmembrane associated with an AKR2A-binding sequence (ABS)
CC and subsequently binding glycolipids (e.g. monogalactosyldiacylglycerol
CC (MGDG) and phosphatidylglycerol (PG)) present in the membrane of the
CC target organelle. {ECO:0000250|UniProtKB:Q9SAR5}.
CC -!- SUBUNIT: Binds to chloroplast outer envelope membrane (OEM) protein
CC targeting signals, as well as to chloroplasts. Binds specifically to
CC two chloroplast glycolipids, monogalactosyldiacylglycerol (MGDG) and
CC phosphatidylglycerol (PG) (By similarity). Interacts with APX3, APX5
CC and TOC34 (PubMed:20215589). {ECO:0000250|UniProtKB:Q9SAR5,
CC ECO:0000269|PubMed:20215589}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9SAR5}. Nucleus
CC {ECO:0000250|UniProtKB:Q9SAR5}. Plastid, chloroplast outer membrane
CC {ECO:0000250|UniProtKB:Q9SAR5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9SAR5}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9SAR5}.
CC -!- DOMAIN: The ankyrin repeats (ANK) mediate interactions with hexoses-
CC containing lipids present in organellar membranes (e.g. chloroplast),
CC such as monogalactosyldiacylglycerol (MGDG) and phosphatidylglycerol
CC (PG). {ECO:0000250|UniProtKB:Q9SAR5}.
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DR EMBL; CP002685; AEC06620.1; -; Genomic_DNA.
DR EMBL; BT024730; ABD59068.1; -; mRNA.
DR PIR; F84551; F84551.
DR RefSeq; NP_179331.1; NM_127294.5.
DR AlphaFoldDB; Q29Q26; -.
DR SMR; Q29Q26; -.
DR IntAct; Q29Q26; 1.
DR STRING; 3702.AT2G17390.1; -.
DR iPTMnet; Q29Q26; -.
DR MetOSite; Q29Q26; -.
DR PaxDb; Q29Q26; -.
DR PRIDE; Q29Q26; -.
DR ProteomicsDB; 244866; -.
DR EnsemblPlants; AT2G17390.1; AT2G17390.1; AT2G17390.
DR GeneID; 816246; -.
DR Gramene; AT2G17390.1; AT2G17390.1; AT2G17390.
DR KEGG; ath:AT2G17390; -.
DR Araport; AT2G17390; -.
DR TAIR; locus:2827572; AT2G17390.
DR eggNOG; KOG0504; Eukaryota.
DR HOGENOM; CLU_057418_1_0_1; -.
DR InParanoid; Q29Q26; -.
DR OMA; SGNIHRT; -.
DR OrthoDB; 1351793at2759; -.
DR PhylomeDB; Q29Q26; -.
DR PRO; PR:Q29Q26; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q29Q26; baseline and differential.
DR Genevisible; Q29Q26; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0031359; C:integral component of chloroplast outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030941; F:chloroplast targeting sequence binding; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0045036; P:protein targeting to chloroplast; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR041243; STI1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF17830; STI1; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW ANK repeat; Chaperone; Chloroplast; Cytoplasm; Lipid-binding; Membrane;
KW Nucleus; Plastid; Plastid outer membrane; Reference proteome; Repeat.
FT CHAIN 1..344
FT /note="Ankyrin repeat domain-containing protein 2B"
FT /id="PRO_0000434613"
FT REPEAT 219..248
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 252..281
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 285..314
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 318..344
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 225
FT /ligand="a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:17615"
FT /evidence="ECO:0000250|UniProtKB:Q9SAR5"
FT BINDING 248
FT /ligand="a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol"
FT /ligand_id="ChEBI:CHEBI:17615"
FT /evidence="ECO:0000250|UniProtKB:Q9SAR5"
FT BINDING 296
FT /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT /ligand_id="ChEBI:CHEBI:64716"
FT /evidence="ECO:0000250|UniProtKB:Q9SAR5"
FT BINDING 298
FT /ligand="1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)"
FT /ligand_id="ChEBI:CHEBI:64716"
FT /evidence="ECO:0000250|UniProtKB:Q9SAR5"
SQ SEQUENCE 344 AA; 36899 MW; A130E0AEC4DF206E CRC64;
MASSSEKTPL IPSDEKNDTK EESKSTTKPE SGSGAPPSPS PTDPGLDFNA FDFSGMAGIL
NDPSIKELAE QIAKDPSFNQ LAEQLQRSVP TGSHEGGLPN FDPQQYMQTM QQVMENPEFR
TMAERLGNAL VQDPQMSPFL EALGNPAASE QFAERMAQMK EDPELKPILA EIDAGGPSAM
MKYWNDKDVL AKLGEAMGIA VGADQTVAAE PEEAEEGEEE ESIVHQTASL GDVEGLKAAL
ASGGNKDEED SEGRTALHFA CGYGEVRCAQ VLLDAGANAN AIDKNKNTPL HYAAGYGRKE
CVSLLLENGA AVTQQNMDNK NPIDVARLNN QLDVVKLLEK DAFL
