WDR26_ARATH
ID WDR26_ARATH Reviewed; 589 AA.
AC Q9FNN2;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=WD repeat-containing protein 26 homolog {ECO:0000305};
DE Short=AtWDR26 {ECO:0000303|PubMed:26706055};
GN Name=WDR26 {ECO:0000303|PubMed:26706055};
GN OrderedLocusNames=At5g08560 {ECO:0000312|Araport:AT5G08560};
GN ORFNames=MAH20.12 {ECO:0000312|EMBL:BAB10005.1};
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RANBPM, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22676313; DOI=10.1186/1471-2229-12-83;
RA Tomastikova E., Cenklova V., Kohoutova L., Petrovska B., Vachova L.,
RA Halada P., Kocarova G., Binarova P.;
RT "Interactions of an Arabidopsis RanBPM homologue with LisH-CTLH domain
RT proteins revealed high conservation of CTLH complexes in eukaryotes.";
RL BMC Plant Biol. 12:83-83(2012).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=26706055; DOI=10.1016/j.plantsci.2015.09.024;
RA Chuang H.W., Feng J.H., Feng Y.L., Wei M.J.;
RT "An Arabidopsis WDR protein coordinates cellular networks involved in
RT light, stress response and hormone signals.";
RL Plant Sci. 241:23-31(2015).
CC -!- FUNCTION: Acts as a component involved in the crosstalk regulation
CC between light, hormone and abiotic stress response.
CC {ECO:0000269|PubMed:26706055}.
CC -!- SUBUNIT: Interacts with RANBPM. {ECO:0000269|PubMed:26706055}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22676313}.
CC Note=Associates predominantly in the form of large cytoplasmic
CC complexes. {ECO:0000269|PubMed:22676313}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:26706055}.
CC -!- INDUCTION: Induced by auxin, abscisic acid (ABA), ethylene, mannitol
CC and salt stress. Down-regulated by dark. {ECO:0000269|PubMed:26706055}.
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DR EMBL; AB006697; BAB10005.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91320.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91321.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70934.1; -; Genomic_DNA.
DR EMBL; AY054535; AAK96726.1; -; mRNA.
DR EMBL; AY064639; AAL47352.1; -; mRNA.
DR RefSeq; NP_001078546.1; NM_001085077.1.
DR RefSeq; NP_001318513.1; NM_001343018.1.
DR RefSeq; NP_196473.1; NM_120942.3.
DR AlphaFoldDB; Q9FNN2; -.
DR SMR; Q9FNN2; -.
DR IntAct; Q9FNN2; 4.
DR STRING; 3702.AT5G08560.1; -.
DR iPTMnet; Q9FNN2; -.
DR PaxDb; Q9FNN2; -.
DR PRIDE; Q9FNN2; -.
DR ProteomicsDB; 242334; -.
DR EnsemblPlants; AT5G08560.1; AT5G08560.1; AT5G08560.
DR EnsemblPlants; AT5G08560.2; AT5G08560.2; AT5G08560.
DR EnsemblPlants; AT5G08560.3; AT5G08560.3; AT5G08560.
DR GeneID; 830756; -.
DR Gramene; AT5G08560.1; AT5G08560.1; AT5G08560.
DR Gramene; AT5G08560.2; AT5G08560.2; AT5G08560.
DR Gramene; AT5G08560.3; AT5G08560.3; AT5G08560.
DR KEGG; ath:AT5G08560; -.
DR Araport; AT5G08560; -.
DR TAIR; locus:2159562; AT5G08560.
DR eggNOG; KOG0293; Eukaryota.
DR HOGENOM; CLU_000288_57_25_1; -.
DR InParanoid; Q9FNN2; -.
DR OMA; QRDSCVF; -.
DR OrthoDB; 349428at2759; -.
DR PhylomeDB; Q9FNN2; -.
DR PRO; PR:Q9FNN2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNN2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0010150; P:leaf senescence; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009646; P:response to absence of light; IDA:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009723; P:response to ethylene; IMP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..589
FT /note="WD repeat-containing protein 26 homolog"
FT /id="PRO_0000442058"
FT DOMAIN 64..96
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 97..154
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REPEAT 272..311
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 317..358
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 360..398
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 401..440
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 442..480
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 484..526
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 529..569
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 589 AA; 65830 MW; DA4A46CFCA066184 CRC64;
MGVVEDTEPP LKRAKRLADE PNGFSANSSV RGSSVNSNSL GDLMARPLPS QGDDETIGSK
GVIRKSEFVR IITRALYSLG YDKTGAMLEE ESGISLHNST IKLFLQQVKD GKWDQSVKTL
HRIGFPDEKA VKAASFLLLE QKFLEFLKVE KIADALRTLR NEMAPLRINT KRVHELASSL
ISPSSFISHT TSTPGKESVN SRSKVLEELQ TLLPASVIIP EKRLECLVEN SLHIQRDSCV
FHNTLDSDLS LYSDHQCGKH QIPSQTAQIL ESHTDEVWFL QFSHNGKYLA SSSKDQTAII
WEISADGHIS LKHTLVGHHK PVIAILWSPD DRQVLTCGAE EVIRRWDVDS GDCVHMYEKG
GISPISCGWY PDGQGIIAGM TDRSICMWDL DGREKECWKG QRTQKVSDIA MTDDGKWLVS
VCKDSVISLF DREATVERLI EEEDMITSFS LSNDNKYILV NLLNQEIRLW NIEGDPKIVS
RYKGHKRSRF IIRSCFGGYK QAFIASGSED SQVYIWHRST GKLIVELPGH AGAVNCVSWS
PTNLHMLASA SDDGTIRIWG LDRINQQNQK KKLVQGSSSN GVIHRCNGN
