LUH_ARATH
ID LUH_ARATH Reviewed; 787 AA.
AC O48847; F4ITU4; F4ITV0; Q0WWP4; Q3EBQ0;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Transcriptional corepressor LEUNIG_HOMOLOG;
DE AltName: Full=Protein MUCILAGE-MODIFIED 1 {ECO:0000303|PubMed:11706181};
GN Name=LUH {ECO:0000312|EMBL:AEC08720.1};
GN Synonyms=MUM1 {ECO:0000303|PubMed:11706181};
GN OrderedLocusNames=At2g32700 {ECO:0000312|Araport:AT2G32700};
GN ORFNames=F24L7.16 {ECO:0000312|EMBL:AAC04493.1};
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=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] (ISOFORM 1).
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] OF 544-787 (ISOFORM 1/2/3).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11706181; DOI=10.1104/pp.010410;
RA Western T.L., Burn J., Tan W.L., Skinner D.J., Martin-McCaffrey L.,
RA Moffatt B.A., Haughn G.W.;
RT "Isolation and characterization of mutants defective in seed coat mucilage
RT secretory cell development in Arabidopsis.";
RL Plant Physiol. 127:998-1011(2001).
RN [6]
RP ALTERNATIVE SPLICING.
RX PubMed=14500829; DOI=10.1093/nar/gkg770;
RA Haas B.J., Delcher A.L., Mount S.M., Wortman J.R., Smith R.K. Jr.,
RA Hannick L.I., Maiti R., Ronning C.M., Rusch D.B., Town C.D., Salzberg S.L.,
RA White O.;
RT "Improving the Arabidopsis genome annotation using maximal transcript
RT alignment assemblies.";
RL Nucleic Acids Res. 31:5654-5666(2003).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-123, INTERACTION WITH
RP SEU, TISSUE SPECIFICITY, AND INDUCTION BY BIOTIC AND ABIOTIC STRESSES.
RX PubMed=18390806; DOI=10.1104/pp.108.115923;
RA Sitaraman J., Bui M., Liu Z.;
RT "LEUNIG_HOMOLOG and LEUNIG perform partially redundant functions during
RT Arabidopsis embryo and floral development.";
RL Plant Physiol. 147:672-681(2008).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH YAB3; YAB5 AND YAB1/FIL,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=19837869; DOI=10.1105/tpc.109.070458;
RA Stahle M.I., Kuehlich J., Staron L., von Arnim A.G., Golz J.F.;
RT "YABBYs and the transcriptional corepressors LEUNIG and LEUNIG_HOMOLOG
RT maintain leaf polarity and meristem activity in Arabidopsis.";
RL Plant Cell 21:3105-3118(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=21362134; DOI=10.1111/j.1744-7909.2011.01036.x;
RA Bui M., Lim N., Sijacic P., Liu Z.;
RT "LEUNIG_HOMOLOG and LEUNIG regulate seed mucilage extrusion in
RT Arabidopsis.";
RL J. Integr. Plant Biol. 53:399-408(2011).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21402796; DOI=10.1104/pp.111.172692;
RA Walker M., Tehseen M., Doblin M.S., Pettolino F.A., Wilson S.M., Bacic A.,
RA Golz J.F.;
RT "The transcriptional regulator LEUNIG_HOMOLOG regulates mucilage release
RT from the Arabidopsis testa.";
RL Plant Physiol. 156:46-60(2011).
RN [12]
RP SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=cv. Col-2, and cv. Landsberg erecta;
RX PubMed=21518777; DOI=10.1104/pp.111.172023;
RA Huang J., DeBowles D., Esfandiari E., Dean G., Carpita N.C., Haughn G.W.;
RT "The Arabidopsis transcription factor LUH/MUM1 is required for extrusion of
RT seed coat mucilage.";
RL Plant Physiol. 156:491-502(2011).
RN [13]
RP FUNCTION IN ABIOTIC STRESSES, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP SLK1 AND SLK2.
RX PubMed=24564815; DOI=10.1186/1471-2229-14-54;
RA Shrestha B., Guragain B., Sridhar V.V.;
RT "Involvement of co-repressor LUH and the adapter proteins SLK1 and SLK2 in
RT the regulation of abiotic stress response genes in Arabidopsis.";
RL BMC Plant Biol. 14:54-54(2014).
RN [14]
RP REVIEW ON MUCILAGE EXTRUSION.
RX PubMed=25658798; DOI=10.3390/ijms16023452;
RA Voiniciuc C., Yang B., Schmidt M.H.-W., Guenl M., Usadel B.;
RT "Starting to gel: how Arabidopsis seed coat epidermal cells produce
RT specialized secondary cell walls.";
RL Int. J. Mol. Sci. 16:3452-3473(2015).
CC -!- FUNCTION: Transcription repressor subunit of the SEU-SLK1 and SEU-SLK2
CC transcriptional corepressor of abiotic stress (e.g. salt and osmotic
CC stress) response genes, by means of an epigenetic process involving
CC histone modification (e.g. H3K9 and H3K14 acetylation), probably by
CC recruiting HDAC, to facilitate the condensation of chromatin thus
CC preventing transcription at the target genes (PubMed:24564815). Can
CC also act as a transcription activator (PubMed:21518777). Implicated in
CC embryo and floral development (PubMed:18390806). Involved in post-
CC synthesis cell wall modifications necessary for mucilage extrusion from
CC seeds upon imbibition, probably by promoting the expression of genes
CC required for mucilage maturation (e.g. MUM2) (PubMed:11706181,
CC PubMed:21362134, PubMed:21402796, PubMed:21518777). Regulates the
CC maintenance on leaf polarity and meristem activity as well as the
CC initiation of embryonic shoot apical meristem (SAM) development
CC (PubMed:19837869). {ECO:0000269|PubMed:11706181,
CC ECO:0000269|PubMed:18390806, ECO:0000269|PubMed:19837869,
CC ECO:0000269|PubMed:21362134, ECO:0000269|PubMed:21402796,
CC ECO:0000269|PubMed:21518777, ECO:0000269|PubMed:24564815}.
CC -!- SUBUNIT: Forms corepressor complexes with SLK1 and SLK2; LUH is the
CC transcription repressor subunit and SLK1 and SLK2 the specific DNA-
CC binding adapters (PubMed:24564815). Interacts with SEU
CC (PubMed:18390806). Binds to YAB3, YAB5 and YAB1/FIL; these complexes
CC promote adaxial cell identity in leaves as well as embryonic shoot
CC apical meristem (SAM) initiation and postembryonic SAM maintenance
CC (PubMed:19837869). {ECO:0000269|PubMed:18390806,
CC ECO:0000269|PubMed:19837869, ECO:0000269|PubMed:24564815}.
CC -!- INTERACTION:
CC O48847; Q8H102: BHLH128; NbExp=4; IntAct=EBI-3387563, EBI-3387023;
CC O48847; Q9C8Y3: RGL1; NbExp=3; IntAct=EBI-3387563, EBI-963647;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21518777}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O48847-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O48847-2; Sequence=VSP_057680;
CC Name=3;
CC IsoId=O48847-3; Sequence=VSP_057681;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, seedlings, apex,
CC flowers, siliques, flower organs and seeds (including seed coat).
CC {ECO:0000269|PubMed:18390806, ECO:0000269|PubMed:21518777}.
CC -!- DEVELOPMENTAL STAGE: Accumulates throughout young developing leaves,
CC before being confined to the vasculature of older leaves
CC (PubMed:19837869). Expressed during seed coat development, reaching
CC peak expression late in differentiation at 10 days post anthesis (DPA)
CC (PubMed:21518777). {ECO:0000269|PubMed:19837869,
CC ECO:0000269|PubMed:21518777}.
CC -!- INDUCTION: Induced by exposures to biotic stress (e.g. nematode and
CC Botrytis cinerea) and abiotic stress (e.g. salt, genotoxic, wounding,
CC drought and oxidative stress). Repressed by exposures to biotic stress
CC (e.g. Agrobacterium tumefaciens) and abiotic stress (e.g. hypoxia,
CC cycloheximide, 2,4-dichlorophenoxyacetic acid, AgNO(3) and
CC aminoethoxyvinylglycine). {ECO:0000269|PubMed:18390806}.
CC -!- DISRUPTION PHENOTYPE: Strong defects in seed mucilage extrusion; no
CC mucilage capsule formation and slightly irregular columellae in seeds.
CC Altered structure of mucilage that accumulates abnormal levels of
CC substituted rhamnogalacturonan I and methyl-esterified
CC homogalacturonan. Increased amount of most sugars associated with an
CC increase in methylation of the mucilage and/or primary cell wall
CC pectins (PubMed:11706181, PubMed:21362134, PubMed:21402796,
CC PubMed:21518777). Reduced MUM2 expression in seed coat and embryo.
CC Shorter roots (PubMed:21402796). Enhanced tolerance to salt and osmotic
CC stress conditions (PubMed:24564815). In plants lacking both LUG and
CC LUH, embryo lethality and abnormal flowers (PubMed:18390806). Enhance
CC the polarity and growth defects of luh/+ lug mutant leaves, being
CC partially abaxialized (PubMed:19837869). {ECO:0000269|PubMed:11706181,
CC ECO:0000269|PubMed:18390806, ECO:0000269|PubMed:19837869,
CC ECO:0000269|PubMed:21362134, ECO:0000269|PubMed:21402796,
CC ECO:0000269|PubMed:21518777, ECO:0000269|PubMed:24564815}.
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DR EMBL; AC003974; AAC04493.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08720.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08721.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08722.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08723.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08724.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08725.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08726.1; -; Genomic_DNA.
DR EMBL; AF367306; AAK32893.1; -; mRNA.
DR EMBL; BT002219; AAN72230.1; -; mRNA.
DR EMBL; AK226299; BAE98454.1; -; mRNA.
DR PIR; T00798; T00798.
DR RefSeq; NP_001031466.2; NM_001036389.4. [O48847-3]
DR RefSeq; NP_001189659.1; NM_001202730.1. [O48847-2]
DR RefSeq; NP_565749.1; NM_128829.4. [O48847-1]
DR RefSeq; NP_850192.1; NM_179861.3. [O48847-1]
DR RefSeq; NP_850193.1; NM_179862.2. [O48847-1]
DR RefSeq; NP_850194.1; NM_179863.3. [O48847-1]
DR RefSeq; NP_850195.2; NM_179864.3. [O48847-1]
DR AlphaFoldDB; O48847; -.
DR SMR; O48847; -.
DR IntAct; O48847; 11.
DR STRING; 3702.AT2G32700.7; -.
DR iPTMnet; O48847; -.
DR PaxDb; O48847; -.
DR PRIDE; O48847; -.
DR ProteomicsDB; 238742; -. [O48847-1]
DR EnsemblPlants; AT2G32700.1; AT2G32700.1; AT2G32700. [O48847-1]
DR EnsemblPlants; AT2G32700.2; AT2G32700.2; AT2G32700. [O48847-1]
DR EnsemblPlants; AT2G32700.3; AT2G32700.3; AT2G32700. [O48847-1]
DR EnsemblPlants; AT2G32700.4; AT2G32700.4; AT2G32700. [O48847-1]
DR EnsemblPlants; AT2G32700.5; AT2G32700.5; AT2G32700. [O48847-1]
DR EnsemblPlants; AT2G32700.6; AT2G32700.6; AT2G32700. [O48847-3]
DR EnsemblPlants; AT2G32700.7; AT2G32700.7; AT2G32700. [O48847-2]
DR GeneID; 817830; -.
DR Gramene; AT2G32700.1; AT2G32700.1; AT2G32700. [O48847-1]
DR Gramene; AT2G32700.2; AT2G32700.2; AT2G32700. [O48847-1]
DR Gramene; AT2G32700.3; AT2G32700.3; AT2G32700. [O48847-1]
DR Gramene; AT2G32700.4; AT2G32700.4; AT2G32700. [O48847-1]
DR Gramene; AT2G32700.5; AT2G32700.5; AT2G32700. [O48847-1]
DR Gramene; AT2G32700.6; AT2G32700.6; AT2G32700. [O48847-3]
DR Gramene; AT2G32700.7; AT2G32700.7; AT2G32700. [O48847-2]
DR KEGG; ath:AT2G32700; -.
DR Araport; AT2G32700; -.
DR TAIR; locus:2046437; AT2G32700.
DR eggNOG; KOG0266; Eukaryota.
DR OMA; ETMVAIF; -.
DR OrthoDB; 222806at2759; -.
DR PhylomeDB; O48847; -.
DR PRO; PR:O48847; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O48847; baseline and differential.
DR Genevisible; O48847; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:TAIR.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
DR GO; GO:0071217; P:cellular response to external biotic stimulus; IDA:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0009908; P:flower development; IGI:TAIR.
DR GO; GO:0010393; P:galacturonan metabolic process; IMP:UniProtKB.
DR GO; GO:0010073; P:meristem maintenance; IMP:UniProtKB.
DR GO; GO:0010192; P:mucilage biosynthetic process; IMP:UniProtKB.
DR GO; GO:0080001; P:mucilage extrusion from seed coat; IMP:UniProtKB.
DR GO; GO:0048359; P:mucilage metabolic process involved in seed coat development; IMP:UniProtKB.
DR GO; GO:0048358; P:mucilage pectin biosynthetic process; IMP:TAIR.
DR GO; GO:1901001; P:negative regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0009827; P:plant-type cell wall modification; IMP:UniProtKB.
DR GO; GO:0009944; P:polarity specification of adaxial/abaxial axis; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1902066; P:regulation of cell wall pectin metabolic process; IMP:TAIR.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IMP:UniProtKB.
DR GO; GO:2000024; P:regulation of leaf development; IMP:UniProtKB.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IMP:UniProtKB.
DR GO; GO:1902183; P:regulation of shoot apical meristem development; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0010044; P:response to aluminum ion; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0046898; P:response to cycloheximide; IEP:UniProtKB.
DR GO; GO:0009620; P:response to fungus; IEP:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEP:UniProtKB.
DR GO; GO:0009624; P:response to nematode; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0010272; P:response to silver ion; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR044716; LEUNIG-like.
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 PANTHER; PTHR44376; PTHR44376; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Developmental protein;
KW Differentiation; Flowering; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; WD repeat.
FT CHAIN 1..787
FT /note="Transcriptional corepressor LEUNIG_HOMOLOG"
FT /id="PRO_0000433165"
FT DOMAIN 8..40
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REPEAT 508..547
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 550..589
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 593..633
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 635..671
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 675..715
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 717..755
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 757..787
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 1..88
FT /note="Required for SEU-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9FUY2"
FT REGION 299..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 77..106
FT /evidence="ECO:0000255"
FT COMPBIAS 323..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 237
FT /note="A -> AGKYINVLHCRVIAHRKENG (in isoform 2)"
FT /id="VSP_057680"
FT VAR_SEQ 449..450
FT /note="Missing (in isoform 3)"
FT /id="VSP_057681"
FT MUTAGEN 123
FT /note="S->F: In luh-2;."
FT /evidence="ECO:0000269|PubMed:18390806"
SQ SEQUENCE 787 AA; 85515 MW; 995B52584090CEC3 CRC64;
MAQSNWEADK MLDVYIYDYL VKKKLHNTAK SFMTEGKVSP DPVAIDAPGG FLFEWWSVFW
DIFIARTNEK HSEAAAAYIE AQQGKAKEQQ MQIQQLQMMR QAQMQRRDPN HPSLGGPMNA
IGSEGMIGQS NASALAAKMY EERMKQPNPM NSETSQPHLD ARMALLKSAT NHHGQIVQGN
HQGGVSAALQ QIQSRTQQPT EIKTEVNLGT SPRQLPVDPS TVYGQGILQS KPGMGSAGLN
PGVSGLPLKG WPLTGIEQMR PGLGGPQVQK SFLQNQSQFQ LSPQQQQHQM LAQVQAQGNM
TNSPMYGGDM DPRRFTGLPR GNLNPKDGQQ NANDGSIGSP MQSSSSKHIS MPPVQQSSSQ
QQDHLLSQQS QQNNRKRKGP SSSGPANSTG TGNTVGPSNS QPSTPSTHTP VDGVAIAGNM
HHVNSMPKGP MMYGSDGIGG LASSANQLLQ DDMDQFGDVG ALEDNVESFL SQDDGDGGSL
FGTLKRNSSV HTETSKPFSF NEVSCIRKSA SKVICCSFSY DGKLLASAGH DKKVFIWNME
TLQVESTPEE HAHIITDVRF RPNSTQLATS SFDKTIKIWD ASDPGYFLRT ISGHAAPVMS
IDFHPKKTEL LCSCDSNNDI RFWDINASCV RAVKGASTQV RFQPRTGQFL AAASENTVSI
FDIENNNKRV NIFKGHSSNV HSVCWSPNGE LVASVSEDAV KLWSLSSGDC IHELSNSGNK
FHSVVFHPSY PDLLVIGGYQ AIELWNTMEN KCMTVAGHEC VISALAQSPS TGVVASASHD
KSVKIWK
