ID VAL1_ARATH Reviewed; 790 AA.
AC Q8W4L5; O04346;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=B3 domain-containing transcription repressor VAL1;
DE AltName: Full=Protein HIGH-LEVEL EXPRESSION OF SUGAR-INDUCIBLE 2;
DE AltName: Full=Protein VP1/ABI3-LIKE 1;
GN Name=VAL1; Synonyms=HSI2; OrderedLocusNames=At2g30470; ORFNames=T6B20.17;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15894743; DOI=10.1104/pp.104.057752;
RA Tsukagoshi H., Saijo T., Shibata D., Morikami A., Nakamura K.;
RT "Analysis of a sugar response mutant of Arabidopsis identified a novel B3
RT domain protein that functions as an active transcriptional repressor.";
RL Plant Physiol. 138:675-685(2005).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=17158584; DOI=10.1104/pp.106.092320;
RA Suzuki M., Wang H.H.-Y., McCarty D.R.;
RT "Repression of the LEAFY COTYLEDON 1/B3 regulatory network in plant embryo
RT development by VP1/ABSCISIC ACID INSENSITIVE 3-LIKE B3 genes.";
RL Plant Physiol. 143:902-911(2007).
RN [6]
RP FUNCTION.
RX PubMed=17267611; DOI=10.1073/pnas.0607940104;
RA Tsukagoshi H., Morikami A., Nakamura K.;
RT "Two B3 domain transcriptional repressors prevent sugar-inducible
RT expression of seed maturation genes in Arabidopsis seedlings.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2543-2547(2007).
RN [7]
RP GENE FAMILY.
RX PubMed=18986826; DOI=10.1016/j.tplants.2008.09.006;
RA Swaminathan K., Peterson K., Jack T.;
RT "The plant B3 superfamily.";
RL Trends Plant Sci. 13:647-655(2008).
RN [8]
RP INTERACTION WITH SNL1.
RX PubMed=19962994; DOI=10.1016/j.jmb.2009.11.065;
RA Bowen A.J., Gonzalez D., Mullins J.G., Bhatt A.M., Martinez A.,
RA Conlan R.S.;
RT "PAH-domain-specific interactions of the Arabidopsis transcription
RT coregulator SIN3-LIKE1 (SNL1) with telomere-binding protein 1 and ALWAYS
RT EARLY2 Myb-DNA binding factors.";
RL J. Mol. Biol. 395:937-949(2010).
CC -!- FUNCTION: Transcriptional repressor of gene expression involved in
CC embryonic pathways, such as LEC1, ABI3, and FUS3. Repressor of the
CC sugar-inducible genes involved in the seed maturation program in
CC seedlings. Plays an essential role in regulating the transition from
CC seed maturation to seedling growth. Functionally redundant with
CC VAL2/HSL1. {ECO:0000269|PubMed:15894743, ECO:0000269|PubMed:17158584,
CC ECO:0000269|PubMed:17267611}.
CC -!- SUBUNIT: Interacts with SNL1. {ECO:0000269|PubMed:19962994}.
CC -!- INTERACTION:
CC Q8W4L5; Q84MC7: PYL9; NbExp=3; IntAct=EBI-2616403, EBI-2349513;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326,
CC ECO:0000269|PubMed:15894743}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers and at lower levels in roots,
CC stems and leaves. {ECO:0000269|PubMed:15894743}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63089.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB206553; BAD90970.1; -; mRNA.
DR EMBL; U93215; AAB63089.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08392.1; -; Genomic_DNA.
DR EMBL; AY062492; AAL32570.1; -; mRNA.
DR PIR; G84708; G84708.
DR RefSeq; NP_850146.1; NM_179815.3.
DR PDB; 5YUG; X-ray; 1.57 A; A/B/E/G=1-110.
DR PDB; 5YUH; X-ray; 1.80 A; A=1-110.
DR PDB; 5YZY; X-ray; 2.61 A; C=273-400.
DR PDB; 5YZZ; X-ray; 2.58 A; C=273-400.
DR PDB; 5Z00; X-ray; 2.59 A; C/G/K/M=273-400.
DR PDB; 6FAS; X-ray; 1.90 A; A/B=287-397.
DR PDB; 6J9A; X-ray; 2.92 A; A=273-403.
DR PDBsum; 5YUG; -.
DR PDBsum; 5YUH; -.
DR PDBsum; 5YZY; -.
DR PDBsum; 5YZZ; -.
DR PDBsum; 5Z00; -.
DR PDBsum; 6FAS; -.
DR PDBsum; 6J9A; -.
DR AlphaFoldDB; Q8W4L5; -.
DR SMR; Q8W4L5; -.
DR BioGRID; 2946; 9.
DR IntAct; Q8W4L5; 6.
DR MINT; Q8W4L5; -.
DR STRING; 3702.Q8W4L5; -.
DR iPTMnet; Q8W4L5; -.
DR PaxDb; 3702-AT2G30470-1; -.
DR ProteomicsDB; 243257; -.
DR EnsemblPlants; AT2G30470.1; AT2G30470.1; AT2G30470.
DR GeneID; 817597; -.
DR Gramene; AT2G30470.1; AT2G30470.1; AT2G30470.
DR KEGG; ath:AT2G30470; -.
DR Araport; AT2G30470; -.
DR TAIR; AT2G30470; HSI2.
DR eggNOG; ENOG502QWC1; Eukaryota.
DR HOGENOM; CLU_015907_0_0_1; -.
DR InParanoid; Q8W4L5; -.
DR OMA; GWRECRT; -.
DR OrthoDB; 933627at2759; -.
DR PhylomeDB; Q8W4L5; -.
DR PRO; PR:Q8W4L5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8W4L5; baseline and differential.
DR Genevisible; Q8W4L5; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; TAS:TAIR.
DR GO; GO:0009744; P:response to sucrose; TAS:TAIR.
DR CDD; cd10017; B3_DNA; 1.
DR Gene3D; 3.30.40.100; -; 1.
DR Gene3D; 2.40.330.10; DNA-binding pseudobarrel domain; 1.
DR InterPro; IPR003340; B3_DNA-bd.
DR InterPro; IPR015300; DNA-bd_pseudobarrel_sf.
DR InterPro; IPR011124; Znf_CW.
DR PANTHER; PTHR46245; B3 DOMAIN-CONTAINING PROTEIN OS07G0563300; 1.
DR PANTHER; PTHR46245:SF3; B3 DOMAIN-CONTAINING TRANSCRIPTION REPRESSOR VAL1; 1.
DR Pfam; PF02362; B3; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SMART; SM01019; B3; 1.
DR SUPFAM; SSF101936; DNA-binding pseudobarrel domain; 1.
DR PROSITE; PS50863; B3; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..790
FT /note="B3 domain-containing transcription repressor VAL1"
FT /id="PRO_0000375117"
FT DNA_BIND 295..396
FT /note="TF-B3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00326"
FT ZN_FING 538..588
FT /note="CW-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT REGION 234..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 685..732
FT /evidence="ECO:0000255"
FT COMPBIAS 234..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 580
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:5YUG"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:5YUG"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5YUG"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:5YUG"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:5YUG"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5YUG"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5YUG"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:5YUG"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:5YUG"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5YUG"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5YUG"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:5YUG"
FT STRAND 290..298
FT /evidence="ECO:0007829|PDB:6FAS"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:6FAS"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5YZY"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:6FAS"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:6FAS"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5YZZ"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:6FAS"
FT STRAND 341..351
FT /evidence="ECO:0007829|PDB:6FAS"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:6FAS"
FT HELIX 363..368
FT /evidence="ECO:0007829|PDB:6FAS"
FT STRAND 376..383
FT /evidence="ECO:0007829|PDB:6FAS"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:6FAS"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:6FAS"
SQ SEQUENCE 790 AA; 87002 MW; D81BDF8A40B3053C CRC64;
MFEVKMGSKM CMNASCGTTS TVEWKKGWPL RSGLLADLCY RCGSAYESSL FCEQFHKDQS
GWRECYLCSK RLHCGCIASK VTIELMDYGG VGCSTCACCH QLNLNTRGEN PGVFSRLPMK
TLADRQHVNG ESGGRNEGDL FSQPLVMGGD KREEFMPHRG FGKLMSPEST TTGHRLDAAG
EMHESSPLQP SLNMGLAVNP FSPSFATEAV EGMKHISPSQ SNMVHCSASN ILQKPSRPAI
STPPVASKSA QARIGRPPVE GRGRGHLLPR YWPKYTDKEV QQISGNLNLN IVPLFEKTLS
ASDAGRIGRL VLPKACAEAY FPPISQSEGI PLKIQDVRGR EWTFQFRYWP NNNSRMYVLE
GVTPCIQSMM LQAGDTVTFS RVDPGGKLIM GSRKAANAGD MQGCGLTNGT STEDTSSSGV
TENPPSINGS SCISLIPKEL NGMPENLNSE TNGGRIGDDP TRVKEKKRTR TIGAKNKRLL
LHSEESMELR LTWEEAQDLL RPSPSVKPTI VVIEEQEIEE YDEPPVFGKR TIVTTKPSGE
QERWATCDDC SKWRRLPVDA LLSFKWTCID NVWDVSRCSC SAPEESLKEL ENVLKVGREH
KKRRTGESQA AKSQQEPCGL DALASAAVLG DTIGEPEVAT TTRHPRHRAG CSCIVCIQPP
SGKGRHKPTC GCTVCSTVKR RFKTLMMRRK KKQLERDVTA AEDKKKKDME LAESDKSKEE
KEVNTARIDL NSDPYNKEDV EAVAVEKEES RKRAIGQCSG VVAQDASDVL GVTELEGEGK
NVREEPRVSS
//
