VAL2_ARATH
ID VAL2_ARATH Reviewed; 780 AA.
AC Q5CCK4; O49390; Q0WSC1;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=B3 domain-containing transcription repressor VAL2;
DE AltName: Full=Protein HIGH-LEVEL EXPRESSION OF SUGAR-INDUCIBLE-LIKE 1;
DE AltName: Full=Protein VP1/ABI3-LIKE 2;
GN Name=VAL2; Synonyms=HSL1; OrderedLocusNames=At4g32010; ORFNames=F10N7.180;
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] (ISOFORM 1).
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] (ISOFORM 2).
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.
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).
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 VAL1/HSI2. {ECO:0000269|PubMed:17158584, ECO:0000269|PubMed:17267611}.
CC -!- INTERACTION:
CC Q5CCK4; Q9S7Z2: AFP4; NbExp=3; IntAct=EBI-15193683, EBI-1778843;
CC Q5CCK4; Q9FLI3: AHG1; NbExp=5; IntAct=EBI-15193683, EBI-2363348;
CC Q5CCK4; Q9SAZ5: AHP3; NbExp=3; IntAct=EBI-15193683, EBI-1100711;
CC Q5CCK4; Q9LNW3: AIP1; NbExp=3; IntAct=EBI-15193683, EBI-1573499;
CC Q5CCK4; Q9STS3: APC8; NbExp=3; IntAct=EBI-15193683, EBI-2130714;
CC Q5CCK4; Q9C5W9: ARF18; NbExp=8; IntAct=EBI-15193683, EBI-3946783;
CC Q5CCK4; Q29PY0: At1g01225; NbExp=3; IntAct=EBI-15193683, EBI-25517779;
CC Q5CCK4; Q8GZ67: At1g68160/T22E19_21; NbExp=3; IntAct=EBI-15193683, EBI-25518084;
CC Q5CCK4; Q9SAG6: At1g80940; NbExp=3; IntAct=EBI-15193683, EBI-25517938;
CC Q5CCK4; Q9LS47: At3g18430; NbExp=3; IntAct=EBI-15193683, EBI-25517954;
CC Q5CCK4; A0A384L7B9: At3g62550; NbExp=3; IntAct=EBI-15193683, EBI-25517258;
CC Q5CCK4; F4JJA3: At4g09060; NbExp=3; IntAct=EBI-15193683, EBI-25517233;
CC Q5CCK4; A0A178V4E1: At4g33925; NbExp=3; IntAct=EBI-15193683, EBI-25517714;
CC Q5CCK4; Q6NNP0: ATG16; NbExp=3; IntAct=EBI-15193683, EBI-25517622;
CC Q5CCK4; A0A384KYS8: AXX17_At3g42630; NbExp=3; IntAct=EBI-15193683, EBI-25517043;
CC Q5CCK4; A0A178UVG5: AXX17_At4g41180; NbExp=3; IntAct=EBI-15193683, EBI-25517978;
CC Q5CCK4; A0A178UNB2: AXX17_At5g54780; NbExp=3; IntAct=EBI-15193683, EBI-25517652;
CC Q5CCK4; Q9SJ56: BLH1; NbExp=3; IntAct=EBI-15193683, EBI-1148379;
CC Q5CCK4; Q8L5U0: CSN4; NbExp=3; IntAct=EBI-15193683, EBI-531074;
CC Q5CCK4; Q9C968: CYCA2-4; NbExp=3; IntAct=EBI-15193683, EBI-25518099;
CC Q5CCK4; Q94AY3: DRIP2; NbExp=3; IntAct=EBI-15193683, EBI-1787347;
CC Q5CCK4; Q9SKK0: EBF1; NbExp=3; IntAct=EBI-15193683, EBI-401198;
CC Q5CCK4; Q9MAI5: ERF8; NbExp=3; IntAct=EBI-15193683, EBI-2000137;
CC Q5CCK4; Q9FN91: EXO70H7; NbExp=3; IntAct=EBI-15193683, EBI-25516131;
CC Q5CCK4; P16972: FD2; NbExp=3; IntAct=EBI-15193683, EBI-449431;
CC Q5CCK4; O23624: FPF1; NbExp=3; IntAct=EBI-15193683, EBI-4476833;
CC Q5CCK4; O49653: GCP2; NbExp=3; IntAct=EBI-15193683, EBI-4458381;
CC Q5CCK4; P46639: KNAT1; NbExp=3; IntAct=EBI-15193683, EBI-530486;
CC Q5CCK4; Q9FIR9: LSU2; NbExp=3; IntAct=EBI-15193683, EBI-4424076;
CC Q5CCK4; Q9M0V0: MFDX1; NbExp=3; IntAct=EBI-15193683, EBI-25517302;
CC Q5CCK4; Q9FMI5: MHJ24.13; NbExp=3; IntAct=EBI-15193683, EBI-25518065;
CC Q5CCK4; Q9FFJ9: MJJ3.20; NbExp=3; IntAct=EBI-15193683, EBI-15211238;
CC Q5CCK4; Q9LPQ3: MKK7; NbExp=5; IntAct=EBI-15193683, EBI-2128593;
CC Q5CCK4; Q9FJ98: NRPB6A; NbExp=3; IntAct=EBI-15193683, EBI-25517907;
CC Q5CCK4; O22229: NTRC; NbExp=3; IntAct=EBI-15193683, EBI-4427818;
CC Q5CCK4; Q9XF57: PEX7; NbExp=3; IntAct=EBI-15193683, EBI-9536794;
CC Q5CCK4; Q1H5E9: PRDA1; NbExp=3; IntAct=EBI-15193683, EBI-1998055;
CC Q5CCK4; Q9XI19: PTAC6; NbExp=3; IntAct=EBI-15193683, EBI-7890412;
CC Q5CCK4; Q84L33: RAD23B; NbExp=3; IntAct=EBI-15193683, EBI-20557876;
CC Q5CCK4; Q93ZX1: RFC4; NbExp=3; IntAct=EBI-15193683, EBI-4470690;
CC Q5CCK4; Q9LF53: RGL3; NbExp=3; IntAct=EBI-15193683, EBI-15681313;
CC Q5CCK4; A8MRK9: RPC14; NbExp=3; IntAct=EBI-15193683, EBI-25518040;
CC Q5CCK4; Q9FHZ1: SCL23; NbExp=5; IntAct=EBI-15193683, EBI-1238460;
CC Q5CCK4; Q9FLP5: SUMO3; NbExp=3; IntAct=EBI-15193683, EBI-25512645;
CC Q5CCK4; A0ME58; NbExp=3; IntAct=EBI-15193683, EBI-25518134;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5CCK4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5CCK4-2; Sequence=VSP_037329;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16588.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79919.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB206554; BAD90971.1; -; mRNA.
DR EMBL; AL021636; CAA16588.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161580; CAB79919.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85993.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67961.1; -; Genomic_DNA.
DR EMBL; AK228013; BAE99977.1; -; mRNA.
DR PIR; T04644; T04644.
DR RefSeq; NP_001329752.1; NM_001342124.1. [Q5CCK4-2]
DR RefSeq; NP_194929.2; NM_119353.4. [Q5CCK4-1]
DR PDB; 5Z28; X-ray; 2.25 A; A/B=4-105.
DR PDBsum; 5Z28; -.
DR AlphaFoldDB; Q5CCK4; -.
DR SMR; Q5CCK4; -.
DR BioGRID; 14618; 55.
DR IntAct; Q5CCK4; 54.
DR STRING; 3702.AT4G32010.1; -.
DR PaxDb; Q5CCK4; -.
DR PRIDE; Q5CCK4; -.
DR ProteomicsDB; 242309; -. [Q5CCK4-1]
DR EnsemblPlants; AT4G32010.1; AT4G32010.1; AT4G32010. [Q5CCK4-1]
DR EnsemblPlants; AT4G32010.2; AT4G32010.2; AT4G32010. [Q5CCK4-2]
DR GeneID; 829332; -.
DR Gramene; AT4G32010.1; AT4G32010.1; AT4G32010. [Q5CCK4-1]
DR Gramene; AT4G32010.2; AT4G32010.2; AT4G32010. [Q5CCK4-2]
DR KEGG; ath:AT4G32010; -.
DR Araport; AT4G32010; -.
DR TAIR; locus:2116592; AT4G32010.
DR eggNOG; ENOG502S8EJ; Eukaryota.
DR HOGENOM; CLU_015907_0_0_1; -.
DR InParanoid; Q5CCK4; -.
DR OMA; ADANKGH; -.
DR OrthoDB; 186755at2759; -.
DR PhylomeDB; Q5CCK4; -.
DR PRO; PR:Q5CCK4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5CCK4; baseline and differential.
DR Genevisible; Q5CCK4; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR CDD; cd10017; B3_DNA; 1.
DR Gene3D; 2.40.330.10; -; 1.
DR InterPro; IPR003340; B3_DNA-bd.
DR InterPro; IPR015300; DNA-bd_pseudobarrel_sf.
DR InterPro; IPR011124; Znf_CW.
DR Pfam; PF02362; B3; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SMART; SM01019; B3; 1.
DR SUPFAM; SSF101936; SSF101936; 1.
DR PROSITE; PS50863; B3; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..780
FT /note="B3 domain-containing transcription repressor VAL2"
FT /id="PRO_0000375118"
FT DNA_BIND 286..387
FT /note="TF-B3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00326"
FT ZN_FING 515..565
FT /note="CW-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT REGION 577..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 524
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 545
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT VAR_SEQ 273..277
FT /note="QYPHL -> H (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_037329"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:5Z28"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:5Z28"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:5Z28"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:5Z28"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:5Z28"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:5Z28"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:5Z28"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5Z28"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:5Z28"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5Z28"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5Z28"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:5Z28"
SQ SEQUENCE 780 AA; 86012 MW; 6CA5BC9A178E2B72 CRC64;
MESIKVCMNA LCGAASTSGE WKKGWPMRSG DLASLCDKCG CAYEQSIFCE VFHAKESGWR
ECNSCDKRLH CGCIASRFMM ELLENGGVTC ISCAKKSGLI SMNVSHESNG KDFPSFASAE
HVGSVLERTN LKHLLHFQRI DPTHSSLQMK QEESLLPSSL DALRHKTERK ELSAQPNLSI
SLGPTLMTSP FHDAAVDDRS KTNSIFQLAP RSRQLLPKPA NSAPIAAGME PSGSLVSQIH
VARPPPEGRG KTQLLPRYWP RITDQELLQL SGQYPHLSNS KIIPLFEKVL SASDAGRIGR
LVLPKACAEA YFPPISLPEG LPLKIQDIKG KEWVFQFRFW PNNNSRMYVL EGVTPCIQSM
QLQAGDTVTF SRTEPEGKLV MGYRKATNST ATQMFKGSSE PNLNMFSNSL NPGCGDINWS
KLEKSEDMAK DNLFLQSSLT SARKRVRNIG TKSKRLLIDS VDVLELKITW EEAQELLRPP
QSTKPSIFTL ENQDFEEYDE PPVFGKRTLF VSRQTGEQEQ WVQCDACGKW RQLPVDILLP
PKWSCSDNLL DPGRSSCSAP DELSPREQDT LVRQSKEFKR RRLASSNEKL NQSQDASALN
SLGNAGITTT GEQGEITVAA TTKHPRHRAG CSCIVCSQPP SGKGKHKPSC TCTVCEAVKR
RFRTLMLRKR NKGEAGQASQ QAQSQSECRD ETEVESIPAV ELAAGENIDL NSDPGASRVS
MMRLLQAAAF PLEAYLKQKA ISNTAGEQQS SDMVSTEHGS SSAAQETEKD TTNGAHDPVN
