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VAL1_ARATH
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   03-AUG-2022, entry version 132.
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};
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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.AT2G30470.1; -.
DR   iPTMnet; Q8W4L5; -.
DR   PaxDb; Q8W4L5; -.
DR   PRIDE; Q8W4L5; -.
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; locus:2064417; AT2G30470.
DR   eggNOG; ENOG502QWC1; Eukaryota.
DR   HOGENOM; CLU_015907_0_0_1; -.
DR   InParanoid; Q8W4L5; -.
DR   OMA; TGYTHES; -.
DR   OrthoDB; 186755at2759; -.
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 transcription, DNA-templated; 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; 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; 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
 
 
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