WRI1_ARATH
ID WRI1_ARATH Reviewed; 430 AA.
AC Q6X5Y6; Q2V3P6; Q6J9N7; Q9M2V3; Q9M2V4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Ethylene-responsive transcription factor WRI1;
DE AltName: Full=Protein ACTIVATOR OF SPORAMIN::LUC 1;
DE AltName: Full=Protein WRINKLED 1;
GN Name=WRI1; Synonyms=ASML1; OrderedLocusNames=At3g54320;
GN ORFNames=T12E18.10, T12E18.20;
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), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Col-2;
RX PubMed=15500472; DOI=10.1111/j.1365-313x.2004.02235.x;
RA Cernac A., Benning C.;
RT "WRINKLED1 encodes an AP2/EREB domain protein involved in the control of
RT storage compound biosynthesis in Arabidopsis.";
RL Plant J. 40:575-585(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=15753106; DOI=10.1093/pcp/pci072;
RA Masaki T., Mitsui N., Tsukagoshi H., Nishii T., Morikami A., Nakamura K.;
RT "ACTIVATOR of Spomin::LUC1/WRINKLED1 of Arabidopsis thaliana transactivates
RT sugar-inducible promoters.";
RL Plant Cell Physiol. 46:547-556(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Pan Y., Gong W., Liu D., Fu Q., Mei W.-Q., Song W.-Q., Ma L.-G., Luo J.-C.,
RA Deng X.-W., Zhu Y.-X.;
RT "Molecular cloning, expression, phylogenetic and functional
RT characterization of the Arabidopsis AP2/EREBP transcription factor
RT family.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [5]
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 [6]
RP FUNCTION.
RX PubMed=9733529; DOI=10.1104/pp.118.1.91;
RA Focks N., Benning C.;
RT "wrinkled1: A novel, low-seed-oil mutant of Arabidopsis with a deficiency
RT in the seed-specific regulation of carbohydrate metabolism.";
RL Plant Physiol. 118:91-101(1998).
RN [7]
RP FUNCTION.
RX PubMed=12084821; DOI=10.1105/tpc.000877;
RA Ruuska S.A., Girke T., Benning C., Ohlrogge J.B.;
RT "Contrapuntal networks of gene expression during Arabidopsis seed
RT filling.";
RL Plant Cell 14:1191-1206(2002).
RN [8]
RP FUNCTION.
RX PubMed=16553903; DOI=10.1111/j.1365-313x.2006.02682.x;
RA Baud S., Graham I.A.;
RT "A spatiotemporal analysis of enzymatic activities associated with carbon
RT metabolism in wild-type and mutant embryos of Arabidopsis using in situ
RT histochemistry.";
RL Plant J. 46:155-169(2006).
RN [9]
RP FUNCTION.
RX PubMed=16632590; DOI=10.1104/pp.106.079574;
RA Cernac A., Andre C., Hoffmann-Benning S., Benning C.;
RT "WRI1 is required for seed germination and seedling establishment.";
RL Plant Physiol. 141:745-757(2006).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16407444; DOI=10.1104/pp.105.073783;
RA Nakano T., Suzuki K., Fujimura T., Shinshi H.;
RT "Genome-wide analysis of the ERF gene family in Arabidopsis and rice.";
RL Plant Physiol. 140:411-432(2006).
RN [11]
RP ACTIVITY REGULATION, MUTAGENESIS OF LYS-2; LYS-3; THR-70 AND SER-166,
RP UBIQUITINATION, INTERACTION WITH KIN10 AND KIN11, PHOSPHORYLATION AT THR-70
RP AND SER-166, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28314829; DOI=10.1105/tpc.17.00019;
RA Zhai Z., Liu H., Shanklin J.;
RT "Phosphorylation of WRINKLED1 by KIN10 results in its proteasomal
RT degradation, providing a link between energy homeostasis and lipid
RT biosynthesis.";
RL Plant Cell 29:871-889(2017).
CC -!- FUNCTION: May be involved in the regulation of gene expression by
CC stress factors and by components of stress signal transduction pathways
CC (By similarity). Transcriptional activator involved in the activation
CC of a subset of sugar-responsive genes and the control of carbon flow
CC from sucrose import to oil accumulation in developing seeds. Binds to
CC the GCC-box pathogenesis-related promoter element. Promotes sugar
CC uptake and seed oil accumulation by glycolysis. Required for embryo
CC development, seed germination and, indirectly, for seedling
CC establishment. Negative regulator of the ABA-mediated germination
CC inhibition. {ECO:0000250, ECO:0000269|PubMed:12084821,
CC ECO:0000269|PubMed:15500472, ECO:0000269|PubMed:15753106,
CC ECO:0000269|PubMed:16553903, ECO:0000269|PubMed:16632590,
CC ECO:0000269|PubMed:9733529}.
CC -!- ACTIVITY REGULATION: Down-regulated by KIN10 that controls its protein
CC stability under a phosphorylation-dependent manner.
CC {ECO:0000269|PubMed:28314829}.
CC -!- SUBUNIT: Interacts with KIN10 and KIN11. {ECO:0000269|PubMed:28314829}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6X5Y6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6X5Y6-2; Sequence=VSP_027415, VSP_027416;
CC Name=3;
CC IsoId=Q6X5Y6-3; Sequence=VSP_027417;
CC -!- TISSUE SPECIFICITY: Mostly expressed in siliques, especially in seeds.
CC Also detected in roots and flowers, and, to a lower extent, in leaves
CC stems and seedlings. {ECO:0000269|PubMed:15500472,
CC ECO:0000269|PubMed:15753106}.
CC -!- INDUCTION: Transiantly in leaves by sucrose, but not by abscisic acid
CC (ABA). {ECO:0000269|PubMed:15753106}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:28314829}.
CC -!- PTM: The phosphorylation at Thr-70 and Ser-166 by KIN10 facilitates its
CC degradation via the proteasomal pathway. {ECO:0000269|PubMed:28314829}.
CC -!- SIMILARITY: Belongs to the AP2/ERF transcription factor family. AP2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81797.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81798.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY254038; AAP80382.1; -; mRNA.
DR EMBL; AY885245; AAX11223.1; -; mRNA.
DR EMBL; AY560888; AAT44955.1; -; mRNA.
DR EMBL; AL132971; CAB81797.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL132971; CAB81798.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79213.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79215.1; -; Genomic_DNA.
DR PIR; T47591; T47591.
DR PIR; T47592; T47592.
DR RefSeq; NP_001030857.1; NM_001035780.3. [Q6X5Y6-1]
DR RefSeq; NP_191000.3; NM_115292.4. [Q6X5Y6-3]
DR AlphaFoldDB; Q6X5Y6; -.
DR SMR; Q6X5Y6; -.
DR BioGRID; 9916; 6.
DR STRING; 3702.AT3G54320.1; -.
DR iPTMnet; Q6X5Y6; -.
DR PaxDb; Q6X5Y6; -.
DR PRIDE; Q6X5Y6; -.
DR EnsemblPlants; AT3G54320.1; AT3G54320.1; AT3G54320. [Q6X5Y6-3]
DR EnsemblPlants; AT3G54320.3; AT3G54320.3; AT3G54320. [Q6X5Y6-1]
DR GeneID; 824599; -.
DR Gramene; AT3G54320.1; AT3G54320.1; AT3G54320. [Q6X5Y6-3]
DR Gramene; AT3G54320.3; AT3G54320.3; AT3G54320. [Q6X5Y6-1]
DR KEGG; ath:AT3G54320; -.
DR Araport; AT3G54320; -.
DR TAIR; locus:2096144; AT3G54320.
DR eggNOG; ENOG502QQW2; Eukaryota.
DR HOGENOM; CLU_048809_0_0_1; -.
DR InParanoid; Q6X5Y6; -.
DR OrthoDB; 934258at2759; -.
DR PhylomeDB; Q6X5Y6; -.
DR PRO; PR:Q6X5Y6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q6X5Y6; baseline and differential.
DR Genevisible; Q6X5Y6; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:TAIR.
DR GO; GO:0006629; P:lipid metabolic process; IMP:TAIR.
DR GO; GO:1901959; P:positive regulation of cutin biosynthetic process; IGI:TAIR.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IMP:TAIR.
DR GO; GO:0006110; P:regulation of glycolytic process; IMP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IMP:TAIR.
DR CDD; cd00018; AP2; 2.
DR Gene3D; 3.30.730.10; -; 2.
DR InterPro; IPR001471; AP2/ERF_dom.
DR InterPro; IPR036955; AP2/ERF_dom_sf.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR Pfam; PF00847; AP2; 2.
DR PRINTS; PR00367; ETHRSPELEMNT.
DR SMART; SM00380; AP2; 2.
DR SUPFAM; SSF54171; SSF54171; 2.
DR PROSITE; PS51032; AP2_ERF; 2.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Ethylene signaling pathway;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..430
FT /note="Ethylene-responsive transcription factor WRI1"
FT /id="PRO_0000297946"
FT DNA_BIND 65..131
FT /note="AP2/ERF 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT DNA_BIND 167..225
FT /note="AP2/ERF 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00366"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphothreonine; by KIN10"
FT /evidence="ECO:0000269|PubMed:28314829"
FT MOD_RES 166
FT /note="Phosphoserine; by KIN10"
FT /evidence="ECO:0000269|PubMed:28314829"
FT VAR_SEQ 199..208
FT /note="NTQEEAAAAY -> STLSPFPFFF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_027415"
FT VAR_SEQ 209..430
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_027416"
FT VAR_SEQ 430
FT /note="V -> FQGLFVGSE (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_027417"
FT MUTAGEN 2
FT /note="K->R: Favorises its stability; when associated with
FT R-3."
FT /evidence="ECO:0000269|PubMed:28314829"
FT MUTAGEN 3
FT /note="K->R: Favorises its stability; when associated with
FT R-2."
FT /evidence="ECO:0000269|PubMed:28314829"
FT MUTAGEN 70
FT /note="T->A: Loss of KIN10-dependent phosphorylation; when
FT associated with A-166."
FT /evidence="ECO:0000269|PubMed:28314829"
FT MUTAGEN 166
FT /note="S->A: Loss of KIN10-dependent phosphorylation; when
FT associated with A-70."
FT /evidence="ECO:0000269|PubMed:28314829"
SQ SEQUENCE 430 AA; 48436 MW; 8B2F2C9B402DEE0F CRC64;
MKKRLTTSTC SSSPSSSVSS STTTSSPIQS EAPRPKRAKR AKKSSPSGDK SHNPTSPAST
RRSSIYRGVT RHRWTGRFEA HLWDKSSWNS IQNKKGKQVY LGAYDSEEAA AHTYDLAALK
YWGPDTILNF PAETYTKELE EMQRVTKEEY LASLRRQSSG FSRGVSKYRG VARHHHNGRW
EARIGRVFGN KYLYLGTYNT QEEAAAAYDM AAIEYRGANA VTNFDISNYI DRLKKKGVFP
FPVNQANHQE GILVEAKQEV ETREAKEEPR EEVKQQYVEE PPQEEEEKEE EKAEQQEAEI
VGYSEEAAVV NCCIDSSTIM EMDRCGDNNE LAWNFCMMDT GFSPFLTDQN LANENPIEYP
ELFNELAFED NIDFMFDDGK HECLNLENLD CCVVGRESPP SSSSPLSCLS TDSASSTTTT
TTSVSCNYLV
