VRN2_ARATH
ID VRN2_ARATH Reviewed; 440 AA.
AC Q8W5B1; O23524; O23525; Q8W5B2; Q94CF5;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Polycomb group protein VERNALIZATION 2;
GN Name=VRN2; OrderedLocusNames=At4g16845; ORFNames=dl4450w, FCAALL.23;
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] (ISOFORMS 1 AND 2), FUNCTION, AND
RP CHARACTERIZATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11719192; DOI=10.1016/s0092-8674(01)00573-6;
RA Gendall A.R., Levy Y.Y., Wilson A., Dean C.;
RT "The VERNALIZATION2 (VRN2) gene mediates the epigenetic regulation of
RT vernalization in Arabidopsis.";
RL Cell 107:525-535(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18854416; DOI=10.1073/pnas.0808687105;
RA De Lucia F., Crevillen P., Jones A.M.E., Greb T., Dean C.;
RT "A PHD-polycomb repressive complex 2 triggers the epigenetic silencing of
RT FLC during vernalization.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:16831-16836(2008).
RN [7]
RP INTERACTION WITH ALP1.
RX PubMed=26642436; DOI=10.1371/journal.pgen.1005660;
RA Liang S.C., Hartwig B., Perera P., Mora-Garcia S., de Leau E., Thornton H.,
RA de Lima Alves F., de Alves F.L., Rappsilber J., Rapsilber J., Yang S.,
RA James G.V., Schneeberger K., Finnegan E.J., Turck F., Goodrich J.;
RT "Kicking against the PRCs - A domesticated transposase antagonises
RT silencing mediated by polycomb group proteins and is an accessory component
RT of polycomb repressive complex 2.";
RL PLoS Genet. 11:E1005660-E1005660(2015).
CC -!- FUNCTION: Polycomb group (PcG) protein. Plays a central role in
CC vernalization by maintaining repressed the homeotic gene FLC, a floral
CC repressor, after a cold treatment. PcG proteins act by forming
CC multiprotein complexes, which are required to maintain the
CC transcriptionally repressive state of homeotic genes throughout
CC development. PcG proteins are not required to initiate repression, but
CC to maintain it during later stages of development. They probably act
CC via the methylation of histones, rendering chromatin heritably changed
CC in its expressibility. Associates constitutively along the whole FLC
CC locus. {ECO:0000269|PubMed:11719192, ECO:0000269|PubMed:18854416}.
CC -!- SUBUNIT: Probable component of a PcG complex. In plants, PcG complexes
CC are probably composed of a member of the EZ family (CLF or MEA), FIE,
CC and a member of the VEFS family (FIS2, VRN2 or EMF2) (By similarity).
CC Component of the plant homeodomain / polycomb repressive complex 2
CC (PHD-PRC2) large complex during prolonged cold, composed of core PRC2
CC components (VRN2, EZA1, FIE and MSI1), and three related PHD finger
CC proteins (VIL1, VIL2 and VIN3) that mediates histone H3 trimethylation
CC on 'Lys-27' (H3K27me3). Binds to ALP1 (PubMed:26642436). {ECO:0000250,
CC ECO:0000269|PubMed:18854416, ECO:0000269|PubMed:26642436}.
CC -!- INTERACTION:
CC Q8W5B1; P93831: CLF; NbExp=3; IntAct=EBI-2128880, EBI-307155;
CC Q8W5B1; Q9ZSM8: EZA1; NbExp=3; IntAct=EBI-2128880, EBI-1102047;
CC Q8W5B1; Q9LT47: FIE; NbExp=3; IntAct=EBI-2128880, EBI-307146;
CC Q8W5B1; Q9FIE3: VIN3; NbExp=2; IntAct=EBI-2128880, EBI-2358223;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8W5B1-1; Sequence=Displayed;
CC Name=2; Synonyms=VRN2';
CC IsoId=Q8W5B1-2; Sequence=VSP_007457, VSP_007458;
CC -!- TISSUE SPECIFICITY: Weakly expressed. Expressed both during, and in the
CC absence of vernalization.
CC -!- SIMILARITY: Belongs to the VEFS (VRN2-EMF2-FIS2-SU(Z)12) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10457.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80955.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF284500; AAL32135.1; -; mRNA.
DR EMBL; AF284501; AAL32136.1; -; mRNA.
DR EMBL; Z97342; CAB10457.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161545; CAB80955.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83814.1; -; Genomic_DNA.
DR EMBL; AY034902; AAK59409.1; -; mRNA.
DR EMBL; AY063047; AAL34221.1; -; mRNA.
DR PIR; G71435; G71435.
DR RefSeq; NP_567517.1; NM_117787.4. [Q8W5B1-1]
DR AlphaFoldDB; Q8W5B1; -.
DR BioGRID; 12685; 8.
DR DIP; DIP-48610N; -.
DR IntAct; Q8W5B1; 8.
DR STRING; 3702.AT4G16845.1; -.
DR PaxDb; Q8W5B1; -.
DR PRIDE; Q8W5B1; -.
DR ProteomicsDB; 242332; -. [Q8W5B1-1]
DR EnsemblPlants; AT4G16845.1; AT4G16845.1; AT4G16845. [Q8W5B1-1]
DR GeneID; 827392; -.
DR Gramene; AT4G16845.1; AT4G16845.1; AT4G16845. [Q8W5B1-1]
DR KEGG; ath:AT4G16845; -.
DR Araport; AT4G16845; -.
DR TAIR; locus:3685330; AT4G16845.
DR eggNOG; KOG2350; Eukaryota.
DR eggNOG; KOG4197; Eukaryota.
DR HOGENOM; CLU_047065_0_0_1; -.
DR InParanoid; Q8W5B1; -.
DR OMA; INSNAMD; -.
DR OrthoDB; 516359at2759; -.
DR PhylomeDB; Q8W5B1; -.
DR PRO; PR:Q8W5B1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W5B1; baseline and differential.
DR Genevisible; Q8W5B1; AT.
DR GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0010048; P:vernalization response; IMP:TAIR.
DR InterPro; IPR019135; Polycomb_protein_VEFS-Box.
DR Pfam; PF09733; VEFS-Box; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..440
FT /note="Polycomb group protein VERNALIZATION 2"
FT /id="PRO_0000047841"
FT ZN_FING 86..111
FT /note="C2H2-type"
FT REGION 267..345
FT /note="VEFS-box"
FT REGION 398..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 156..163
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 398..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 102..107
FT /note="GLQFHL -> VGNYYN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11719192"
FT /id="VSP_007457"
FT VAR_SEQ 108..440
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11719192"
FT /id="VSP_007458"
FT CONFLICT 81
FT /note="R -> K (in Ref. 1; AAL32135/AAL32136)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="L -> S (in Ref. 1; AAL32135)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="A -> T (in Ref. 1; AAL32135)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="A -> T (in Ref. 1; AAL32135)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="T -> S (in Ref. 1; AAL32135)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="V -> A (in Ref. 1; AAL32135)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="C -> R (in Ref. 1; AAL32135)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..398
FT /note="TSVTN -> SSDTTTT (in Ref. 1; AAL32135)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="H -> R (in Ref. 1; AAL32135)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="K -> N (in Ref. 1; AAL32135)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="K -> KVIK (in Ref. 1; AAL32135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 50624 MW; 0E0AB2C55517BE6F CRC64;
MCRQNCRAKS SPEEVISTDE NLLIYCKPVR LYNIFHLRSL GNPSFLPRCL NYKIGAKRKR
KSRSTGMVVF NYKDCNNTLQ RTEVREDCSC PFCSMLCGSF KGLQFHLNSS HDLFEFEFKL
LEEYQTVNVS VKLNSFIFEE EGSDDDKFEP FSLCSKPRKR RQRGGRNNTR RLKVCFLPLD
SPSLANGTEN GIALLNDGNR GLGYPEATEL AGQFEMTSNI PPAIAHSSLD AGAKVILTTE
AVVPATKTRK LSAERSEARS HLLLQKRQFY HSHRVQPMAL EQVMSDRDSE DEVDDDVADF
EDRQMLDDFV DVNKDEKQFM HLWNSFVRKQ RVIADGHISW ACEVFSRFYE KELHCYSSLF
WCWRLFLIKL WNHGLVDSAT INNCNTILEN CRNTSVTNNN NNSVDHPSDS NTNNNNIVDH
PNDIKNKNNV DNKDNNSRDK
