VIP6_ARATH
ID VIP6_ARATH Reviewed; 1091 AA.
AC B5X0I6; Q8S8H1; Q8VYL2;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein CTR9 homolog {ECO:0000305};
DE AltName: Full=Protein EARLY FLOWERING 8 {ECO:0000303|PubMed:15520273};
DE AltName: Full=Protein VERNALIZATION INDEPENDENCE 6 {ECO:0000303|PubMed:15472079};
GN Name=VIP6 {ECO:0000303|PubMed:15472079};
GN Synonyms=ELF8 {ECO:0000303|PubMed:15520273};
GN OrderedLocusNames=At2g06210 {ECO:0000312|Araport:AT2G06210};
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-914.
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 [4]
RP IDENTIFICATION.
RA Shiraya T., Sato S., Kato T., Tabata S., Iwasaki T.;
RT "Arabidopsis VIP6/ELF8, the homolog of CTR9 component of the
RT transcriptional complex PAF1, is essential for plant development.";
RL Plant Biotechnol. 25:447-455(2008).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=12750345; DOI=10.1093/genetics/164.1.347;
RA Zhang H., Ransom C., Ludwig P., van Nocker S.;
RT "Genetic analysis of early flowering mutants in Arabidopsis defines a class
RT of pleiotropic developmental regulator required for expression of the
RT flowering-time switch flowering locus C.";
RL Genetics 164:347-358(2003).
RN [6]
RP FUNCTION.
RX PubMed=15520273; DOI=10.1101/gad.1244504;
RA He Y., Doyle M.R., Amasino R.M.;
RT "PAF1-complex-mediated histone methylation of FLOWERING LOCUS C chromatin
RT is required for the vernalization-responsive, winter-annual habit in
RT Arabidopsis.";
RL Genes Dev. 18:2774-2784(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH VIP3 AND VIP4.
RX PubMed=15472079; DOI=10.1105/tpc.104.026062;
RA Oh S., Zhang H., Ludwig P., van Nocker S.;
RT "A mechanism related to the yeast transcriptional regulator Paf1c is
RT required for expression of the Arabidopsis FLC/MAF MADS box gene family.";
RL Plant Cell 16:2940-2953(2004).
RN [8]
RP IDENTIFICATION IN THE PAF1 COMPLEX, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20363855; DOI=10.1104/pp.110.155838;
RA Park S., Oh S., Ek-Ramos J., van Nocker S.;
RT "PLANT HOMOLOGOUS TO PARAFIBROMIN is a component of the PAF1 complex and
RT assists in regulating expression of genes within H3K27ME3-enriched
RT chromatin.";
RL Plant Physiol. 153:821-831(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21799800; DOI=10.1371/journal.pone.0022241;
RA Liu Y., Geyer R., van Zanten M., Carles A., Li Y., Horold A.,
RA van Nocker S., Soppe W.J.;
RT "Identification of the Arabidopsis REDUCED DORMANCY 2 gene uncovers a role
RT for the polymerase associated factor 1 complex in seed dormancy.";
RL PLoS ONE 6:E22241-E22241(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which is involved in
CC histone modifications such as methylation on histone H3 'Lys-4'
CC (H3K4me3) (PubMed:20363855). Involved in regulation of flowering time.
CC Required for the expression of the MADS box genes and flowering
CC repressors FLC, AGL27/FLM and AGL31/MAF2 (PubMed:15520273,
CC PubMed:15472079). Required for histone H3 trimethylation on 'Lys-4'
CC H3K4me3 at the FLC and AGL27/FLM loci (PubMed:15520273). Involved in
CC the control of seed dormancy and germination (PubMed:21799800).
CC {ECO:0000269|PubMed:15472079, ECO:0000269|PubMed:15520273,
CC ECO:0000269|PubMed:20363855, ECO:0000269|PubMed:21799800}.
CC -!- SUBUNIT: Component of the nuclear PAF1 complex (PAF1C), which consists
CC of VIP2/ELF7/PAF1, VIP3/SKI8/WDR61, VIP4/LEO1, VIP5/RTF1,
CC VIP6/ELF8/CTR9 and CDC73 (PubMed:20363855). Interacts with VIP3 and
CC VIP4 (PubMed:15472079). {ECO:0000269|PubMed:15472079,
CC ECO:0000269|PubMed:20363855}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20363855}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and shoot apex.
CC {ECO:0000269|PubMed:15520273}.
CC -!- DISRUPTION PHENOTYPE: Early flowering, reduced plant size and defects
CC in floral morphology in whorls 1-3, but fully fertile flowers
CC (PubMed:12750345). Reduced seed dormancy and increased germination rate
CC of freshly harvested seeds (PubMed:21799800).
CC {ECO:0000269|PubMed:12750345, ECO:0000269|PubMed:21799800}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL49858.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM15237.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006413; AAM15237.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06005.2; -; Genomic_DNA.
DR EMBL; AY070455; AAL49858.1; ALT_FRAME; mRNA.
DR EMBL; BR000721; FAA00428.1; -; mRNA.
DR PIR; B84476; B84476.
DR RefSeq; NP_178674.7; NM_126631.7.
DR AlphaFoldDB; B5X0I6; -.
DR SMR; B5X0I6; -.
DR IntAct; B5X0I6; 7.
DR STRING; 3702.AT2G06210.1; -.
DR iPTMnet; B5X0I6; -.
DR PaxDb; B5X0I6; -.
DR PeptideAtlas; B5X0I6; -.
DR PRIDE; B5X0I6; -.
DR ProteomicsDB; 234184; -.
DR GeneID; 815177; -.
DR KEGG; ath:AT2G06210; -.
DR Araport; AT2G06210; -.
DR TAIR; locus:2051592; AT2G06210.
DR eggNOG; KOG2002; Eukaryota.
DR HOGENOM; CLU_284636_0_0_1; -.
DR InParanoid; B5X0I6; -.
DR OrthoDB; 396755at2759; -.
DR PhylomeDB; B5X0I6; -.
DR PRO; PR:B5X0I6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR Genevisible; B5X0I6; AT.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0016571; P:histone methylation; IMP:TAIR.
DR GO; GO:0009910; P:negative regulation of flower development; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR031101; Ctr9.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14027; PTHR14027; 1.
DR Pfam; PF13181; TPR_8; 3.
DR SMART; SM00028; TPR; 13.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 11.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Flowering; Nucleus; Reference proteome; Repeat; TPR repeat;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..1091
FT /note="Protein CTR9 homolog"
FT /id="PRO_0000432762"
FT REPEAT 90..127
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 128..161
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 163..195
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 197..230
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REPEAT 232..267
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 305..338
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 343..376
FT /note="TPR 7"
FT /evidence="ECO:0000255"
FT REPEAT 377..410
FT /note="TPR 8"
FT /evidence="ECO:0000255"
FT REPEAT 412..443
FT /note="TPR 9"
FT /evidence="ECO:0000255"
FT REPEAT 449..482
FT /note="TPR 10"
FT /evidence="ECO:0000255"
FT REPEAT 558..591
FT /note="TPR 11"
FT /evidence="ECO:0000255"
FT REPEAT 593..625
FT /note="TPR 12"
FT /evidence="ECO:0000255"
FT REPEAT 640..673
FT /note="TPR 13"
FT /evidence="ECO:0000255"
FT REPEAT 674..707
FT /note="TPR 14"
FT /evidence="ECO:0000255"
FT REPEAT 713..746
FT /note="TPR 15"
FT /evidence="ECO:0000255"
FT REPEAT 749..782
FT /note="TPR 16"
FT /evidence="ECO:0000255"
FT REGION 919..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..952
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..996
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1091
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 1091 AA; 124088 MW; E019CD1F47373EE5 CRC64;
MASVYIPVQN SEEEVRVVLD QLPRDASDIL DILKAEQAPL DLWLIIAREY FKQGKIEQFR
QILEEGSSSD IDEYYADVKY ERIAILNALG AYYSYLGKTE TKNREKEEQF ISATRYYNKA
SRIDMHEPST WVGKGQLLLA KGEIDNALQA FKIVLDTAPD NVPALLGQAS VEFNRGRFSE
SLQLYKRALQ VFPGCPAAVR LGIGLCRYKL GQLDKARQAF DRVLQLDPDN VEALVALGIM
DLQANDSIGM RKGMDRMQQA FEIYPYCASA LNYLANHFFF TGQHFLVEQL TETALAVTTH
GPTKSHSFYN LARSYHSKGD FEKAGMYYMA AIKETNNNPH EFVFPYFGLG QVQLKLGELK
GSVFNFEKVL EVYPDNCETL KALGHLYTQL GQNEKALEYM RKATKLDPRD AQAFVGLGEL
LISSDTGAAL DAFKMARTLM KKGGQEVPIE VLNDIGALHF EREEFESALE NFKEALGDGI
WISFLDEKEN LEQTGVSVLG YKDTGIFHRL IESGHSVDVP WNKVTTLFNL ARLLEQIHKT
EAATFMYRLI LFKYPGYIDA YLRLAASAKA QNNLPLAIEL VNEALKVDDK NPNALSLLGE
LELKNDDWVK AKETFRAAND ATDGKDSYAI LSLGNWNYFA AMRNEKRNPK LEATHLEKAK
ELYTKVLTQH NSNMYAANGS GIVLAEKGQF DIAKDVFTQV QEAASGSVFL QMPDVWVNLA
HVYFAQGNFA LTVKMYQNCL RKFFYNTDSQ ILLYLARTHY EAEQWQECKK TLLRAIHLTP
SNYTFRFDLG AVMQKSSSST LQKKKRTADE VRSTVAEAEN AVRVFTQLSA ASDLHVHGFD
SKKIQTHVQY CSHLLEAAKV HREAAEQEEL QNRQRLEVAR QAALAEEARR KAEEQRKYQL
EKRKQEEELR RLKQEEEKFQ RIKEQWKSST PGSNKRKDRV EDDDGESKPS ERRRKKGGKR
RKKDKSSRAR HYEDDEEEAA TMDDHNEVED EDANTNYNRE DEMTTQEAEE PVDDDAHDLL
AAAGLEDPDV DDDEVPTSGV RRRRALSSSD EEGELMEESH PNSSPQKEKE ESNGEAGDPN
MEEEEEEEEA N
