OBE1_ARATH
ID OBE1_ARATH Reviewed; 566 AA.
AC Q9S736;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Protein OBERON 1 {ECO:0000303|PubMed:18403411};
DE AltName: Full=Potyvirus VPg-interacting protein 2 {ECO:0000303|PubMed:14963126};
GN Name=OBE1 {ECO:0000303|PubMed:18403411};
GN Synonyms=PVIP2 {ECO:0000303|PubMed:14963126};
GN OrderedLocusNames=At3g07780 {ECO:0000312|Araport:AT3G07780};
GN ORFNames=F17A17.12 {ECO:0000312|EMBL:AAF21188.1},
GN MLP3.23 {ECO:0000312|EMBL:AAF13095.1};
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].
RC STRAIN=cv. Columbia;
RA Callis J., Stone S.L., Troy A.;
RT "Functional Analysis of the Arabidopsis PHD family of proteins.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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; TISSUE=Leaf;
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 INTERACTION WITH POTYVIRUS VPG PROTEIN.
RX PubMed=14963126; DOI=10.1128/jvi.78.5.2301-2309.2004;
RA Dunoyer P., Thomas C., Harrison S., Revers F., Maule A.;
RT "A cysteine-rich plant protein potentiates Potyvirus movement through an
RT interaction with the virus genome-linked protein VPg.";
RL J. Virol. 78:2301-2309(2004).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DIMERIZATION.
RX PubMed=18403411; DOI=10.1242/dev.014993;
RA Saiga S., Furumizu C., Yokoyama R., Kurata T., Sato S., Kato T., Tabata S.,
RA Suzuki M., Komeda Y.;
RT "The Arabidopsis OBERON1 and OBERON2 genes encode plant homeodomain finger
RT proteins and are required for apical meristem maintenance.";
RL Development 135:1751-1759(2008).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION BY AUXIN, SUBUNIT, AND INTERACTION WITH OBE2; OBE3 AND OBE4.
RX PubMed=19392692; DOI=10.1111/j.1365-313x.2009.03874.x;
RA Thomas C.L., Schmidt D., Bayer E.M., Dreos R., Maule A.J.;
RT "Arabidopsis plant homeodomain finger proteins operate downstream of auxin
RT accumulation in specifying the vasculature and primary root meristem.";
RL Plant J. 59:426-436(2009).
RN [8]
RP INTERACTION WITH OBE2; OBE3 AND OBE4.
RX PubMed=22378640; DOI=10.1242/dev.074492;
RA Saiga S., Moeller B., Watanabe-Taneda A., Abe M., Weijers D., Komeda Y.;
RT "Control of embryonic meristem initiation in Arabidopsis by PHD-finger
RT protein complexes.";
RL Development 139:1391-1398(2012).
RN [9]
RP INTERACTION WITH RBL, AND SUBCELLULAR LOCATION.
RX PubMed=30338215; DOI=10.1002/2211-5463.12504;
RA de Bossoreille S., Morel P., Trehin C., Negrutiu I.;
RT "REBELOTE, a regulator of floral determinacy in Arabidopsis thaliana,
RT interacts with both nucleolar and nucleoplasmic proteins.";
RL FEBS Open Bio 8:1636-1648(2018).
CC -!- FUNCTION: Probable transcription factor that acts together with OBE2
CC for the maintenance and/or establishment of both the shoot and root
CC meristems, probably by controlling the expression of the meristem genes
CC such as WUS, PLT1 and PLT2 and of genes required for auxin responses.
CC Promotes cell meristematic activity via the WUSCHEL-CLAVATA pathway.
CC Involved in the development of the basal pole and in auxin-mediated
CC root and vascular development in the embryo. Confers sensitivity to
CC turnip mosaic virus (TuMV) probably by promoting viral movement and
CC multiplication via interaction with TuMV VPg.
CC {ECO:0000269|PubMed:18403411, ECO:0000269|PubMed:19392692}.
CC -!- SUBUNIT: Self-interacts (PubMed:18403411, PubMed:19392692,
CC PubMed:22378640). Interacts with OBE2, OBE3 and OBE4 (PubMed:19392692,
CC PubMed:22378640). Binds to VPg of pea seed borne mosaic virus (PSbMV),
CC turnip mosaic virus (TuMV) and lettuce mosaic virus (LMV), but not with
CC VPg of tobacco etch virus (TEV), cowpea mosaic virus (CPMV), tomato
CC black ring virus (TBRV) and grapevine fan leaf virus (GFLV)
CC (PubMed:14963126). Interacts with RBL (PubMed:30338215).
CC {ECO:0000269|PubMed:14963126, ECO:0000269|PubMed:18403411,
CC ECO:0000269|PubMed:19392692, ECO:0000269|PubMed:22378640,
CC ECO:0000269|PubMed:30338215}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18403411}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:30338215}. Note=Colocalizes with
CC heterochromatin. {ECO:0000269|PubMed:30338215}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, seedlings, stems, leaves,
CC flowers and siliques, especially in the vasculature.
CC {ECO:0000269|PubMed:18403411, ECO:0000269|PubMed:19392692}.
CC -!- DEVELOPMENTAL STAGE: First observed in the embryo proper at the four-
CC cell stage. Later expressed throughout the embryo from the eight-cell
CC to the bent-cotyledon stages. Until the torpedo stage of development,
CC mostly concentrated at the root pole. At the torpedo stage, strongest
CC levels in the columella and lateral root cap. Hardly detected in the
CC suspensor. Present in seedling roots. In mature and fully
CC differentiated young roots, accumulates from the root cap to the
CC emerging root hair zone. {ECO:0000269|PubMed:18403411,
CC ECO:0000269|PubMed:19392692}.
CC -!- INDUCTION: By auxin in the root elongation zone.
CC {ECO:0000269|PubMed:19392692}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. When associated with OBE2
CC disruption, plants exhibit premature termination of the shoot meristem
CC and impaired root apical meristem establishment, leading to a
CC diminutive phenotype characterized by an absence of roots and defective
CC development of the vasculature. {ECO:0000269|PubMed:18403411,
CC ECO:0000269|PubMed:19392692}.
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DR EMBL; DQ059085; AAY57579.1; -; mRNA.
DR EMBL; AC009176; AAF13095.1; -; Genomic_DNA.
DR EMBL; AC013483; AAF21188.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74603.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64894.1; -; Genomic_DNA.
DR EMBL; AY045899; AAK76573.1; -; mRNA.
DR EMBL; AY113947; AAM44995.1; -; mRNA.
DR RefSeq; NP_001326896.1; NM_001337745.1.
DR RefSeq; NP_566320.1; NM_111657.4.
DR AlphaFoldDB; Q9S736; -.
DR SMR; Q9S736; -.
DR BioGRID; 5304; 32.
DR IntAct; Q9S736; 27.
DR STRING; 3702.AT3G07780.1; -.
DR iPTMnet; Q9S736; -.
DR PaxDb; Q9S736; -.
DR PRIDE; Q9S736; -.
DR ProteomicsDB; 250852; -.
DR EnsemblPlants; AT3G07780.1; AT3G07780.1; AT3G07780.
DR EnsemblPlants; AT3G07780.3; AT3G07780.3; AT3G07780.
DR GeneID; 819969; -.
DR Gramene; AT3G07780.1; AT3G07780.1; AT3G07780.
DR Gramene; AT3G07780.3; AT3G07780.3; AT3G07780.
DR KEGG; ath:AT3G07780; -.
DR Araport; AT3G07780; -.
DR TAIR; locus:2077362; AT3G07780.
DR eggNOG; ENOG502QSQF; Eukaryota.
DR HOGENOM; CLU_006737_2_0_1; -.
DR InParanoid; Q9S736; -.
DR PhylomeDB; Q9S736; -.
DR PRO; PR:Q9S736; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S736; baseline and differential.
DR Genevisible; Q9S736; AT.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; TAS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0010078; P:maintenance of root meristem identity; IGI:TAIR.
DR GO; GO:0010492; P:maintenance of shoot apical meristem identity; IGI:TAIR.
DR GO; GO:0080022; P:primary root development; IGI:TAIR.
DR GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IGI:TAIR.
DR GO; GO:0010071; P:root meristem specification; IGI:TAIR.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IMP:UniProtKB.
DR InterPro; IPR004082; OBERON.
DR InterPro; IPR032535; Oberon_cc.
DR InterPro; IPR032881; Oberon_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR PANTHER; PTHR21736; PTHR21736; 1.
DR Pfam; PF16312; Oberon_cc; 1.
DR Pfam; PF07227; PHD_Oberon; 1.
DR PIRSF; PIRSF025218; DUF1423_pln; 1.
DR PRINTS; PR01544; ARATH130DUF.
DR SMART; SM00249; PHD; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Host-virus interaction; Metal-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..566
FT /note="Protein OBERON 1"
FT /id="PRO_0000399746"
FT ZN_FING 225..289
FT /note="PHD-type"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 407..522
FT /evidence="ECO:0000255"
FT COMPBIAS 1..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 64159 MW; DAC1161B995BFC71 CRC64;
MGTSSGSNLP HQMLPPRQQL QTSLSLVSSD PHLSRSNSGI VRESPAESAS SQETWPTSKS
IMGRKTDSGK TGPDSHDQHV IRHVSIADKV SLRDIARERL DIVAERMHRL PEEYLEELKN
GLKAILEGNG AQPIDEFMFL QKFVQTRSDL TSKTLVRAHR VQLEVLVVIN TGIQAFLHPN
INLSQSSLIE IFVYKRCRNI ACQNELPADG CPCEICANRK GFCNLCMCVI CNKFDFAVNT
CRWIGCDVCS HWTHTDCAIR DGEISMGVSP KSVSGMGEML FKCRACNHTS ELLGWVKDVF
QHCAPNWDRE SLMKELDFVS RIFRGSEDTR GRKLFWKCEE LMEKIKGGLA EATAAKLILM
FFQEIELDSP KSLESGEGGG TIAPQDACNR IAEVVKETLR KMEIVGEEKT RMYKKARMGL
EECEREVEEK AKQVAELQME RQKKKQQIEE VERIVRLKQA EAEMFQLKAN EAKVEAERLE
RIVKAKKEKT EEEYASNYLK LRLSEAEAEK EYLFEKIKEQ ESGGNGGEAS QAVMYSKIRE
MLHGYNASSP RVDPRSNQRN PFRSNP
