OBE3_ARATH
ID OBE3_ARATH Reviewed; 733 AA.
AC Q94B71; Q9LQV7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Protein OBERON 3 {ECO:0000305};
DE AltName: Full=Protein TITANIA 1 {ECO:0000303|PubMed:22378640};
DE AltName: Full=Protein WUS ENHANCER 9 {ECO:0000303|PubMed:27196372};
GN Name=OBE3 {ECO:0000303|PubMed:27196372};
GN Synonyms=WEN9 {ECO:0000303|PubMed:27196372};
GN OrderedLocusNames=At1g14740 {ECO:0000312|Araport:AT1G14740};
GN ORFNames=F10B6.14 {ECO:0000312|EMBL:AAF79245.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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 INTERACTION WITH OBE1 AND OBE2.
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 [5]
RP FUNCTION, INTERACTION WITH OBE1; OBE2 AND OBE4, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27196372; DOI=10.1371/journal.pone.0155657;
RA Lin T.F., Saiga S., Abe M., Laux T.;
RT "OBE3 and WUS interaction in shoot meristem stem cell regulation.";
RL PLoS ONE 11:E0155657-E0155657(2016).
CC -!- FUNCTION: Probable transcription factor that functions redundantly with
CC OBE4 in specification of the hypophysis and establishment of the
CC embryonic root (PubMed:22378640). Involved in the activation of
CC ARF5/MP-dependent gene expression during embryonic root meristem
CC initiation (PubMed:22378640). Involved in shoot meristem homeostasis
CC (PubMed:27196372). {ECO:0000269|PubMed:22378640,
CC ECO:0000269|PubMed:27196372}.
CC -!- SUBUNIT: Self-interacts (PubMed:22378640). Interacts with OBE1 and OBE2
CC (PubMed:19392692, PubMed:22378640). Interacts with OBE4
CC (PubMed:22378640). {ECO:0000269|PubMed:19392692,
CC ECO:0000269|PubMed:22378640}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9S736}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the two-cell stage embryo
CC (PubMed:22378640). At early globular embryo stage, expressed both in
CC the basal region of embryo proper and suspensor cells
CC (PubMed:22378640). At heart and torpedo embryo stages expressed in the
CC basal region apical regions of the embryo proper (PubMed:22378640).
CC {ECO:0000269|PubMed:22378640}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutants tta1 and tta2 exhibit a rootless
CC phenotype and seedling lethality (PubMed:22378640). No visible
CC phenotype under normal growth conditions, but the double mutants obe3-2
CC and obe4-2 exhibit broad growth defects and developmental arrest of
CC seedlings (PubMed:27196372). {ECO:0000269|PubMed:22378640,
CC ECO:0000269|PubMed:27196372}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79245.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006917; AAF79245.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29216.1; -; Genomic_DNA.
DR EMBL; AY042810; AAK68750.1; -; mRNA.
DR EMBL; AY081688; AAM10250.1; -; mRNA.
DR PIR; F86281; F86281.
DR RefSeq; NP_563958.1; NM_101343.2.
DR AlphaFoldDB; Q94B71; -.
DR SMR; Q94B71; -.
DR BioGRID; 23279; 5.
DR IntAct; Q94B71; 2.
DR STRING; 3702.AT1G14740.1; -.
DR iPTMnet; Q94B71; -.
DR PaxDb; Q94B71; -.
DR PRIDE; Q94B71; -.
DR ProteomicsDB; 250853; -.
DR EnsemblPlants; AT1G14740.1; AT1G14740.1; AT1G14740.
DR GeneID; 838039; -.
DR Gramene; AT1G14740.1; AT1G14740.1; AT1G14740.
DR KEGG; ath:AT1G14740; -.
DR Araport; AT1G14740; -.
DR TAIR; locus:2006837; AT1G14740.
DR eggNOG; ENOG502QPTA; Eukaryota.
DR HOGENOM; CLU_006737_3_0_1; -.
DR InParanoid; Q94B71; -.
DR OMA; CAKNWGL; -.
DR OrthoDB; 340123at2759; -.
DR PhylomeDB; Q94B71; -.
DR PRO; PR:Q94B71; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94B71; baseline and differential.
DR Genevisible; Q94B71; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001708; P:cell fate specification; IGI:TAIR.
DR GO; GO:0090421; P:embryonic meristem initiation; IGI:TAIR.
DR GO; GO:0009880; P:embryonic pattern specification; IGI:TAIR.
DR GO; GO:0055065; P:metal ion homeostasis; IEA:EnsemblPlants.
DR InterPro; IPR004082; OBERON.
DR InterPro; IPR032535; Oberon_cc.
DR InterPro; IPR032881; Oberon_PHD.
DR PANTHER; PTHR21736; PTHR21736; 1.
DR Pfam; PF16312; Oberon_cc; 1.
DR Pfam; PF07227; PHD_Oberon; 1.
DR PRINTS; PR01544; ARATH130DUF.
PE 1: Evidence at protein level;
KW Coiled coil; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..733
FT /note="Protein OBERON 3"
FT /id="PRO_0000399748"
FT ZN_FING 436..500
FT /note="PHD-type"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 120..153
FT /evidence="ECO:0000255"
FT COILED 644..733
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 82389 MW; 6B8B010CF4316455 CRC64;
MIGEKDLAGD GECSRTKTSK PRFSNLNNQT HQDDKTGQYH QKGVDFLNVR SNNLDGGFSS
KSSPRSGNEL TLSYLCENSG KLAESLGQKG KEVVTFSENS SYDDKWVERD FFNLREMNPN
SSKRKAHEEE EEAEEEEDKK SNKIETLNLS LALPDVSLSL TASNAVKRPR VVTSERTTTS
FSNDFTATAP SMSYSYSHPF SHNISCSMTR NSTDFDCSVG KDDHIWCAGE GTNGSVHSRF
RPIGDGGVAL ANNPVSGKPS SSADYSFFPS ELPARPGNEV TISGDSRKKV ANLEDNDAVR
SERVLYDIVS KSISSVALII QGMADETLES AKEYLRNLID SPEKKEKLVN LQNQIDKRSD
LSKETLSKCV KDQLDILVAV RTGLKYFLSG KIRIPMNELV EIFLFLRCRN VNCKSLLPVD
DCECKICSNN KGFCSSCMCP VCLRFDSASN TCSWVGCDVC SHWCHAACGI QKNLIKPGHS
LKGQRGTTEM MFHCIGCAHK SEMFGFVKDV FVCCAKNWGL ETLIKELDCV RKVFRGSDDA
KGKALHLKAN EMVKKLESKQ ISPLDASNFI IQFFNYAESI PEIPDPPREL TVAAETSYRK
DEASVTPSTS KDQKKKSFAL TDAMMNSFDS LESMVRIKEA ETRMFQKKAD EARIEAESFK
RMIEMKTEKM EEEYTEKLAR LCLQETEERR RNKLEELKKL ENSHCDYRNM KLRMEAEIAG
LLKRMEVTRQ QLV
