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MYB98_ARATH
ID   MYB98_ARATH             Reviewed;         427 AA.
AC   Q9S7L2; A0MF81; Q3HSE6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Transcription factor MYB98 {ECO:0000303|PubMed:11597504};
DE   AltName: Full=Myb-related protein 98 {ECO:0000303|PubMed:11597504};
DE            Short=AtMYB98 {ECO:0000303|PubMed:11597504};
GN   Name=MYB98 {ECO:0000303|PubMed:11597504};
GN   OrderedLocusNames=At4g18770 {ECO:0000312|Araport:AT4G18770};
GN   ORFNames=F28A21.180 {ECO:0000312|EMBL:CAB37462.1};
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;
RX   PubMed=10743663; DOI=10.1046/j.1365-313x.2000.00666.x;
RA   Kranz H., Scholz K., Weisshaar B.;
RT   "c-MYB oncogene-like genes encoding three MYB repeats occur in all major
RT   plant lineages.";
RL   Plant J. 21:231-235(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=16214903; DOI=10.1105/tpc.105.034603;
RA   Kasahara R.D., Portereiko M.F., Sandaklie-Nikolova L., Rabiger D.S.,
RA   Drews G.N.;
RT   "MYB98 is required for pollen tube guidance and synergid cell
RT   differentiation in Arabidopsis.";
RL   Plant Cell 17:2981-2992(2005).
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].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11597504; DOI=10.1016/s1369-5266(00)00199-0;
RA   Stracke R., Werber M., Weisshaar B.;
RT   "The R2R3-MYB gene family in Arabidopsis thaliana.";
RL   Curr. Opin. Plant Biol. 4:447-456(2001).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=17693534; DOI=10.1105/tpc.107.052076;
RA   Punwani J.A., Rabiger D.S., Drews G.N.;
RT   "MYB98 positively regulates a battery of synergid-expressed genes encoding
RT   filiform apparatus localized proteins.";
RL   Plant Cell 19:2557-2568(2007).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=17937500; DOI=10.1371/journal.pgen.0030171;
RA   Jones-Rhoades M.W., Borevitz J.O., Preuss D.;
RT   "Genome-wide expression profiling of the Arabidopsis female gametophyte
RT   identifies families of small, secreted proteins.";
RL   PLoS Genet. 3:1848-1861(2007).
RN   [9]
RP   FUNCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=18410484; DOI=10.1111/j.1365-313x.2008.03514.x;
RA   Punwani J.A., Rabiger D.S., Lloyd A., Drews G.N.;
RT   "The MYB98 subcircuit of the synergid gene regulatory network includes
RT   genes directly and indirectly regulated by MYB98.";
RL   Plant J. 55:406-414(2008).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=23093426; DOI=10.1242/dev.081208;
RA   Iwano M., Ngo Q.A., Entani T., Shiba H., Nagai T., Miyawaki A., Isogai A.,
RA   Grossniklaus U., Takayama S.;
RT   "Cytoplasmic Ca2+ changes dynamically during the interaction of the pollen
RT   tube with synergid cells.";
RL   Development 139:4202-4209(2012).
CC   -!- FUNCTION: Transcription factor that binds to the motif 5'-GTAACNT-3' in
CC       the promoter of target genes (e.g. DD11 and DD18) and promotes their
CC       expression within synergid cells (e.g. in the filiform apparatus) in
CC       ovules (PubMed:16214903, PubMed:17693534, PubMed:18410484,
CC       PubMed:17937500). Required for the formation of the filiform apparatus
CC       during synergid cell differentiation in the female gametophyte
CC       (PubMed:16214903). Involved in pollen tube guidance to the micropyle
CC       (PubMed:16214903, PubMed:17937500, PubMed:23093426).
CC       {ECO:0000269|PubMed:16214903, ECO:0000269|PubMed:17693534,
CC       ECO:0000269|PubMed:17937500, ECO:0000269|PubMed:18410484,
CC       ECO:0000269|PubMed:23093426}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC       ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:17693534}.
CC       Note=Localized to the nuclei of the synergid cells.
CC       {ECO:0000269|PubMed:17693534}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in the synergid cells of
CC       the female gametophyte, and at lower levels in the endosperm of young
CC       seeds and the trichomes of young leaves and sepals.
CC       {ECO:0000269|PubMed:16214903, ECO:0000269|PubMed:17693534}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in cellularized but not uncellularized
CC       female gametophytes. {ECO:0000269|PubMed:16214903}.
CC   -!- DISRUPTION PHENOTYPE: Impaired in pollen tube attraction associated
CC       with a reduced cytoplasmic calcium burst during pollen tube tips
CC       growing (PubMed:17937500, PubMed:23093426). Altered expression of
CC       several ovule-specific genes (PubMed:17937500).
CC       {ECO:0000269|PubMed:17937500, ECO:0000269|PubMed:23093426}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK28639.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF176003; AAD53108.1; -; mRNA.
DR   EMBL; DQ198082; ABA42061.1; -; mRNA.
DR   EMBL; AL035526; CAB37462.1; -; Genomic_DNA.
DR   EMBL; AL161549; CAB78879.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84088.1; -; Genomic_DNA.
DR   EMBL; DQ446849; ABE66076.1; -; mRNA.
DR   EMBL; DQ653207; ABK28639.1; ALT_SEQ; mRNA.
DR   PIR; T04869; T04869.
DR   RefSeq; NP_193612.1; NM_117993.3.
DR   AlphaFoldDB; Q9S7L2; -.
DR   SMR; Q9S7L2; -.
DR   BioGRID; 12904; 4.
DR   STRING; 3702.AT4G18770.1; -.
DR   PaxDb; Q9S7L2; -.
DR   PRIDE; Q9S7L2; -.
DR   EnsemblPlants; AT4G18770.1; AT4G18770.1; AT4G18770.
DR   GeneID; 827611; -.
DR   Gramene; AT4G18770.1; AT4G18770.1; AT4G18770.
DR   KEGG; ath:AT4G18770; -.
DR   Araport; AT4G18770; -.
DR   TAIR; locus:2124162; AT4G18770.
DR   eggNOG; KOG0048; Eukaryota.
DR   HOGENOM; CLU_028567_9_0_1; -.
DR   InParanoid; Q9S7L2; -.
DR   OMA; CSYQENM; -.
DR   OrthoDB; 1499244at2759; -.
DR   PhylomeDB; Q9S7L2; -.
DR   PRO; PR:Q9S7L2; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9S7L2; baseline and differential.
DR   Genevisible; Q9S7L2; AT.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR   GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR   GO; GO:0010183; P:pollen tube guidance; IMP:UniProtKB.
DR   GO; GO:0045691; P:regulation of embryo sac central cell differentiation; IMP:UniProtKB.
DR   GO; GO:0045697; P:regulation of synergid differentiation; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   CDD; cd00167; SANT; 2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS51294; HTH_MYB; 2.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..427
FT                   /note="Transcription factor MYB98"
FT                   /id="PRO_0000234360"
FT   DOMAIN          212..267
FT                   /note="HTH myb-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          268..318
FT                   /note="HTH myb-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        240..263
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DNA_BIND        291..314
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   MOTIF           195..202
FT                   /note="Nuclear localization signal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   MOTIF           361..368
FT                   /note="Nuclear localization signal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   CONFLICT        82
FT                   /note="N -> T (in Ref. 2; ABA42061)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        96..97
FT                   /note="DF -> EL (in Ref. 2; ABA42061)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113
FT                   /note="V -> M (in Ref. 2; ABA42061)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="H -> HP (in Ref. 2; ABA42061)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        136
FT                   /note="Missing (in Ref. 2; ABA42061)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   427 AA;  50116 MW;  77E03B27C7A45538 CRC64;
     MENFVDENGF ASLNQNIFTR DQEHMKEEDF PFEVVDQSKP TSFLQDFHHL DHDHQFDHHH
     HHGSSSSHPL LSVQTTSSCI NNAPFEHCSY QENMVDFYET KPNLMNHHHF QAVENSYFTR
     NHHHHQEINL VDEHDDPMDL EQNNMMMMRM IPFDYPPTET FKPMNFVMPD EISCVSADND
     CYRATSFNKT KPFLTRKLSS SSSSSSWKET KKSTLVKGQW TAEEDRVLIQ LVEKYGLRKW
     SHIAQVLPGR IGKQCRERWH NHLRPDIKKE TWSEEEDRVL IEFHKEIGNK WAEIAKRLPG
     RTENSIKNHW NATKRRQFSK RKCRSKYPRP SLLQDYIKSL NMGALMASSV PARGRRRESN
     NKKKDVVVAV EEKKKEEEVY GQDRIVPECV FTDDFGFNEK LLEEGCSIDS LLDDIPQPDI
     DAFVHGL
 
 
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