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LG2_MAIZE
ID   LG2_MAIZE               Reviewed;         531 AA.
AC   O49067;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Transcription factor LG2 {ECO:0000303|PubMed:9490265};
DE   AltName: Full=Protein LIGULELESS 2 {ECO:0000303|PubMed:9490265};
DE   AltName: Full=Protein TGACG (TGA) motif-binding protein LG2 {ECO:0000303|PubMed:9490265};
GN   Name=LG2 {ECO:0000303|PubMed:9490265};
GN   ORFNames=GRMZM2G060216 {ECO:0000312|EMBL:AAO45627.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=9490265; DOI=10.1101/gad.12.2.208;
RA   Walsh J., Waters C.A., Freeling M.;
RT   "The maize gene liguleless2 encodes a basic leucine zipper protein involved
RT   in the establishment of the leaf blade-sheath boundary.";
RL   Genes Dev. 12:208-218(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73;
RX   PubMed=19965430; DOI=10.1126/science.1178534;
RA   Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA   Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA   Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA   Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA   Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA   Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA   Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA   Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA   Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA   Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA   Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA   Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA   Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA   Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA   Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA   Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA   Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA   Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA   Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA   Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA   SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA   Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA   Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA   Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA   Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA   Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT   "The B73 maize genome: complexity, diversity, and dynamics.";
RL   Science 326:1112-1115(2009).
CC   -!- FUNCTION: Required for the formation of the blade-sheath boundary in
CC       leaves. Promotes flowering. {ECO:0000269|PubMed:9490265}.
CC   -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000250|UniProtKB:Q39140}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC       ECO:0000255|PROSITE-ProRule:PRU00978}.
CC   -!- TISSUE SPECIFICITY: Expression in meristem/developing ligule regions.
CC       {ECO:0000269|PubMed:9490265}.
CC   -!- DISRUPTION PHENOTYPE: Defects in the formation of the blade-sheath
CC       boundary in leaves (e.g. absent or incorrectly positioned ligule and
CC       auricles) and delayed flowering. {ECO:0000269|PubMed:9490265}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR   EMBL; AF036949; AAC39351.1; -; mRNA.
DR   EMBL; AY180106; AAO45627.1; -; Genomic_DNA.
DR   PIR; T01415; T01415.
DR   RefSeq; NP_001104893.1; NM_001111423.1.
DR   AlphaFoldDB; O49067; -.
DR   STRING; 4577.GRMZM2G060216_P01; -.
DR   PaxDb; O49067; -.
DR   EnsemblPlants; Zm00001eb147220_T001; Zm00001eb147220_P001; Zm00001eb147220.
DR   GeneID; 541670; -.
DR   Gramene; Zm00001eb147220_T001; Zm00001eb147220_P001; Zm00001eb147220.
DR   KEGG; zma:541670; -.
DR   MaizeGDB; 219512; -.
DR   eggNOG; ENOG502QRFK; Eukaryota.
DR   HOGENOM; CLU_024782_0_2_1; -.
DR   Proteomes; UP000007305; Chromosome 3.
DR   ExpressionAtlas; O49067; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:1905623; P:positive regulation of leaf development; IMP:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR025422; TGA_domain.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF14144; DOG1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   PROSITE; PS51806; DOG1; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..531
FT                   /note="Transcription factor LG2"
FT                   /id="PRO_0000438996"
FT   DOMAIN          220..264
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   DOMAIN          285..499
FT                   /note="DOG1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01147"
FT   REGION          115..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..242
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          248..262
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   MOTIF           224..231
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        199..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   531 AA;  57680 MW;  C34353E459079BA1 CRC64;
     MVQGEESSWR MERAALPLNQ ALAYGVQAHA AAAAAPPTCF LDFQPAAASA AYFGFGELEE
     ALIHGGGAAS AGGGVDPGVI IKNDVAQAKS AAGYLAGAGT GRPPTLEIFP SWPMRHQQQL
     HSGNSQSVGS TGTDSSSAQN TMSQMELVSP ASSAPRQEVM MVTTDDYSYK PGLAAAPAAA
     APPSFQQHHP LPLQLHGGEG GGDHDKRKHG STRKDGKLVD AKTERRLAQN REAARKSRLR
     KKAYVQQLET SRIRLQQVEH ELQRARSQGL FVGGCSAAGD MSSGAAMFDM EYARWLDDDT
     KRLAELRGGL QAHLLDGNLG LIVEECMQHY DELFQLKAAL ARSDVFHLLT GSWATPAERC
     FFWMGGFRPS ELLKILIPQL DPLTEQQLLG ICNLQQSSEQ AEEALAQGLH QLHQSLADTV
     AAGTLNDGAA APNYMNIMAV ALEKLASLEN FYQQADNLRH QTLHQMRRIL TTRQAARCFL
     SIGEYYSRLR ALSNLWASRP RDNFIGTESL SPTATELQAL HHQQQNQFAG F
 
 
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