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LEC2_ARATH
ID   LEC2_ARATH              Reviewed;         363 AA.
AC   Q1PFR7; A0ME96; Q93VR5; Q9FZA3;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=B3 domain-containing transcription factor LEC2;
DE   AltName: Full=Protein LEAFY COTYLEDON 2;
GN   Name=LEC2; OrderedLocusNames=At1g28300; ORFNames=F3H9.5;
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 [GENOMIC DNA / MRNA], FUNCTION, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=11573014; DOI=10.1073/pnas.201413498;
RA   Stone S.L., Kwong L.W., Yee K.M., Pelletier J., Lepiniec L., Fischer R.L.,
RA   Goldberg R.B., Harada J.J.;
RT   "LEAFY COTYLEDON2 encodes a B3 domain transcription factor that induces
RT   embryo development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:11806-11811(2001).
RN   [2]
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   [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;
RX   PubMed=15208423; DOI=10.1104/pp.104.042176;
RA   Gong W., Shen Y.-P., Ma L.-G., Pan Y., Du Y.-L., Wang D.-H., Yang J.-Y.,
RA   Hu L.-D., Liu X.-F., Dong C.-X., Ma L., Chen Y.-H., Yang X.-Y., Gao Y.,
RA   Zhu D., Tan X., Mu J.-Y., Zhang D.-B., Liu Y.-L., Dinesh-Kumar S.P., Li Y.,
RA   Wang X.-P., Gu H.-Y., Qu L.-J., Bai S.-N., Lu Y.-T., Li J.-Y., Zhao J.-D.,
RA   Zuo J., Huang H., Deng X.-W., Zhu Y.-X.;
RT   "Genome-wide ORFeome cloning and analysis of Arabidopsis transcription
RT   factor genes.";
RL   Plant Physiol. 135:773-782(2004).
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   DISRUPTION PHENOTYPE.
RX   PubMed=12244265; DOI=10.2307/3869884;
RA   Meinke D.W., Franzmann L.H., Nickle T.C., Yeung E.C.;
RT   "Leafy cotyledon mutants of Arabidopsis.";
RL   Plant Cell 6:1049-1064(1994).
RN   [7]
RP   FUNCTION.
RX   PubMed=16492731; DOI=10.1073/pnas.0511331103;
RA   Braybrook S.A., Stone S.L., Park S., Bui A.Q., Le B.H., Fischer R.L.,
RA   Goldberg R.B., Harada J.J.;
RT   "Genes directly regulated by LEAFY COTYLEDON2 provide insight into the
RT   control of embryo maturation and somatic embryogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3468-3473(2006).
RN   [8]
RP   FUNCTION.
RX   PubMed=18287041; DOI=10.1073/pnas.0712364105;
RA   Stone S.L., Braybrook S.A., Paula S.L., Kwong L.W., Meuser J.,
RA   Pelletier J., Hsieh T.-F., Fischer R.L., Goldberg R.B., Harada J.J.;
RT   "Arabidopsis LEAFY COTYLEDON2 induces maturation traits and auxin activity:
RT   implications for somatic embryogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:3151-3156(2008).
RN   [9]
RP   GENE FAMILY.
RX   PubMed=18986826; DOI=10.1016/j.tplants.2008.09.006;
RA   Swaminathan K., Peterson K., Jack T.;
RT   "The plant B3 superfamily.";
RL   Trends Plant Sci. 13:647-655(2008).
CC   -!- FUNCTION: Transcription regulator that plays a central role in embryo
CC       development. Required for the maintenance of suspensor morphology,
CC       specification of cotyledon identity, progression through the maturation
CC       phase and suppression of premature germination. Ectopic expression is
CC       sufficient to promote somatic embryogenesis.
CC       {ECO:0000269|PubMed:11573014, ECO:0000269|PubMed:16492731,
CC       ECO:0000269|PubMed:18287041}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryo development.
CC       {ECO:0000269|PubMed:11573014}.
CC   -!- DISRUPTION PHENOTYPE: Pigmented seeds. Distorted seedlings with
CC       elongated hypocotyl and curled cotyledons. Presence of trichomes and
CC       accumulation of anthocyanins on cotyledons. Unusual pattern of storage
CC       product accumulation in seedlings. {ECO:0000269|PubMed:12244265}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF98425.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=ABK28418.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF400123; AAL12004.1; -; mRNA.
DR   EMBL; AF400124; AAL12005.1; -; Genomic_DNA.
DR   EMBL; AC021044; AAF98425.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE30945.1; -; Genomic_DNA.
DR   EMBL; AJ630496; CAG25869.1; -; mRNA.
DR   EMBL; AY568668; AAS79558.1; -; mRNA.
DR   EMBL; DQ446296; ABE65660.1; -; mRNA.
DR   EMBL; DQ652865; ABK28418.1; ALT_SEQ; mRNA.
DR   PIR; C86409; C86409.
DR   RefSeq; NP_564304.1; NM_102595.2.
DR   PDB; 6J9C; X-ray; 3.10 A; A/D=160-273.
DR   PDBsum; 6J9C; -.
DR   AlphaFoldDB; Q1PFR7; -.
DR   SMR; Q1PFR7; -.
DR   BioGRID; 24959; 1.
DR   STRING; 3702.AT1G28300.1; -.
DR   PaxDb; Q1PFR7; -.
DR   PRIDE; Q1PFR7; -.
DR   EnsemblPlants; AT1G28300.1; AT1G28300.1; AT1G28300.
DR   GeneID; 839724; -.
DR   Gramene; AT1G28300.1; AT1G28300.1; AT1G28300.
DR   KEGG; ath:AT1G28300; -.
DR   Araport; AT1G28300; -.
DR   TAIR; locus:2032170; AT1G28300.
DR   eggNOG; ENOG502S2IE; Eukaryota.
DR   HOGENOM; CLU_768029_0_0_1; -.
DR   InParanoid; Q1PFR7; -.
DR   OMA; MTKMARI; -.
DR   OrthoDB; 911852at2759; -.
DR   PhylomeDB; Q1PFR7; -.
DR   PRO; PR:Q1PFR7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q1PFR7; baseline and differential.
DR   Genevisible; Q1PFR7; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0010601; P:positive regulation of auxin biosynthetic process; IMP:TAIR.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR   GO; GO:0010431; P:seed maturation; IMP:TAIR.
DR   GO; GO:0010344; P:seed oilbody biogenesis; IMP:TAIR.
DR   GO; GO:0010262; P:somatic embryogenesis; IMP:TAIR.
DR   CDD; cd10017; B3_DNA; 1.
DR   Gene3D; 2.40.330.10; -; 1.
DR   InterPro; IPR003340; B3_DNA-bd.
DR   InterPro; IPR015300; DNA-bd_pseudobarrel_sf.
DR   InterPro; IPR044800; LEC2-like.
DR   PANTHER; PTHR31140; PTHR31140; 1.
DR   Pfam; PF02362; B3; 1.
DR   SMART; SM01019; B3; 1.
DR   SUPFAM; SSF101936; SSF101936; 1.
DR   PROSITE; PS50863; B3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..363
FT                   /note="B3 domain-containing transcription factor LEC2"
FT                   /id="PRO_0000375090"
FT   DNA_BIND        171..272
FT                   /note="TF-B3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00326"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        339..341
FT                   /note="SMP -> MT (in Ref. 1; AAL12004/AAL12005 and 4;
FT                   AAS79558/CAG25869)"
FT                   /evidence="ECO:0000305"
FT   STRAND          167..174
FT                   /evidence="ECO:0007829|PDB:6J9C"
FT   TURN            177..180
FT                   /evidence="ECO:0007829|PDB:6J9C"
FT   STRAND          185..188
FT                   /evidence="ECO:0007829|PDB:6J9C"
FT   HELIX           190..196
FT                   /evidence="ECO:0007829|PDB:6J9C"
FT   STRAND          206..211
FT                   /evidence="ECO:0007829|PDB:6J9C"
FT   STRAND          218..228
FT                   /evidence="ECO:0007829|PDB:6J9C"
FT   STRAND          231..237
FT                   /evidence="ECO:0007829|PDB:6J9C"
FT   HELIX           240..246
FT                   /evidence="ECO:0007829|PDB:6J9C"
FT   STRAND          253..262
FT                   /evidence="ECO:0007829|PDB:6J9C"
FT   STRAND          269..271
FT                   /evidence="ECO:0007829|PDB:6J9C"
SQ   SEQUENCE   363 AA;  41708 MW;  5CF6D8ABE53CD45A CRC64;
     MDNFLPFPSS NANSVQELSM DPNNNRSHFT TVPTYDHHQA QPHHFLPPFS YPVEQMAAVM
     NPQPVYLSEC YPQIPVTQTG SEFGSLVGNP CLWQERGGFL DPRMTKMARI NRKNAMMRSR
     NNSSPNSSPS ELVDSKRQLM MLNLKNNVQI SDKKDSYQQS TFDNKKLRVL CEKELKNSDV
     GSLGRIVLPK RDAEANLPKL SDKEGIVVQM RDVFSMQSWS FKYKFWSNNK SRMYVLENTG
     EFVKQNGAEI GDFLTIYEDE SKNLYFAMNG NSGKQNEGRE NESRERNHYE EAMLDYIPRD
     EEEASIAMLI GNLNDHYPIP NDLMDLTTDL QHHQATSSSM PPEDHAYVGS SDDQVSFNDF
     EWW
 
 
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