ASIL1_ARATH
ID ASIL1_ARATH Reviewed; 383 AA.
AC Q9SYG2;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Trihelix transcription factor ASIL1 {ECO:0000305};
DE AltName: Full=6B-interacting protein 1-like 1 {ECO:0000303|PubMed:19155348};
DE AltName: Full=Trihelix DNA-binding protein ASIL1 {ECO:0000305};
GN Name=ASIL1 {ECO:0000303|PubMed:19155348};
GN OrderedLocusNames=At1g54060 {ECO:0000312|Araport:AT1G54060};
GN ORFNames=F15I1.14 {ECO:0000312|EMBL:AAD25778.1};
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 {ECO:0000312|EMBL:AAD25778.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19155348; DOI=10.1105/tpc.108.061309;
RA Gao M.J., Lydiate D.J., Li X., Lui H., Gjetvaj B., Hegedus D.D.,
RA Rozwadowski K.;
RT "Repression of seed maturation genes by a trihelix transcriptional
RT repressor in Arabidopsis seedlings.";
RL Plant Cell 21:54-71(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION.
RX PubMed=21330492; DOI=10.1104/pp.110.171355;
RA Willmann M.R., Mehalick A.J., Packer R.L., Jenik P.D.;
RT "MicroRNAs regulate the timing of embryo maturation in Arabidopsis.";
RL Plant Physiol. 155:1871-1884(2011).
RN [8]
RP FUNCTION.
RX PubMed=22231199; DOI=10.4161/psb.6.12.18709;
RA Gao M.J., Li X., Lui H., Gropp G.M., Lydiate D.D., Wei S., Hegedus D.D.;
RT "ASIL1 is required for proper timing of seed filling in Arabidopsis.";
RL Plant Signal. Behav. 6:1886-1888(2011).
CC -!- FUNCTION: Transcription repressor that binds specific DNA sequence such
CC as the GT-box-like motif 5'-CGTGATT-3' in the AT2S3 promoter. Negative
CC regulator of seed maturation genes during seed germination and seedling
CC development. May target GT-box-containing embryonic genes by competing
CC with the binding of transcriptional activators to this promoter region
CC (PubMed:19155348). Contributes to the maintenance and control of seed
CC filling (PubMed:22231199) and may repress the maturation program during
CC early embryogenesis (PubMed:21330492). {ECO:0000269|PubMed:19155348,
CC ECO:0000269|PubMed:21330492, ECO:0000269|PubMed:22231199}.
CC -!- INTERACTION:
CC Q9SYG2; Q8VZI9: At3g11100; NbExp=4; IntAct=EBI-4424669, EBI-1998580;
CC Q9SYG2; Q8GXR6: At3g58630/F14P22_220; NbExp=3; IntAct=EBI-4424669, EBI-4457957;
CC Q9SYG2; F4K0Q7: MOP10.9; NbExp=4; IntAct=EBI-4424669, EBI-15192203;
CC Q9SYG2; Q9LSI7: MYB35; NbExp=3; IntAct=EBI-4424669, EBI-25523050;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:19155348}.
CC -!- DEVELOPMENTAL STAGE: Induced by seed imbibition with a peak after 1
CC hour and then steadily decreases to be barely detectable at day 3.
CC {ECO:0000269|PubMed:19155348}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth of leaves, petioles, stems and
CC siliques. Delayed flowering. {ECO:0000269|PubMed:19155348}.
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DR EMBL; AC006577; AAD25778.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33042.1; -; Genomic_DNA.
DR EMBL; AF360325; AAK26035.1; -; mRNA.
DR EMBL; AY056333; AAL07182.1; -; mRNA.
DR EMBL; AY084772; AAM61340.1; -; mRNA.
DR PIR; C96581; C96581.
DR RefSeq; NP_564648.1; NM_104283.3.
DR AlphaFoldDB; Q9SYG2; -.
DR SMR; Q9SYG2; -.
DR BioGRID; 27069; 60.
DR IntAct; Q9SYG2; 62.
DR STRING; 3702.AT1G54060.1; -.
DR iPTMnet; Q9SYG2; -.
DR PaxDb; Q9SYG2; -.
DR PRIDE; Q9SYG2; -.
DR ProteomicsDB; 246860; -.
DR EnsemblPlants; AT1G54060.1; AT1G54060.1; AT1G54060.
DR GeneID; 841844; -.
DR Gramene; AT1G54060.1; AT1G54060.1; AT1G54060.
DR KEGG; ath:AT1G54060; -.
DR Araport; AT1G54060; -.
DR TAIR; locus:2014445; AT1G54060.
DR eggNOG; KOG4282; Eukaryota.
DR HOGENOM; CLU_042856_1_0_1; -.
DR InParanoid; Q9SYG2; -.
DR OMA; CKYAKTD; -.
DR OrthoDB; 1221690at2759; -.
DR PhylomeDB; Q9SYG2; -.
DR PRO; PR:Q9SYG2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYG2; baseline and differential.
DR Genevisible; Q9SYG2; AT.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0010431; P:seed maturation; IMP:TAIR.
DR InterPro; IPR044823; ASIL1/2-like.
DR InterPro; IPR044822; Myb_DNA-bind_4.
DR PANTHER; PTHR31307; PTHR31307; 1.
DR Pfam; PF13837; Myb_DNA-bind_4; 1.
PE 1: Evidence at protein level;
KW Coiled coil; DNA-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..383
FT /note="Trihelix transcription factor ASIL1"
FT /id="PRO_0000430502"
FT DOMAIN 94..153
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 304..365
FT /evidence="ECO:0000255"
FT MOTIF 228..241
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768,
FT ECO:0000303|PubMed:19155348"
FT COMPBIAS 208..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 41732 MW; D7AE4D93DAF2B1EC CRC64;
MEDDDEIQSI PSPGDSSLSP QAPPSPPILP TNDVTVAVVK KPQPGLSSQS PSMNALALVV
HTPSVTGGGG SGNRNGRGGG GGSGGGGGGR DDCWSEEATK VLIEAWGDRF SEPGKGTLKQ
QHWKEVAEIV NKSRQCKYPK TDIQCKNRID TVKKKYKQEK AKIASGDGPS KWVFFKKLES
LIGGTTTFIA SSKASEKAPM GGALGNSRSS MFKRQTKGNQ IVQQQQEKRG SDSMRWHFRK
RSASETESES DPEPEASPEE SAESLPPLQP IQPLSFHMPK RLKVDKSGGG GSGVGDVARA
ILGFTEAYEK AETAKLKLMA ELEKERMKFA KEMELQRMQF LKTQLEITQN NQEEEERSRQ
RGERRIVDDD DDRNGKNNGN VSS
