ASI1_ARATH
ID ASI1_ARATH Reviewed; 650 AA.
AC Q9LYE3; F4JXV7;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein ANTI-SILENCING 1 {ECO:0000303|PubMed:24003136};
DE AltName: Full=Protein INCREASE IN BONSAI METHYLATION 2 {ECO:0000303|PubMed:23934508};
DE AltName: Full=Protein SHOOT GROWTH 1 {ECO:0000303|PubMed:24404182};
GN Name=ASI1 {ECO:0000303|PubMed:24003136};
GN Synonyms=IBM2 {ECO:0000303|PubMed:23934508},
GN SG2 {ECO:0000303|PubMed:24404182};
GN OrderedLocusNames=At5g11470 {ECO:0000312|Araport:AT5G11470};
GN ORFNames=F15N18_60 {ECO:0000312|EMBL:CAB87707.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23934508; DOI=10.1038/ncomms3301;
RA Saze H., Kitayama J., Takashima K., Miura S., Harukawa Y., Ito T.,
RA Kakutani T.;
RT "Mechanism for full-length RNA processing of Arabidopsis genes containing
RT intragenic heterochromatin.";
RL Nat. Commun. 4:2301-2301(2013).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24003136; DOI=10.1073/pnas.1315399110;
RA Wang X., Duan C.-G., Tang K., Wang B., Zhang H., Lei M., Lu K.,
RA Mangrauthia S.K., Wang P., Zhu G., Zhao Y., Zhu J.-K.;
RT "RNA-binding protein regulates plant DNA methylation by controlling mRNA
RT processing at the intronic heterochromatin-containing gene IBM1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:15467-15472(2013).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24404182; DOI=10.1371/journal.pone.0084687;
RA Coustham V., Vlad D., Deremetz A., Gy I., Cubillos F.A., Kerdaffrec E.,
RA Loudet O., Bouche N.;
RT "SHOOT GROWTH1 maintains Arabidopsis epigenomes by regulating IBM1.";
RL PLoS ONE 9:E84687-E84687(2014).
CC -!- FUNCTION: Required to prevent promoter DNA hypermethylation and
CC transcriptional silencing of some transgenes (PubMed:24003136). Plays a
CC similar role to that of the histone H3K9 demethylase JMJ25/IBM1 in
CC preventing CHG methylation in the bodies of numerous genes. RNA-binding
CC protein that ensures the proper expression of JMJ25/IBM1 full-length
CC transcript by associating with an intronic heterochromatic repeat
CC element of JMJ25/IBM1 (PubMed:24003136, PubMed:23934508,
CC PubMed:24404182). May associate with intronic heterochromatin and bind
CC gene transcripts to promote their 3' distal polyadenylation
CC (PubMed:24003136). Contributes to a unique mechanism to deal with the
CC collateral effect of silencing intronic repeat elements
CC (PubMed:24003136, PubMed:23934508, PubMed:24404182).
CC {ECO:0000269|PubMed:23934508, ECO:0000269|PubMed:24003136,
CC ECO:0000269|PubMed:24404182}.
CC -!- DISRUPTION PHENOTYPE: Developmental defects, dwarf phenotype and short
CC siliques. DNA hypermethylation at genic regions.
CC {ECO:0000269|PubMed:23934508, ECO:0000269|PubMed:24003136}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87707.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163815; CAB87707.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; ANM69537.1; -; Genomic_DNA.
DR PIR; T48506; T48506.
DR RefSeq; NP_001331207.1; NM_001343194.1.
DR AlphaFoldDB; Q9LYE3; -.
DR STRING; 3702.AT5G11470.1; -.
DR PRIDE; Q9LYE3; -.
DR ProteomicsDB; 246502; -.
DR EnsemblPlants; AT5G11470.2; AT5G11470.2; AT5G11470.
DR GeneID; 831018; -.
DR Gramene; AT5G11470.2; AT5G11470.2; AT5G11470.
DR KEGG; ath:AT5G11470; -.
DR Araport; AT5G11470; -.
DR TAIR; locus:2144256; AT5G11470.
DR eggNOG; ENOG502QSH0; Eukaryota.
DR OMA; KIWQQNQ; -.
DR OrthoDB; 909309at2759; -.
DR PRO; PR:Q9LYE3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYE3; baseline and differential.
DR GO; GO:0032991; C:protein-containing complex; IPI:TAIR.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:1905642; P:negative regulation of DNA methylation; IMP:UniProtKB.
DR GO; GO:0044030; P:regulation of DNA methylation; IMP:TAIR.
DR GO; GO:0051570; P:regulation of histone H3-K9 methylation; IGI:TAIR.
DR GO; GO:0031060; P:regulation of histone methylation; IDA:TAIR.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF01426; BAH; 1.
DR SMART; SM00439; BAH; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS50102; RRM; 1.
PE 4: Predicted;
KW Chromatin regulator; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..650
FT /note="Protein ANTI-SILENCING 1"
FT /id="PRO_0000437259"
FT DOMAIN 38..169
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 486..569
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 202..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 72782 MW; 28924A837A39A595 CRC64;
MEESVASEGL EFKWGKKKGV GGKKKDVQFY ESFTYDGDEY RLYDCVLVGN ASEPDSTEPF
IGMIIKIWEH ANKHIPKKVK LLWFFKPSEI APYLEGVPNV LANEVFLASG EGLGLANTNQ
LEAIGGKCSV LCISKDKRNP QPSDEKFNSA DFVFCRAFDV GSCKVVDTID DKIAGVDVKF
IFNRACSEKE ATAVQNIEAD VNGKSDSLKP NGPLARGASG SVRKIEDSAF ESSDCKENSN
GCKEEKEKGH YQLAIKKSTL AEERSNKDSG SRGNHYNGKD QESEVKKQLT KQKSMPGEER
YSNSFEASGS RTIHSISKKA QENDVKKQLT KQKSMPAGER YSQESSGLDD RPLKKQKLDG
SVTVRDGWDT TILQNITSDG KKDTGSFKRP RDKVTIEEVP PEKRSFVKNR DLVVSVSEGK
TTKTVTEKGI SKKPSFGRAE DKMSADDNER NYQVTEVCRR PDAGKSKWFR SLPWEESMRE
AEKKGTVVLL QNLDPTYTSD EVEDIVYSAL NQQCEARMIE RTSVTIPHIG EALVIFKTRE
VAERVIRRLD EGCLLLSSGR PLVASFAKIT PPGKPSLFSG HIKLHKTQTR REMRDAVATS
HSSQPNNLEF DMAMEWCLHQ ARHEQASESV SKRQLEEMKS LRINFKLKLP
