SNL1_ARATH
ID SNL1_ARATH Reviewed; 1372 AA.
AC Q9SRH9;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Paired amphipathic helix protein Sin3-like 1;
GN Name=SNL1; OrderedLocusNames=At3g01320; ORFNames=T22N4.5;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH ALY2; ALY3; GATA21; TBP1; TRP2; TKI1; VAL1; SKP1B; FBX5 AND PUB14,
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19962994; DOI=10.1016/j.jmb.2009.11.065;
RA Bowen A.J., Gonzalez D., Mullins J.G., Bhatt A.M., Martinez A.,
RA Conlan R.S.;
RT "PAH-domain-specific interactions of the Arabidopsis transcription
RT coregulator SIN3-LIKE1 (SNL1) with telomere-binding protein 1 and ALWAYS
RT EARLY2 Myb-DNA binding factors.";
RL J. Mol. Biol. 395:937-949(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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).
CC -!- FUNCTION: Acts as a transcriptional repressor. An histone deacetylase
CC (HDAC) activity is required for transcription repression. May play a
CC role in telomere stability. {ECO:0000269|PubMed:19962994}.
CC -!- SUBUNIT: Interacts (via PAH3) with ALY2. Interacts (via PAH2) with
CC TBP1. Interacts with ALY3, GATA21, TRP2, TKI1, VAL1, SKP1B, FBX5 and
CC PUB14. {ECO:0000269|PubMed:19962994}.
CC -!- INTERACTION:
CC Q9SRH9; Q6A333: ALY2; NbExp=2; IntAct=EBI-2616294, EBI-2616358;
CC Q9SRH9; Q9FFY9: TRP4; NbExp=2; IntAct=EBI-2616294, EBI-2616485;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810,
CC ECO:0000269|PubMed:19962994}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SRH9-1; Sequence=Displayed;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF03494.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010676; AAF03494.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73639.1; -; Genomic_DNA.
DR RefSeq; NP_186781.4; NM_110998.5. [Q9SRH9-1]
DR AlphaFoldDB; Q9SRH9; -.
DR SMR; Q9SRH9; -.
DR BioGRID; 6598; 14.
DR IntAct; Q9SRH9; 13.
DR STRING; 3702.AT3G01320.1; -.
DR iPTMnet; Q9SRH9; -.
DR PaxDb; Q9SRH9; -.
DR PRIDE; Q9SRH9; -.
DR ProteomicsDB; 232626; -. [Q9SRH9-1]
DR EnsemblPlants; AT3G01320.1; AT3G01320.1; AT3G01320. [Q9SRH9-1]
DR GeneID; 821265; -.
DR Gramene; AT3G01320.1; AT3G01320.1; AT3G01320. [Q9SRH9-1]
DR KEGG; ath:AT3G01320; -.
DR Araport; AT3G01320; -.
DR TAIR; locus:2100277; AT3G01320.
DR eggNOG; KOG4204; Eukaryota.
DR InParanoid; Q9SRH9; -.
DR OMA; MFHDQRE; -.
DR OrthoDB; 253485at2759; -.
DR PRO; PR:Q9SRH9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRH9; baseline and differential.
DR Genevisible; Q9SRH9; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016580; C:Sin3 complex; IDA:TAIR.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR Gene3D; 1.20.1160.11; -; 3.
DR InterPro; IPR013194; HDAC_interact_dom.
DR InterPro; IPR003822; PAH.
DR InterPro; IPR036600; PAH_sf.
DR InterPro; IPR039774; Sin3-like.
DR InterPro; IPR031693; Sin3_C.
DR PANTHER; PTHR12346; PTHR12346; 1.
DR Pfam; PF02671; PAH; 3.
DR Pfam; PF08295; Sin3_corepress; 1.
DR Pfam; PF16879; Sin3a_C; 1.
DR SMART; SM00761; HDAC_interact; 1.
DR SUPFAM; SSF47762; SSF47762; 3.
DR PROSITE; PS51477; PAH; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1372
FT /note="Paired amphipathic helix protein Sin3-like 1"
FT /id="PRO_0000394040"
FT DOMAIN 51..121
FT /note="PAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 136..206
FT /note="PAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 331..400
FT /note="PAH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..992
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1014
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1049
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LFQ3"
SQ SEQUENCE 1372 AA; 156209 MW; 60E5F3E09F38B0C0 CRC64;
MKRIRDDVYA SGSQFRRPLG SSRGQLCGQS PVHGSGDTEE EEEGGSRRVS QKLTTNDALS
YLREVKEMFQ DQREKYDRFL EVMKDFKAQR TDTGGVIARV KELFKGHNNL IYGFNTFLPK
GYEITLIEED DALPKKTVEF EQAINFVNKI KMRFKHDEHV YKSFLEILNM YRKENKEIKE
VYNEVSILFQ GHLDLLEQFT RFLPASLPSH SAAQHSRSQA QQYSDRGSDP PLLHQMQVEK
ERRRERAVAL RGDYSVERYD LNDDKTMVKI QREQRKRLDK ENRARRGRDL DDREAGQDNL
HHFPEKRKSS RRAEALEAYS GSASHSEKDN LKSMYKQAFV FCEKVKDRLC SQDDYQTFLK
CLNIFSNGII QRKDLQNLVS DLLGKFPDLM DEFNQFFERC ESITDGFQRL AGVMSKKLFS
SEEQLSRPMK VEEKESEHKP ELEAVKETEQ CKKEYMGKSI QELDLSDCEC CTPSYRLLPA
DYPIPIASQR SELGAEVLND HWVSVTSGSE DYSFKHMRRN QYEESLFRCE DDRFELDMLL
ESVSSAARSA ESLLNIITEK KISFSGSFRI EDHFTALNLR CIERLYGDHG LDVIDILNKN
PATALPVILT RLKQKQGEWK KCRDDFDKVW ANVYAKNHYK SLDHRSFYFK QQDSKNLSAK
SLLAEIKELK EKSQNDDDVL LSISAGYRQP INPNLEYEYL NRAIHEDMFK VVQFSCEELC
STKEQLSKVL RLWENFLEAV LGVPPRAKGT DLVEDVVINP KTLDVNHSTS PNGEAAVSSG
GDTARLASRK LKSAANGDEN SSSGTFKHGI GLLNKDSTGK ENLEDVEIAN RDGVACSAVK
PQKEQETGNE AEKRFGKPIP MDISERAAIS SISIPSGAEN NHCVVGKEVL PGAHEIQAKP
SDTLTDIHHD VDSIETVHST QGGDVGNSIV LANGLRSDSS KGTRNSDDPE GPSRNEKEEG
ELSPNGDFED NFGVYKDHGV KSTSKPENSA EAEVEADAEV ENEDDADDVD SENASEASGT
ESGGDVCSQD EDREEENGEH DEIDGKAESE GEAEGMDPHL LEGESELLPQ SERVLLSVRP
LSKHVAAVLC DERTKDLQVF YGNDDFYVLF RLHQILYERI LYAKRNCSGG ELKSKNLKDT
NAGDPYARFM RVLYGLLDGS AENTKFEDEC RAIIGNQSYV LFTLDKLIYR LVKQLQAIVA
DEMDNKLLQL YEYEKSRKPG RVIDSVYYEN VRVLVHEENI YRLECSSLPS RLSIQLMDNI
IEKPEAYAVS MDPTFASYMQ TELLSVSSGK KEEGHDIVLQ RNLTGLYDLC KAMEGVEVVN
GLECKMSCSS YKIAYVLDTE DYFHRKKKKK KTEQLWQRNK VRVERFHRFL SA
