SNL3_ARATH
ID SNL3_ARATH Reviewed; 1330 AA.
AC O48686; Q0WTD6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Paired amphipathic helix protein Sin3-like 3;
DE AltName: Full=Histone deacetylase complex subunit Sin3;
DE Short=AtSin3;
DE AltName: Full=Transcriptional corepressor Sin3;
GN Name=SNL3; Synonyms=SIN3; OrderedLocusNames=At1g24190; ORFNames=F3I6.12;
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=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] OF 605-1330.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND INTERACTION WITH ERF7 AND HDA19.
RX PubMed=15994908; DOI=10.1105/tpc.105.033043;
RA Song C.-P., Agarwal M., Ohta M., Guo Y., Halfter U., Wang P., Zhu J.-K.;
RT "Role of an Arabidopsis AP2/EREBP-type transcriptional repressor in
RT abscisic acid and drought stress responses.";
RL Plant Cell 17:2384-2396(2005).
RN [5]
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).
CC -!- FUNCTION: Acts as a transcriptional repressor. Interacts with ERF7 to
CC repress genes in abscisic acid and drought stress responses. The
CC heterodimer represses transcription by tethering SNL3 to DNA.
CC {ECO:0000269|PubMed:15994908}.
CC -!- SUBUNIT: Interacts with ERF7 and the histone deacetylase HDA19.
CC {ECO:0000269|PubMed:15994908}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}.
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=O48686-1; Sequence=Displayed;
CC -!- DOMAIN: The PHA domains are required for interactions with ERF7 and
CC HDA19.
CC -!- MISCELLANEOUS: Loss-of-function mutant (antisense inhibition) leads to
CC abscisic acid hypersensitivity in germination.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00578.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002396; AAC00578.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30493.1; -; Genomic_DNA.
DR EMBL; AK227621; BAE99612.1; -; mRNA.
DR PIR; T00649; T00649.
DR RefSeq; NP_173829.3; NM_102265.3. [O48686-1]
DR AlphaFoldDB; O48686; -.
DR SMR; O48686; -.
DR BioGRID; 24270; 3.
DR IntAct; O48686; 1.
DR STRING; 3702.AT1G24190.1; -.
DR iPTMnet; O48686; -.
DR PaxDb; O48686; -.
DR PRIDE; O48686; -.
DR ProteomicsDB; 228450; -. [O48686-1]
DR EnsemblPlants; AT1G24190.1; AT1G24190.1; AT1G24190. [O48686-1]
DR GeneID; 839032; -.
DR Gramene; AT1G24190.1; AT1G24190.1; AT1G24190. [O48686-1]
DR KEGG; ath:AT1G24190; -.
DR Araport; AT1G24190; -.
DR TAIR; locus:2032382; AT1G24190.
DR eggNOG; KOG4204; Eukaryota.
DR InParanoid; O48686; -.
DR PRO; PR:O48686; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O48686; baseline and differential.
DR Genevisible; O48686; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
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:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
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..1330
FT /note="Paired amphipathic helix protein Sin3-like 3"
FT /id="PRO_0000280073"
FT DOMAIN 8..78
FT /note="PAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 94..164
FT /note="PAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 283..351
FT /note="PAH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT REGION 191..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 996
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LFQ3"
FT CONFLICT 1060
FT /note="Y -> C (in Ref. 3; BAE99612)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1330 AA; 151200 MW; 0BD7B6426BEFC277 CRC64;
MVGGGSAQKL TTNDALAYLK AVKDKFQDQR GKYDEFLEVM KNFKSQRVDT AGVITRVKEL
FKGHQELILG FNTFLPKGFE ITLQPEDGQP PLKKRVEFEE AISFVNKIKT RFQGDDRVYK
SFLDILNMYR RDSKSITEVY QEVAILFRDH SDLLVEFTHF LPDTSATASI PSVKTSVRER
GVSLADKKDR IITPHPDHDY GTEHIDQDRE RPIKKENKEH MRGTNKENEH RDARDFEPHS
KKEQFLNKKQ KLHIRGDDPA EISNQSKLSG AVPSSSTYDE KGAMKSYSQD LAIVDRVKEK
LNASEYQEFL RCLNLFSKEI ISRPELQSLV GNLIGVYPDL MDSFIEFLVQ CEKNEGLLSG
ILTKSKSTYL LQGEGKYPQP SLDNDRDQEH KRDDGLRDRD HEKERLEKAA ANLKWAKPIS
ELDLSNCEQC TPSYRLLPKN YPISIASQKT EIGKLVLNDH WVSVTSGSED YSFSHMRKNQ
YEESLFKCED DRFELDMLLE SVNSTTKHVE ELLTKINSNE LKTNSPIRVE DHLTALNLRC
IERLYGDHGL DVMDVLKKNV SLALPVILTR LKQKQEEWAR CRSDFDKVWA EIYAKNYYKS
LDHRSFYFKQ QDSKKLSMKA LLAEIKEITE KKREDDSLLA FAAGNRLSIS PDLEFDYPDH
DLHEDLYQLI KYSCAEMCST EQLDKVMKIW TTFVEQIFGV PSRPQGAEDQ EDVVKSMNQN
VKSGSSSAGE SEGSPHNYAS VADSRRSKSS RKANEHSQLG QTSNSERDGA AGRTSDALCE
TAQHEKMLKN VVTSDEKPES KQAVSIERAH DSTALAVDGL LDQSNGGSSI VHMTGHCNNN
LKPVTCGTEL ELKMNDGNGP KLEVGNKKLL TNGIAVEITS DQEMAGTSKV EREEGELSPN
GDFEEDNFAV YAKTDFETFS KANDSTGNNI SGDRSREGEP SCLETRAEND AEGDENAARS
SEDSRNEYEN GDVSGTESGG GEDPEDDLDN NNKGESEGEA ECMADAHDAE ENGSALPVSA
RFLLHVKPLV KYVPSAIALH DKDKDSLKNS QVFYGNDSFY VLFRLHRILY ERILSAKVNS
SSPEGKWRTS NTKNPTDSYA RFMTALYNLL DGTSDNAKFE DDCRAIIGTQ SYILFTLDKL
IHKFIKHLQV VVADEMDNKL LQLYFYEKSR RPETIFDAVY YDNTRVLLPD ENIYRIECRL
STPAKLSIQL MCNGLDKPDV TSVSIDPTFA AYLHNDFLSI QPNAREDRRI YLNRNKRKVC
REDEQLYSTD EVKIKNGLEC KIACGSSKVS YVLETEDLLV RVKKRRKTLC HNQDSWVRQM
RLQYYKNNFL
