SIN3_CAEEL
ID SIN3_CAEEL Reviewed; 1507 AA.
AC A5JYW9; O01319;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Paired amphipathic helix protein sin-3 {ECO:0000250|UniProtKB:O75182};
DE AltName: Full=Histone deacetylase complex subunit sin-3 {ECO:0000250|UniProtKB:O75182};
DE AltName: Full=Transcriptional corepressor sin-3 {ECO:0000250|UniProtKB:O75182};
GN Name=sin-3 {ECO:0000312|WormBase:F02E9.4b};
GN Synonyms=pqn-28 {ECO:0000303|PubMed:17506990};
GN ORFNames=F02E9.4 {ECO:0000312|WormBase:F02E9.4b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=16710447; DOI=10.1371/journal.pgen.0020074;
RA Cui M., Kim E.B., Han M.;
RT "Diverse chromatin remodeling genes antagonize the Rb-involved SynMuv
RT pathways in C. elegans.";
RL PLoS Genet. 2:E74-E74(2006).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17506990; DOI=10.1016/j.bbrc.2007.04.194;
RA Choy S.W., Wong Y.-M., Ho S.H., Chow K.L.;
RT "C. elegans SIN-3 and its associated HDAC corepressor complex act as
RT mediators of male sensory ray development.";
RL Biochem. Biophys. Res. Commun. 358:802-807(2007).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21909284; DOI=10.1371/journal.pgen.1002267;
RA Checchi P.M., Engebrecht J.;
RT "Caenorhabditis elegans histone methyltransferase MET-2 shields the male X
RT chromosome from checkpoint machinery and mediates meiotic sex chromosome
RT inactivation.";
RL PLoS Genet. 7:E1002267-E1002267(2011).
RN [5]
RP INTERACTION WITH ZTF-11.
RX PubMed=31386623; DOI=10.7554/elife.46703;
RA Lee J., Taylor C.A., Barnes K.M., Shen A., Stewart E.V., Chen A.,
RA Xiang Y.K., Bao Z., Shen K.;
RT "A Myt1 family transcription factor defines neuronal fate by repressing
RT non-neuronal genes.";
RL Elife 8:0-0(2019).
RN [6] {ECO:0000305}
RP IDENTIFICATION IN THE SIN3S COMPLEX, INTERACTION WITH CFP-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=31602465; DOI=10.1093/nar/gkz880;
RA Beurton F., Stempor P., Caron M., Appert A., Dong Y., Chen R.A., Cluet D.,
RA Coute Y., Herbette M., Huang N., Polveche H., Spichty M., Bedet C.,
RA Ahringer J., Palladino F.;
RT "Physical and functional interaction between SET1/COMPASS complex component
RT CFP-1 and a Sin3S HDAC complex in C. elegans.";
RL Nucleic Acids Res. 47:11164-11180(2019).
CC -!- FUNCTION: Probable transcriptional repressor required for the
CC deposition of dimethylated 'Lys-9' of histone H3 (H3K9me2) on asynapsed
CC chromosome pairs (both autosomes and sex chromosomes) during meiosis,
CC but this does not seem to solely affect the transcriptional status
CC (PubMed:21909284). Plays a role in ray fusion and patterning in the
CC male tail, and this may be through activity of the histone deacetylase
CC complex (HDAC) (PubMed:17506990). {ECO:0000269|PubMed:17506990,
CC ECO:0000269|PubMed:21909284, ECO:0000305|PubMed:21909284}.
CC -!- SUBUNIT: Component of the SIN3S complex, which contains at least sin-3,
CC hda-1, athp-1 and mrg-1 (PubMed:31602465). Interacts with ztf-11; the
CC interaction is weak (PubMed:31386623). Interacts with cfp-1
CC (PubMed:31602465). {ECO:0000269|PubMed:31386623,
CC ECO:0000269|PubMed:31602465}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:F02E9.4b};
CC IsoId=A5JYW9-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F02E9.4a};
CC IsoId=A5JYW9-2; Sequence=VSP_058573;
CC -!- TISSUE SPECIFICITY: Expressed in all ray structural cells including ray
CC 6, 7, 8 and 9 of the male tail. Also expressed in the inner labial
CC neurons, socket cells, the cephalic neurons in the head and the ventral
CC nerve cord. {ECO:0000269|PubMed:17506990}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the L1 stage of larval development
CC to adulthood. {ECO:0000269|PubMed:17506990}.
CC -!- DISRUPTION PHENOTYPE: Uncoordinated movement, protruding vulva and ray
CC fusion defects in the male tail (PubMed:17506990). RNAi-mediated
CC knockdown results in sterility (PubMed:16710447). RNAi-mediated
CC knockdown in a him-8 mutant background results in no deposition of
CC dimethylated 'Lys-9' of histone H3 (H3K9me2) on asynapsed chromosome
CC pairs (PubMed:21909284). {ECO:0000269|PubMed:16710447,
CC ECO:0000269|PubMed:17506990, ECO:0000269|PubMed:21909284}.
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DR EMBL; BX284601; CAB04052.2; -; Genomic_DNA.
DR EMBL; BX284601; CAN86581.1; -; Genomic_DNA.
DR PIR; T20513; T20513.
DR RefSeq; NP_001122442.1; NM_001128970.2. [A5JYW9-1]
DR RefSeq; NP_492284.2; NM_059883.5. [A5JYW9-2]
DR AlphaFoldDB; A5JYW9; -.
DR SMR; A5JYW9; -.
DR IntAct; A5JYW9; 17.
DR STRING; 6239.F02E9.4b; -.
DR iPTMnet; A5JYW9; -.
DR EPD; A5JYW9; -.
DR PaxDb; A5JYW9; -.
DR PeptideAtlas; A5JYW9; -.
DR PRIDE; A5JYW9; -.
DR EnsemblMetazoa; F02E9.4a.1; F02E9.4a.1; WBGene00004117. [A5JYW9-2]
DR EnsemblMetazoa; F02E9.4b.1; F02E9.4b.1; WBGene00004117. [A5JYW9-1]
DR GeneID; 172628; -.
DR KEGG; cel:CELE_F02E9.4; -.
DR UCSC; F02E9.4b; c. elegans.
DR CTD; 172628; -.
DR WormBase; F02E9.4a; CE33046; WBGene00004117; sin-3. [A5JYW9-2]
DR WormBase; F02E9.4b; CE40934; WBGene00004117; sin-3. [A5JYW9-1]
DR eggNOG; KOG4204; Eukaryota.
DR GeneTree; ENSGT00940000171042; -.
DR HOGENOM; CLU_242902_0_0_1; -.
DR InParanoid; A5JYW9; -.
DR OMA; HKNEISY; -.
DR OrthoDB; 253485at2759; -.
DR PhylomeDB; A5JYW9; -.
DR Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR SignaLink; A5JYW9; -.
DR PRO; PR:A5JYW9; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004117; Expressed in adult organism and 4 other tissues.
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; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0001708; P:cell fate specification; IMP:WormBase.
DR GO; GO:0098542; P:defense response to other organism; IGI:UniProtKB.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0090597; P:nematode male tail mating organ morphogenesis; IMP:WormBase.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IGI:UniProtKB.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR Gene3D; 1.20.1160.11; -; 1.
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; 1.
DR Pfam; PF08295; Sin3_corepress; 1.
DR Pfam; PF16879; Sin3a_C; 1.
DR SMART; SM00761; HDAC_interact; 1.
DR SUPFAM; SSF47762; SSF47762; 1.
DR PROSITE; PS51477; PAH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Repressor.
FT CHAIN 1..1507
FT /note="Paired amphipathic helix protein sin-3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437871"
FT DOMAIN 282..352
FT /note="PAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..445
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1378
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1417
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1063..1064
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058573"
SQ SEQUENCE 1507 AA; 171747 MW; FB1793888B158CB0 CRC64;
MYNPPPGGGG GNNGGDQSQQ QPTNNATLFL LQMIQQSQHQ QQHQNQQQQQ LELQIRDQER
ILIEQQRMQH QQQQNQLLQG LNQFPFNPLG LFQVQAAVQA AQAQFAQNAQ GSPIPFHIGS
PLQPSHSPAA SALQQQYLLP SHSPAITPFA RNSEAARNIE QFIAQEEAAN VPRANSQQQS
PLIRPIPQQQ ALNIQNLTST QQAQQILAHH RQVPVQQVQH QQHIPTPPLA LPIAQQGPIS
NEVPSVPPVV PATSAGCPQR EPRQQQGGRR QNRPGRRKKP EGPPRVDEAL AYLRVIKSTF
SSDVPVYHRF LEIMKDFRAQ RIETPDVIEQ VAELLYDSPE LVLGFNTFLP TGYRITLTPD
RKYVFSSPQM QPRVLLSPDE RRARAIEAGA QAVGAIELGS QEGISKDEDR TIEDEDMDKS
KEKDDVDGID DEDDEESGIE DKNNEEMMEE DNHLIEEIIC DDRKKDDCED SQQEIEMSSE
LAAHTLNIIE LLKKSFLARP TKLVDFMTFI DFFMSDQQYK KDMEKLRKDD EDDEIEENEK
IEVDDVPGPS NAPQEIKKPD DIEKKDSSKN LQIEESCSDY LVSMLANCCI GEPDLLAATI
DFLPYLGKLL VNGSDAIALK IKTILHFSAT NDRNDIPPVN RVNPSDVDMD LVKQMEKCKM
GTKKNEKLKL KVAGQGDEGA TVELMILKKS YRILYERLKS RTTPNQLSHL MVLINAYANL
DITREQLISE LPKIMGTSGS DLEMIILQLL GAEKEPKNRP ENDMDAVMRK DLPAIQPKRG
LRDQKMLQQV KNVEAATVCT LGPSYRFMKD TKATDCSGRV ELDDDLKGVL NDTWTSIPSW
SSEDTGSQAI KKSNLEEFHF KTEDERYELD IIVDSNRTVI EQLSKTLRDY EAMSDEDKKS
FKLDKWLNAS SRSTTIRVLA KVFTNSAQDF IDAAQKNPLV GLRRILESLK EKDLLWSRFQ
QDTNRTWRDA LDKQMSAATT ILNNQHKNYD QKAFKSKPLV NQIEQICEER RKNNSTDTSP
HLILEYTPER KVYRDVNDVT GHFFHDLSGT KCDRDRTKIV LFSYRILMEW LCQEGQQVQI
DLDNGEIFKF QGDLNEDENL MTLLNMDGRR ICGDRVVPVS TSLESNESSI DHFSENLHQK
RTRRTFYGDD SVYMIIRYHH MIQERFAKIL STQAIYAQEH FDNQKKNKRW EDGIGADMHG
RKALQENIKQ RRAAVNDIRN VRSCPSSSYE TTLRELKQLG NAQMDIVAFE EAVKNLFPGD
IVLFNNIDKL FSSLAKNIHH ATCAEERENP IKLYLKYRQR IMNAERDEDM ESVIQEYGQT
AEEVLRGKNT YRFEFVEEQN KPFIKIWVIP REEKDDDDDD DEEGNEGGKD EDNVKDEDDG
GDGEGRDGPD DDQPPPSNDD GDDEEDEDDE EDGPSGADEP ESTSGSGNVP MDHLNIGENF
LWSPPEEKVC TGKMTTNEKE QRNSVDYMKV TTTPRLRIHK RMLKEHKGCN VELMTGFQQL
SAIVPLM
