ID A0A7J8AQF1_MYOMY Unreviewed; 1275 AA.
AC A0A7J8AQF1;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 11.
DE RecName: Full=Paired amphipathic helix protein Sin3a {ECO:0000256|ARBA:ARBA00068512};
DE AltName: Full=Histone deacetylase complex subunit Sin3a {ECO:0000256|ARBA:ARBA00075105};
DE AltName: Full=Transcriptional corepressor Sin3a {ECO:0000256|ARBA:ARBA00081271};
GN ORFNames=mMyoMyo1_017494 {ECO:0000313|EMBL:KAF6388827.1};
OS Myotis myotis (Greater mouse-eared bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=51298 {ECO:0000313|EMBL:KAF6388827.1, ECO:0000313|Proteomes:UP000527355};
RN [1] {ECO:0000313|EMBL:KAF6388827.1, ECO:0000313|Proteomes:UP000527355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMyoMyo1 {ECO:0000313|EMBL:KAF6388827.1};
RC TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6388827.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- FUNCTION: Acts as a transcriptional repressor. Corepressor for REST.
CC Interacts with MXI1 to repress MYC responsive genes and antagonize MYC
CC oncogenic activities. Also interacts with MXD1-MAX heterodimers to
CC repress transcription by tethering SIN3A to DNA. Acts cooperatively
CC with OGT to repress transcription in parallel with histone
CC deacetylation. Involved in the control of the circadian rhythms.
CC Required for the transcriptional repression of circadian target genes,
CC such as PER1, mediated by the large PER complex through histone
CC deacetylation. Cooperates with FOXK1 to regulate cell cycle progression
CC probably by repressing cell cycle inhibitor genes expression. Required
CC for cortical neuron differentiation and callosal axon elongation.
CC {ECO:0000256|ARBA:ARBA00056268}.
CC -!- SUBUNIT: Interacts with ARID4B, BRMS1L, HCFC1, HDAC1, HDAC2, MXI1,
CC SAP30L, SAP130, SFPQ and TOPORS. Interacts with OGT (via TPRs 1-6); the
CC interaction mediates transcriptional repression in parallel with
CC histone deacetylase. Interacts with BAZ2A, MXD1, MXD3, MXD4, MBD2,
CC DACH1, NCOR1, NR4A2, REST, RLIM, SAP30, SETDB1, SMYD2, and SUDS3.
CC Interacts with PHF12 in a complex composed of HDAC1, PHF12 and SAP30.
CC Interacts with TET1; the interaction recruits SIN3A to gene promoters.
CC The large PER complex involved in the histone deacetylation is composed
CC of at least HDAC1, PER2, SFPQ and SIN3A. Interacts with KLF11.
CC Interacts with PPHLN1. Found in a complex with YY1, GON4L and HDAC1.
CC Interacts (via PAH2) with FOXK1. Interacts with FOXK2. Found in a
CC complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT
CC and TET1. Interacts with SINHCAF. Interacts with SPHK2.
CC {ECO:0000256|ARBA:ARBA00061761}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6388827.1}.
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DR EMBL; JABWUV010000001; KAF6388827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8AQF1; -.
DR VEuPathDB; HostDB:GeneID_118676090; -.
DR Proteomes; UP000527355; Unassembled WGS sequence.
DR GO; GO:0070822; C:Sin3-type complex; IEA:TreeGrafter.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR FunFam; 1.20.1160.11:FF:000001; Paired amphipathic helix protein Sin3; 1.
DR FunFam; 1.20.1160.11:FF:000002; Paired amphipathic helix protein SIN3; 1.
DR FunFam; 1.20.1160.11:FF:000004; Paired amphipathic helix protein Sin3a; 1.
DR Gene3D; 1.20.1160.11; Paired amphipathic helix; 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:SF2; PAIRED AMPHIPATHIC HELIX PROTEIN SIN3A; 1.
DR PANTHER; PTHR12346; SIN3B-RELATED; 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; PAH2 domain; 3.
DR PROSITE; PS51477; PAH; 3.
PE 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00810}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000527355};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 552..652
FT /note="Histone deacetylase interacting"
FT /evidence="ECO:0000259|SMART:SM00761"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 905..932
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 229..238
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..249
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..283
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..848
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1275 AA; 145274 MW; 2D7B4D3CC56F2DAB CRC64;
MKRRLDDQES PVYAAQQRRI PGNTEAFPHQ HRVLAPAPPV YEAVAETMQS ATGIQYSVTP
SYQVSAVPQG SGGSHGPTIA AVHSSHHHPT AVQPHGGQVV QSHAHPGPPV APVQGQQQFQ
RLKVEDALSY LDQVKLQFGS QPQVYNDFLD IMKEFKSQSI DTPGVISRVS QLFKGHPDLI
MGFNTFLPPG YKIEVQTNDM VNVTTPGQVH QIPTHGIQPQ PQPPPQHPSQ PSAQSAPAPA
QPAPQPPPAK VSKPSQLQAH TPASQQTPPL PPYASPRSPP VQPHTPVTIS LGTAPSLQNN
QPVEFNHAIN YVNKIKNRFQ GQPDIYKAFL EILHTYQKEQ RNAKEAGGNY TPALTEQEVY
AQVARLFKNQ EDLLSEFGQF LPDANSSVLL SKTTAEKVDS VRNDHGGTVK KPQLNNKPQR
PSQNGCQIRR HSGTGTTPPV KKKPKLLSLK DSSMADASKH GVGTESLFFD KVRKALRNAE
AYENFLRCLV IFNQEVISRA ELVQLVSPFL GKFPELFNWF KNFLGYKESV HLETFPKERA
TEGIAMEIDY ASCKRLGSSY RALPKSYQQP KCTGRTPLCK EVLNDTWVSF PSWSEDSTFV
SSKKTQYEEH IYRCEDERFE LDVVLETNLA TIRVLEAIQK KLSRLSAEEQ AKFRLDNTLG
GTSEVIHRKA LQRIYADKAA DIIDGLRKNP SIAVPIVLKR LKMKEEEWRE AQRGFNKVWR
EQNEKYYLKS LDHQGINFKQ NDTKVLRSKS LLNEIESIYD ERQEQATEEN AGVPAGPHLS
LAYEDKQILE DAAALIIHHV KRQAGIQKED KYKIKQIMHH FIPDLLFAQR GDLSDVEEEE
EEEMDVDEAT GVAKKHNGVG GSSPKSKLLF SNTTAQKLRG MDEVYNLFYV NNNWYIFMRL
HQILCLRLLR ICSQAERQIE EENREREWER EVLGIKRDKS DSPAIQLRLK EPMDVDVEDY
YPAFLDMVRS LLDGNIDSSQ YEDSLREMFT IHAYIAFTMD KLIQSIVRQL QHIVSDEICV
QVTDLYLAEN NNGATGGQLN TQTSRSLLES AYQRKAEQLM SEENCFKLMF IQSQGQVQLT
IELLDTEEEN SDDPVEAERW SDYVERYMNS DTTSPELREH LARKPVFLPR NLRRIRKCQR
GREQQEKEGK EGNSKKSMEN VDSLDKLECR FKLNSYKMVY VIKSEDYMYR RTALLRAHQS
HERVSKRLHQ RFQAWVDKWT KEHVPREMAA ETSKWLMGEG LEGLVPCTTT CDTETLHFVN
INKYRVKYGT VFKTP
//
