ID A0A9D3SHE0_9TELE Unreviewed; 1864 AA.
AC A0A9D3SHE0;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
DE RecName: Full=Paired amphipathic helix protein Sin3a {ECO:0000256|ARBA:ARBA00068512};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
DE AltName: Full=Histone deacetylase complex subunit Sin3a {ECO:0000256|ARBA:ARBA00075105};
DE AltName: Full=Transcriptional corepressor Sin3a {ECO:0000256|ARBA:ARBA00081271};
DE AltName: Full=Tyrosine-protein phosphatase non-receptor type 9 {ECO:0000256|ARBA:ARBA00069781};
GN ORFNames=KOW79_012278 {ECO:0000313|EMBL:KAG7324262.1};
OS Hemibagrus wyckioides.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Bagridae; Hemibagrus.
OX NCBI_TaxID=337641 {ECO:0000313|EMBL:KAG7324262.1, ECO:0000313|Proteomes:UP000824219};
RN [1] {ECO:0000313|EMBL:KAG7324262.1, ECO:0000313|Proteomes:UP000824219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC202008001 {ECO:0000313|EMBL:KAG7324262.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAG7324262.1};
RA Shao F.;
RT "Chromosome-level genome assembly of the red-tail catfish (Hemibagrus
RT wyckioides).";
RL Submitted (JUN-2021) to the EMBL/GenBank/DDBJ databases.
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 -!- FUNCTION: Protein-tyrosine phosphatase that could participate in the
CC transfer of hydrophobic ligands or in functions of the Golgi apparatus.
CC {ECO:0000256|ARBA:ARBA00055430}.
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 3 subfamily. {ECO:0000256|ARBA:ARBA00060781}.
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:KAG7324262.1}.
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DR EMBL; JAHKSW010000014; KAG7324262.1; -; Genomic_DNA.
DR OrthoDB; 10265969at2759; -.
DR Proteomes; UP000824219; Miscellaneous, Linkage group lg14.
DR GO; GO:0070822; C:Sin3-type complex; IEA:TreeGrafter.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
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 CDD; cd14543; PTPc-N9; 1.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd22541; SP5_N; 1.
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 FunFam; 3.40.525.10:FF:000005; Tyrosine-protein phosphatase non-receptor type 9; 1.
DR FunFam; 3.90.190.10:FF:000026; tyrosine-protein phosphatase non-receptor type 9; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 1.
DR Gene3D; 1.20.1160.11; Paired amphipathic helix; 3.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR013194; HDAC_interact_dom.
DR InterPro; IPR003822; PAH.
DR InterPro; IPR036600; PAH_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR039774; Sin3-like.
DR InterPro; IPR031693; Sin3_C.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR12346:SF2; PAIRED AMPHIPATHIC HELIX PROTEIN SIN3A; 1.
DR PANTHER; PTHR12346; SIN3B-RELATED; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF02671; PAH; 3.
DR Pfam; PF08295; Sin3_corepress; 1.
DR Pfam; PF16879; Sin3a_C; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00761; HDAC_interact; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR SUPFAM; SSF47762; PAH2 domain; 3.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS51477; PAH; 3.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000824219};
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 74..233
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 289..559
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 466..550
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 652..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1624..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1731..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..848
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..877
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1443
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1637
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1733..1750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1864 AA; 212290 MW; BC400384F7E071B5 CRC64;
MAATLSAEEE QATKQFLEEI NKWTSQHGVS PLTWDVAVKF LMARKFDVLR AIELFHSYRE
TRLREGIVKL QPQEEPLRSE LLSGKFTVLG VRDPSGASIA LYTAKLHHPN KTGNHVVLQA
LFYLLDRAVE SFETQRNGLV FIYDMAGSNY TNFELDLSKK ILNLLKGAFP ARLKKVFIVG
APVWFRVPYN LLSLLLKEKL RERVQMVKMT DLRQHLPRTC LPEHLGGCLP LDVHGWNQRL
LVEQNGRVDP VDELLGVPLA TSAVHVPGPD AMRLPEFTAH LARAQRGGIY HEYEELRKEP
PSGTFHCALA AYNQEKNRYG DVLCLDQTRV RLKSRRNEKS DYINASFMDG YKQRNAYIGT
QGPLEKTYDD FWRMVWEQNV LVIVMTTRTD EGGRRKCGQY WPLQEGGQEV YGHIAVVNQR
VDNHSHYNQT ILELHNTETC EQRQVSHFQF LSWPDYGVPS SALSLLDFLS TVKKQQKRAV
KALGSQWRGH HLGPPMVVHC SAGIGRTGTF CALDICLSQL QDVGTLNVCQ TVRRMRTQRA
FSIQTPEQYY FCHTAILEHT QRQATSSHSA NSASLATARE VFVPLEYEFR MKRRLDDQDV
GFPAQQRRLT GGAEGFQHRV LAPAPTVYEA VADNVQPTSA IQYPVPQSYQ GGSLQVPTAA
QSSGGHGHTP TPAAHSSAHH HSSAVQPHGP ALVPSHTHPP NPTAPAPGQQ QFQRLKVEDA
LSYLDQVKLQ FGSQPQVYND FLDIMKEFKS QSIDTPGVIS RVSQLFKGHP DLIMGFNTFL
PPGYKIEVQT NDLVNVTTPG QIHHITPHGI SVQNIPPTAP AQHQSHLSAQ ASSTGTAPST
QPSQKSKPLQ PPALTPSSQP NPSIPPYASP RSPPLHPHTP VSSTPNAPPL QNNQPVEFNH
AINYVNKIKN RFQGQPDIYK AFLEILHTYQ KEQRNAKEAG GNYTPALTEQ EVYAQVARLF
KNQEDLLSEF GQFLPDASSS VLLGKTTAEK AESVQNDHGS TVKKPQLNNK QRPNQNGCQI
RRHSGSAATT PPVKKKPKLL NQKESSVVEA SKHGVGTESL FFEKVRKALR SAEAYDNFLR
CLVIFNQEVI SRAELVQLVL PFLGKFPELF TWFKNFLGYK EMSHLESYPK ERATEGIAME
IDYSSCKRLG FSYRALPKSY QQPKCTGRSP LCKEVLNDTW VSFPSWSEDS TFVSSKKTQY
EEHIYRCEDE RFELDVVLET NLATIRVLES VQKKLSRMSA EEQAKFRLDN TLGGTSEVIH
RKAIHRIYGD KALDIIDGLK KNPAVSVPIV LKRLKLKEDE WREAQRGFNK IWRQQNEKYY
LKSLDHQGIN FKQNDTKVLR SKTLLNEIES IYDERQEQAS EESGTPASGP HLTFTYEDRQ
ILEDAAALII HHVKRQTSIQ KEDKYKIKQI IHHFIPDMLF SQRGALSDAE EEEEDEEDAE
LDEGGSKKHN GVTGSPSKSK LLFTNTPAQK LRSCDDAYNL FFVNNNWYIF LRLHQTLCTR
LLRLYTQAER QIEEELKERD WEREVLGIKR EKNDNPAVQL RLKEPMDIDV EDYYSAFLEM
VRNLLDGNME ASQYEDSLRE MFTIHAYIAF TMDKLIQSIV RQLQHIVSDE ICVQVTDLYL
SESSSSATGG SLSSQATRST PESAYQRKAE QLMADENCFK LLFMKGHENV QLTIELLDTE
EENSDEQGDS ERWSDYVGRY LSADVTSPEL REHLAQKPVF LPRNLRRIRK CQRGREQQEK
DAKDGSKKEN AENMKMECMF KLNSYKMVYV FKSEDYMYRR TALLRAHQSH EHVSTRLHQR
FQAWLDGWLK EHVSRDMAND TTKWLMGEGH EGLISCTTTC DPETLHFRNI NKYRVKYSSS
YKTP
//
