ID A0A1S3S4X8_SALSA Unreviewed; 1139 AA.
AC A0A1S3S4X8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
GN Name=LOC106607176 {ECO:0000313|RefSeq:XP_014059319.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014059319.1};
RN [1] {ECO:0000313|RefSeq:XP_014059319.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014059319.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC deacetylation gives a tag for epigenetic repression and plays an
CC important role in transcriptional regulation, cell cycle progression
CC and developmental events. {ECO:0000256|PIRNR:PIRNR037911}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000256|PIRNR:PIRNR037911};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037911}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007738,
CC ECO:0000256|PIRNR:PIRNR037911}.
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DR RefSeq; XP_014059319.1; XM_014203844.1.
DR AlphaFoldDB; A0A1S3S4X8; -.
DR GeneID; 106607176; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000087266; Chromosome ssa06.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd10164; ClassIIa_HDAC5_Gln-rich-N; 1.
DR CDD; cd10007; HDAC5; 1.
DR Gene3D; 6.10.250.1550; -; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR046949; HDAC4/5/7/9.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR017320; Histone_deAcase_II_euk.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF8; HISTONE DEACETYLASE 5; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF12203; HDAC4_Gln; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037911-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037911};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 98..186
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 721..1039
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 152..199
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 270..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 850
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 713
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 715
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 721
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 798
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 1023
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1139 AA; 124299 MW; 81C60C74C3E9ADBC CRC64;
MLLRPTVPGL CAMLQTIYET ESCFSSDAVS SRAQPLELLP QSQVSDMPSA AVEVKTTLPS
GMQSPVGGSE QGVGGGGGPV DLRTDPRLGP LGGGGGGVDP AMREQQLQHE LLLLKQQQEL
QKQLLFAEFQ KQHEVLTRQH EVQLQEHLKQ QQEILAAKRQ QELEQKRKLE QQRHEELEKQ
RLEQQLLMLR NKEKGKESAI ASTEVKLKLQ EFLLSKKEPG PPGGLNHSFP QKCWGAHHTS
LGPNSPPQSN TPGTPPSYKL PPLLGSYEGR DDFPLRKTAS EPNLKVRSRL KQKVAERRSS
PLLRRKDGTV ISTFKKRAIE ISVSSMCSSA PGSGPSSPNS SNSAIAENGS SGSVPNIHAE
QLRSLHQTLN ADGTVSPLSL YTSPSLPNIS LGLPANSHLT ANQKLLQEAE RQAIQTMRQG
GALTGKFVST SSLPASCLPP GMQHDLDSTQ APNSHSSHSS LLQHVLLLEQ ARQQSALLSV
PMYGQSPLVT GERVSNSMRT VNKLPRHRPL SRTQSAPLPQ SPQALQQLVM QQQHQQFLEK
QKQYQLNKIL SKGVELPRQP PTHPEETEEE LTETQEMQEE WAGSERLGEG RPQEQRLQKE
ESGETSPPSE RLLTPLKGES TESDLEEEDD EDEAIELREC DEEGVPYGQH HLQQLNVFQA
SLSISGMPHR PLGRAQSSPA TASIKGAPMG EVPIKHLFTT GLVYDTFMLK HQCMCGNTHI
HPEHAGRIQS VWSRLQETGL LGRCERIRGR KATLDEIQTV HSEYHTLLYG TSPLNRQKLD
SKKLLGPISQ KMYAVLPCGG IGVDSDTVWN EMHSSGAVRM AVGCVIELAF KVAAGELKNG
FAVVRPPGHH AEESTAMGFC FFNSVAITAK LLQQKLGVSK ILIVDWDIHH GNGTQQAFYN
DPNVLYISMH RYDDGNFFPG SGAPEEVGVG PGVGFNTNIA WTGGVEPPMG DVEYLTAFRT
VVMPIANEFS PDVVLVSAGF DAVEGHQSPL GGYNVTAKCF GHLTKQLMKL AGGRVVLALE
GGHDLTAICD ASESCVAALL GDELDPLPQA VLQQKPCPKA AASLERVIEI QSKHWSSLQR
LAPTVGQSLM DAQRREKDEA DTVTAMASLT VDTEQAAAST VSTETSRSTE EPMEEEPVL
//