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Database: UniProt
Entry: A0A1S3S4X8_SALSA
LinkDB: A0A1S3S4X8_SALSA
Original site: A0A1S3S4X8_SALSA 
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
//
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