LOCUS       NP_997108               1076 aa            linear   ROD 19-NOV-2024
DEFINITION  histone deacetylase 4 [Mus musculus].
ACCESSION   NP_997108 XP_136806
VERSION     NP_997108.1
DBSOURCE    REFSEQ: accession NM_207225.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1076)
  AUTHORS   Cheung,K.L., Zhao,L., Sharma,R., Ghosh,A.A., Appiah,M., Sun,Y.,
            Jaganathan,A., Hu,Y., LeJeune,A., Xu,F., Han,X., Wang,X., Zhang,F.,
            Ren,C., Walsh,M.J., Xiong,H., Tsankov,A. and Zhou,M.M.
  TITLE     Class IIa HDAC4 and HDAC7 cooperatively regulate gene transcription
            in Th17 cell differentiation
  JOURNAL   Proc Natl Acad Sci U S A 121 (18), e2312111121 (2024)
   PUBMED   38657041
  REMARK    GeneRIF: Class IIa HDAC4 and HDAC7 cooperatively regulate gene
            transcription in Th17 cell differentiation.
REFERENCE   2  (residues 1 to 1076)
  AUTHORS   Schneider,S., Anderson,J.B., Bradley,R.P., Beigel,K., Wright,C.M.,
            Maguire,B.A., Yan,G., Taylor,D.M., Harbour,J.W. and Heuckeroth,R.O.
  TITLE     BAP1 is required prenatally for differentiation and maintenance of
            postnatal murine enteric nervous system
  JOURNAL   J Clin Invest 134 (9), e177771 (2024)
   PUBMED   38690732
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1076)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   4  (residues 1 to 1076)
  AUTHORS   Xu,W., Jin,Q., Li,X., Li,D., Fu,X., Chen,N., Lv,Q., Shi,Y., He,S.,
            Dong,L., Yang,Y., Yan,Y. and Shi,F.
  TITLE     Crosstalk of HDAC4, PP1, and GSDMD in controlling pyroptosis
  JOURNAL   Cell Death Dis 15 (2), 115 (2024)
   PUBMED   38326336
  REMARK    GeneRIF: Crosstalk of HDAC4, PP1, and GSDMD in controlling
            pyroptosis.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1076)
  AUTHORS   Li,Y., Chen,Y., Xiao,X., Deng,S., Kuang,J. and Wang,Y.
  TITLE     CX3CL1 represses autophagy via CX3CR1/ CaMKIIdelta/HDAC4/Rubicon
            axis and exacerbates chronic intermittent hypoxia induced Kupffer
            cell apoptosis
  JOURNAL   Cell Signal 111, 110873 (2023)
   PUBMED   37640194
  REMARK    GeneRIF: CX3CL1 represses autophagy via CX3CR1/
            CaMKIIdelta/HDAC4/Rubicon axis and exacerbates chronic intermittent
            hypoxia induced Kupffer cell apoptosis.
REFERENCE   6  (residues 1 to 1076)
  AUTHORS   Chang,S., McKinsey,T.A., Zhang,C.L., Richardson,J.A., Hill,J.A. and
            Olson,E.N.
  TITLE     Histone deacetylases 5 and 9 govern responsiveness of the heart to
            a subset of stress signals and play redundant roles in heart
            development
  JOURNAL   Mol Cell Biol 24 (19), 8467-8476 (2004)
   PUBMED   15367668
REFERENCE   7  (residues 1 to 1076)
  AUTHORS   Jeong,B.C., Hong,C.Y., Chattopadhyay,S., Park,J.H., Gong,E.Y.,
            Kim,H.J., Chun,S.Y. and Lee,K.
  TITLE     Androgen receptor corepressor-19 kDa (ARR19), a leucine-rich
            protein that represses the transcriptional activity of androgen
            receptor through recruitment of histone deacetylase
  JOURNAL   Mol Endocrinol 18 (1), 13-25 (2004)
   PUBMED   14576337
REFERENCE   8  (residues 1 to 1076)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 1076)
  AUTHORS   Lemercier,C., Verdel,A., Galloo,B., Curtet,S., Brocard,M.P. and
            Khochbin,S.
  TITLE     mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A
            transcriptional activity
  JOURNAL   J Biol Chem 275 (20), 15594-15599 (2000)
   PUBMED   10748098
REFERENCE   10 (residues 1 to 1076)
  AUTHORS   Araki,K., Imaizumi,T., Sekimoto,T., Yoshinobu,K., Yoshimuta,J.,
            Akizuki,M., Miura,K., Araki,M. and Yamamura,K.
  TITLE     Exchangeable gene trap using the Cre/mutated lox system
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 45 (5), 737-750 (1999)
   PUBMED   10512203
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC163436.3, BY265337.1, BC066052.1 and AC109197.9.
            
            On Aug 30, 2004 this sequence version replaced XP_136806.3.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK155250.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMN00849374,
                                           SAMN00849375 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1076
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="1"
                     /map="1 46.24 cM"
     Protein         1..1076
                     /product="histone deacetylase 4"
                     /EC_number="3.5.1.98"
                     /calculated_mol_wt=118432
     Region          <90..151
                     /region_name="ClassIIa_HDAC4_Gln-rich-N"
                     /note="Glutamine-rich N-terminal helical domain of HDAC4,
                     a Class IIa histone deacetylase; cd10162"
                     /db_xref="CDD:197398"
     Site            order(92,96,107..108,111,118,122..123)
                     /site_type="other"
                     /note="dimer interface A, B [polypeptide binding]"
                     /db_xref="CDD:197398"
     Region          117..312
                     /region_name="Interaction with MEF2A.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Region          132..166
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Region          205..225
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Site            209
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Region          239..323
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Site            245
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4 and SIK1.
                     /evidence=ECO:0000269|PubMed:17468767; propagated from
                     UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Region          348..353
                     /region_name="PxLPxI/L motif, mediates interaction with
                     ANKRA2 and 14-3-3 proteins.
                     /evidence=ECO:0000250|UniProtKB:P56524"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Site            349
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Site            465
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4 and SIK1.
                     /evidence=ECO:0000269|PubMed:17468767,
                     ECO:0007744|PubMed:19131326; propagated from
                     UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Region          506..529
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Region          541..580
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Site            562
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Region          622..645
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Site            629
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by CaMK4.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Site            630
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P56524; propagated from
                     UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Region          646..1049
                     /region_name="HDAC4"
                     /note="Histone deacetylase 4; cd10006"
                     /db_xref="CDD:212530"
     Region          652..1076
                     /region_name="Histone deacetylase. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZM9.1)"
     Site            order(794..795,803..804,832,834,926,966)
                     /site_type="active"
                     /db_xref="CDD:212530"
     Region          1043..1076
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q6NZM9.1)"
     CDS             1..1076
                     /gene="Hdac4"
                     /gene_synonym="4932408F19Rik; HD4"
                     /coded_by="NM_207225.2:302..3532"
                     /db_xref="CCDS:CCDS48324.1"
                     /db_xref="GeneID:208727"
                     /db_xref="MGI:MGI:3036234"
ORIGIN      
        1 mssqshpdgl sgrdqpvell nparvnhmps tvdvatalpl qvaptavpmd lrldhqfslp
       61 lepalreqql qqellalkqk qqiqrqilia efqrqheqls rqheaqlheh ikqqqemlam
      121 khqqellehq rklerhrqeq elekqhreqk lqqlknkekg kesavastev kmklqefvln
      181 kkkalahrnl nhcissdpry wygktqhssl dqssppqsgv sasynhpvlg mydakddfpl
      241 rktasepnlk lrsrlkqkva errsspllrr kdgpvatalk krpldvtdsa cssapgsgps
      301 spnsssgnvs tengiaptvp sapaetslah rlvtregsva plplytspsl pnitlglpat
      361 gpaagaagqq daerlalpal qqrilfpgth ltpylstspl erdgaaahnp llqhmvlleq
      421 pptqtplvtg lgalplhsqs lvgadrvsps ihklrqhrpl grtqsaplpq naqalqhlvi
      481 qqqhqqflek hkqqfqqqql hlskiiskps epprqpeshp eeteeelreh qalldepyld
      541 rlpgqkepsl agvqvkqepi eseeeeaeat retepgqrpa teqellfrqq allleqqrih
      601 qlrnyqasme aagipvsfgs hrplsraqss pasatfpmsv qepptkprft tglvydtlml
      661 khqctcgntn shpehagriq siwsrlqetg lrgkcecirg rkatleelqt vhseahtlly
      721 gtnplnrqkl dssltsvfvr lpcggvgvds dtiwnevhss gaarlavgcv velvfkvatg
      781 elkngfavvr ppghhaeest pmgfcyfnsv avaakllqqr lnvskilivd wdvhhgngtq
      841 qafyndpnvl ymslhryddg nffpgsgapd evgtgpgvgf nvnmaftggl eppmgdaeyl
      901 aafrtvvmpi anefapdvvl vssgfdaveg hptplggynl sakcfgyltk qlmglaggrl
      961 vlalegghdl taicdaseac vsallgnele plpekvlhqr pnanavhsme kvmdihskyw
     1021 rclqrlsstv ghslieaqkc ekeeaetvta maslsvgvkp aekrseeepm eeeppl
//
