HDAC5_MOUSE
ID HDAC5_MOUSE Reviewed; 1113 AA.
AC Q9Z2V6; Q9JL73;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Histone deacetylase 5;
DE Short=HD5;
DE EC=3.5.1.98;
DE AltName: Full=Histone deacetylase mHDA1;
GN Name=Hdac5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetus;
RX PubMed=9891014; DOI=10.1074/jbc.274.4.2440;
RA Verdel A., Khochbin S.;
RT "Identification of a new family of higher eukaryotic histone deacetylases.
RT Coordinate expression of differentiation-dependent chromatin modifiers.";
RL J. Biol. Chem. 274:2440-2445(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NCOR2.
RC STRAIN=C57BL/6J;
RX PubMed=10640276;
RA Kao H.-Y., Downes M., Ordentlich P., Evans R.M.;
RT "Isolation of a novel histone deacetylase reveals that class I and class II
RT deacetylases promote SMRT-mediated repression.";
RL Genes Dev. 14:55-66(2000).
RN [3]
RP INTERACTION WITH HDAC7, NUCLEAR EXPORT, AND MUTAGENESIS OF HIS-824 AND
RP HIS-884.
RX PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT "Identification of a nuclear domain with deacetylase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN [4]
RP INTERACTION WITH CTBP1 AND HDAC9.
RX PubMed=11022042; DOI=10.1074/jbc.m007364200;
RA Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.;
RT "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting
RT transcription repressor (MITR) contributes to transcriptional repression of
RT the MEF2 transcription factor.";
RL J. Biol. Chem. 276:35-39(2001).
RN [5]
RP INTERACTION WITH PHB2.
RX PubMed=15140878; DOI=10.1074/jbc.m312300200;
RA Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V., Seiser C.;
RT "Transcriptional regulation by the repressor of estrogen receptor activity
RT via recruitment of histone deacetylases.";
RL J. Biol. Chem. 279:24834-24843(2004).
RN [6]
RP INTERACTION WITH NRIP1.
RX PubMed=15060175; DOI=10.1093/nar/gkh524;
RA Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F.,
RA Khochbin S., Jalaguier S., Cavailles V.;
RT "Multiple domains of the receptor-interacting protein 140 contribute to
RT transcription inhibition.";
RL Nucleic Acids Res. 32:1957-1966(2004).
RN [7]
RP INTERACTION WITH MYOCD.
RX PubMed=15601857; DOI=10.1128/mcb.25.1.364-376.2005;
RA Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A.,
RA Wang D.Z., Olson E.N.;
RT "Modulation of smooth muscle gene expression by association of histone
RT acetyltransferases and deacetylases with myocardin.";
RL Mol. Cell. Biol. 25:364-376(2005).
RN [8]
RP PHOSPHORYLATION AT SER-250 AND SER-488, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF SER-250 AND SER-488.
RX PubMed=17468767; DOI=10.1038/nm1573;
RA Berdeaux R., Goebel N., Banaszynski L., Takemori H., Wandless T.,
RA Shelton G.D., Montminy M.;
RT "SIK1 is a class II HDAC kinase that promotes survival of skeletal
RT myocytes.";
RL Nat. Med. 13:597-603(2007).
RN [9]
RP INTERACTION WITH AHRR.
RX PubMed=17949687; DOI=10.1016/j.bbrc.2007.09.131;
RA Oshima M., Mimura J., Yamamoto M., Fujii-Kuriyama Y.;
RT "Molecular mechanism of transcriptional repression of AhR repressor
RT involving ANKRA2, HDAC4, and HDAC5.";
RL Biochem. Biophys. Res. Commun. 364:276-282(2007).
RN [10]
RP INTERACTION WITH GRK5, AND PHOSPHORYLATION.
RX PubMed=18711143; DOI=10.1073/pnas.0803153105;
RA Martini J.S., Raake P., Vinge L.E., DeGeorge B.R. Jr., Chuprun J.K.,
RA Harris D.M., Gao E., Eckhart A.D., Pitcher J.A., Koch W.J.;
RT "Uncovering G protein-coupled receptor kinase-5 as a histone deacetylase
RT kinase in the nucleus of cardiomyocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12457-12462(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP PHOSPHORYLATION AT SER-250 AND SER-488, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF SER-250 AND SER-488.
RX PubMed=21454484; DOI=10.1074/jbc.m110.199372;
RA Zhao J.X., Yue W.F., Zhu M.J., Du M.;
RT "AMP-activated protein kinase regulates beta-catenin transcription via
RT histone deacetylase 5.";
RL J. Biol. Chem. 286:16426-16434(2011).
RN [13]
RP INTERACTION WITH ZBTB7B.
RX PubMed=22730529; DOI=10.4049/jimmunol.1201077;
RA Rui J., Liu H., Zhu X., Cui Y., Liu X.;
RT "Epigenetic silencing of CD8 genes by ThPOK-mediated deacetylation during
RT CD4 T cell differentiation.";
RL J. Immunol. 189:1380-1390(2012).
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. Histone deacetylases act via the formation of
CC large multiprotein complexes. Involved in muscle maturation by
CC repressing transcription of myocyte enhancer MEF2C. During muscle
CC differentiation, it shuttles into the cytoplasm, allowing the
CC expression of myocyte enhancer factors (By similarity). Serves as a
CC corepressor of RARA and causes its deacetylation (By similarity). In
CC association with RARA, plays a role in the repression of microRNA-10a
CC and thereby in the inflammatory response (By similarity).
CC {ECO:0000250|UniProtKB:Q9UQL6}.
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 -!- SUBUNIT: Interacts with AHRR, BAHD1, BCOR, HDAC7, HDAC9, CTBP1, MEF2C,
CC NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein. Interacts with BCL6,
CC DDIT3/CHOP, GRK5, KDM5B and MYOCD. Interacts with EP300 in the presence
CC of TFAP2C. Interacts with ANKRA2. Interacts with CUL7 (as part of the
CC 3M complex); negatively regulated by ANKRA2. Interacts with ZBTB7B; the
CC interaction allows the recruitment of HDAC4 on CD8 loci for
CC deacetylation and possible inhibition of CD8 genes expression
CC (PubMed:22730529). Interacts with RARA (By similarity).
CC {ECO:0000250|UniProtKB:Q9UQL6, ECO:0000269|PubMed:10640276,
CC ECO:0000269|PubMed:10984530, ECO:0000269|PubMed:11022042,
CC ECO:0000269|PubMed:15060175, ECO:0000269|PubMed:15140878,
CC ECO:0000269|PubMed:15601857, ECO:0000269|PubMed:17949687,
CC ECO:0000269|PubMed:18711143, ECO:0000269|PubMed:22730529}.
CC -!- INTERACTION:
CC Q9Z2V6; P23242: Gja1; NbExp=2; IntAct=EBI-645339, EBI-298630;
CC Q9Z2V6; Q64104: Nr2e1; NbExp=3; IntAct=EBI-645339, EBI-15658561;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the
CC nucleus and the cytoplasm. In muscle cells, it shuttles into the
CC cytoplasm during myocyte differentiation. The export to cytoplasm
CC depends on the interaction with a 14-3-3 chaperone protein and is due
CC to its phosphorylation at Ser-250 and Ser-488 by AMPK, CaMK1 and SIK1.
CC -!- DOMAIN: The nuclear export sequence mediates the shuttling between the
CC nucleus and the cytoplasm.
CC -!- PTM: Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-250 and Ser-
CC 488. The phosphorylation is required for the export to the cytoplasm
CC and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2,
CC impairing nuclear import (By similarity). Phosphorylated by GRK5,
CC leading to nuclear export of HDAC5 and allowing MEF2-mediated
CC transcription. {ECO:0000250, ECO:0000269|PubMed:17468767,
CC ECO:0000269|PubMed:18711143, ECO:0000269|PubMed:21454484}.
CC -!- PTM: Ubiquitinated. Polyubiquitination however does not lead to its
CC degradation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; AF006602; AAD09834.2; -; mRNA.
DR EMBL; AF207748; AAF31418.1; -; mRNA.
DR AlphaFoldDB; Q9Z2V6; -.
DR SMR; Q9Z2V6; -.
DR CORUM; Q9Z2V6; -.
DR DIP; DIP-40855N; -.
DR ELM; Q9Z2V6; -.
DR IntAct; Q9Z2V6; 92.
DR MINT; Q9Z2V6; -.
DR STRING; 10090.ENSMUSP00000102770; -.
DR BindingDB; Q9Z2V6; -.
DR ChEMBL; CHEMBL2768; -.
DR iPTMnet; Q9Z2V6; -.
DR PhosphoSitePlus; Q9Z2V6; -.
DR MaxQB; Q9Z2V6; -.
DR PaxDb; Q9Z2V6; -.
DR PRIDE; Q9Z2V6; -.
DR ProteomicsDB; 269729; -.
DR MGI; MGI:1333784; Hdac5.
DR eggNOG; KOG1343; Eukaryota.
DR InParanoid; Q9Z2V6; -.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR ChiTaRS; Hdac5; mouse.
DR PRO; PR:Q9Z2V6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z2V6; protein.
DR GO; GO:0044295; C:axonal growth cone; IDA:CACAO.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0033558; F:protein lysine deacetylase activity; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:BHF-UCL.
DR GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
DR GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
DR GO; GO:0071498; P:cellular response to fluid shear stress; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR GO; GO:0007507; P:heart development; IGI:MGI.
DR GO; GO:0016575; P:histone deacetylation; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR GO; GO:0033555; P:multicellular organismal response to stress; IMP:MGI.
DR GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; ISO:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; TAS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR GO; GO:0002076; P:osteoblast development; IMP:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:BHF-UCL.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006476; P:protein deacetylation; ISO:MGI.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0010830; P:regulation of myotube differentiation; IDA:UniProtKB.
DR GO; GO:0043393; P:regulation of protein binding; ISO:MGI.
DR GO; GO:0048742; P:regulation of skeletal muscle fiber development; IGI:MGI.
DR GO; GO:1902809; P:regulation of skeletal muscle fiber differentiation; IGI:MGI.
DR GO; GO:0061333; P:renal tubule morphogenesis; IMP:UniProtKB.
DR GO; GO:0042220; P:response to cocaine; IDA:MGI.
DR Gene3D; 3.40.800.20; -; 1.
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; IPR030703; Histone_deacetylase_5.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364; PTHR45364; 1.
DR PANTHER; PTHR45364:SF2; PTHR45364:SF2; 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; SSF52768; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Cytoplasm; Hydrolase; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..1113
FT /note="Histone deacetylase 5"
FT /id="PRO_0000114702"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..1019
FT /note="Histone deacetylase"
FT REGION 1088..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1072..1113
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 240..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 824
FT /evidence="ECO:0000250"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 689
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 695
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 772
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 250
FT /note="Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1"
FT /evidence="ECO:0000269|PubMed:17468767,
FT ECO:0000269|PubMed:21454484"
FT MOD_RES 283
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT MOD_RES 488
FT /note="Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1"
FT /evidence="ECO:0000269|PubMed:17468767,
FT ECO:0000269|PubMed:21454484"
FT MOD_RES 523
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT MUTAGEN 250
FT /note="S->A: Abolishes phosphorylation by SIK1 and fails to
FT promote beta-catenin expression; when associated with A-
FT 488."
FT /evidence="ECO:0000269|PubMed:17468767,
FT ECO:0000269|PubMed:21454484"
FT MUTAGEN 488
FT /note="S->A: Abolishes phosphorylation by SIK1 and fails to
FT promote beta-catenin expression; when associated with A-
FT 250."
FT /evidence="ECO:0000269|PubMed:17468767,
FT ECO:0000269|PubMed:21454484"
FT MUTAGEN 824
FT /note="H->A: Abolishes deacetylase activity."
FT /evidence="ECO:0000269|PubMed:10984530"
FT MUTAGEN 884
FT /note="H->F: Disrupts the dot-like nuclear pattern."
FT /evidence="ECO:0000269|PubMed:10984530"
FT CONFLICT 7
FT /note="S -> SA (in Ref. 2; AAF31418)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="G -> E (in Ref. 2; AAF31418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1113 AA; 120942 MW; 63071AF45B87815A CRC64;
MNSPNESDGM SGREPSLGIL PRTPLHSIPV AVEVKPVLPG AMPSSMGGGG GGSPSPVELR
GALAGPMDPA LREQQLQQEL LVLKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ
QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR LEQQLLILRN KEKSKESAIA STEVKLRLQE
FLLSKSKEPT PGGLNHSLPQ HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK LPLLGPYDSR
DDFPLRKTAS EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE ITGTGPGVSS
VCNSAPGSGP SSPNSSHSTI AENGFTGSVP NIPTEMIPQH RALPLDSSPN QFSLYTSPSL
PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ GGTLTGKFMS TSSIPGCLLG
VALEGDTSPH GHASLLQHVC SWTGRQQSTL IAVPLHGQSP LVTGERVATS MRTVGKLPRH
RPLSRTQSSP LPQSPQALQQ LVMQQQHQQF LEKQKQQQMQ LGKILTKTGE LSRQPTTHPE
ETEEELTEQQ EALLGEGALT IPREGSTESE STQEDLEEEE EEEEEEEEDC IQVKDEDGES
GPDEGPDLEE SSAGYKKLFA DAQQLQPLQV YQAPLSLATV PHQALGRTQS SPAAPGSMKS
PTDQPTVVKH LFTTGVVYDT FMLKHQCMCG NTHVHPEHAG RIQSIWSRLQ ETGLLGKCER
IRGRKATLDE IQTVHSEYHT LLYGTSPLNR QKLDSKKLLG PISQKMYAML PCGGIGVDSD
TVWNEMHSSS AVRMAVGCLV ELAFKVAAGE LKNGFAIIRP PGHHAEESTA MGFCFFNSVA
ITAKLLQQKL SVGKVLIVDW DIHHGNGTQQ AFYNDPSVLY ISLHRYDNGN FFPGSGAPEE
VGGGPGVGYN VNVAWTGGVD PPIGDVEYLT AFRTVVMPIA QEFSPDVVLV SAGFDAVEGH
LSPLGGYSVT ARCFGHLTRQ LMTLAGGRVV LALEGGHDLT AICDASEACV SALLSVELQP
LDEAVLQQKP SVNAVATLEK VIEIQSKHWS CVQRFAAGLG CSLREAQTGE KEEAETVSAM
ALLSVGAEQA QAVATQEHSP RPAEEPMEQE PAL
