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 27-MAR-2024, entry version 179. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSMUSP00000008999; -. DR BindingDB; Q9Z2V6; -. DR ChEMBL; CHEMBL2768; -. DR GlyGen; Q9Z2V6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Z2V6; -. DR PhosphoSitePlus; Q9Z2V6; -. DR MaxQB; Q9Z2V6; -. DR PaxDb; 10090-ENSMUSP00000102770; -. DR ProteomicsDB; 269729; -. DR Pumba; Q9Z2V6; -. DR AGR; MGI:1333784; -. 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; TAS:UniProtKB. 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:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; ISO:MGI. 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; IDA:UniProtKB. 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: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: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:0045892; P:negative regulation of DNA-templated transcription; IDA: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: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: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:0010830; P:regulation of myotube differentiation; IDA:UniProtKB. 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 GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI. 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; IPR023696; Ureohydrolase_dom_sf. DR PANTHER; PTHR45364:SF11; HISTONE DEACETYLASE; 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 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 FT A-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 FT A-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 //