CHD5_MOUSE
ID CHD5_MOUSE Reviewed; 1946 AA.
AC A2A8L1; Q6ZQB2;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 5;
DE Short=CHD-5;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase CHD5;
GN Name=Chd5; Synonyms=Kiaa0444;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1245-1946.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP FUNCTION IN CELL PROLIFERATION.
RX PubMed=17289567; DOI=10.1016/j.cell.2006.11.052;
RA Bagchi A., Papazoglu C., Wu Y., Capurso D., Brodt M., Francis D.,
RA Bredel M., Vogel H., Mills A.A.;
RT "CHD5 is a tumor suppressor at human 1p36.";
RL Cell 128:459-475(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1556, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [5]
RP IDENTIFICATION IN A NURD-LIKE COMPLEX, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=21931736; DOI=10.1371/journal.pone.0024515;
RA Potts R.C., Zhang P., Wurster A.L., Precht P., Mughal M.R., Wood W.H.,
RA Zhang Y., Becker K.G., Mattson M.P., Pazin M.J.;
RT "CHD5, a brain-specific paralog of Mi2 chromatin remodeling enzymes,
RT regulates expression of neuronal genes.";
RL PLoS ONE 6:E24515-E24515(2011).
RN [6]
RP FUNCTION IN TRANSCRIPTION, UNMETHYLATED HISTONE H3K4-BINDING, PHD DOMAINS,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-346; GLY-355; ASP-361;
RP ASP-415; CYS-432 AND ASP-434.
RX PubMed=23318260; DOI=10.1016/j.celrep.2012.12.009;
RA Paul S., Kuo A., Schalch T., Vogel H., Joshua-Tor L., McCombie W.R.,
RA Gozani O., Hammell M., Mills A.A.;
RT "Chd5 requires PHD-mediated histone 3 binding for tumor suppression.";
RL Cell Rep. 3:92-102(2013).
RN [7]
RP FUNCTION IN NEURON DIFFERENTIATION, HISTONE H3K27ME3-BINDING, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=23948251; DOI=10.1016/j.devcel.2013.07.008;
RA Egan C.M., Nyman U., Skotte J., Streubel G., Turner S., O'Connell D.J.,
RA Rraklli V., Dolan M.J., Chadderton N., Hansen K., Farrar G.J., Helin K.,
RA Holmberg J., Bracken A.P.;
RT "CHD5 is required for neurogenesis and has a dual role in facilitating gene
RT expression and polycomb gene repression.";
RL Dev. Cell 26:223-236(2013).
RN [8]
RP FUNCTION IN SPERMATOGENESIS, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=24252660; DOI=10.1016/j.mod.2013.10.005;
RA Zhuang T., Hess R.A., Kolla V., Higashi M., Raabe T.D., Brodeur G.M.;
RT "CHD5 is required for spermiogenesis and chromatin condensation.";
RL Mech. Dev. 131:35-46(2014).
CC -!- FUNCTION: Chromatin-remodeling protein that binds DNA through histones
CC and regulates gene transcription. May specifically recognize and bind
CC trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone
CC H3. Plays a role in the development of the nervous system by activating
CC the expression of genes promoting neuron terminal differentiation. In
CC parallel, it may also positively regulate the trimethylation of histone
CC H3 at 'Lys-27' thereby specifically repressing genes that promote the
CC differentiation into non-neuronal cell lineages. Tumor suppressor, it
CC regulates the expression of genes involved in cell proliferation and
CC differentiation. Downstream activated genes may include CDKN2A that
CC positively regulates the p53/TP53 pathway, which in turn, prevents cell
CC proliferation. In spermatogenesis, it probably regulates histone
CC hyperacetylation and the replacement of histones by transition proteins
CC in chromatin, a crucial step in the condensation of spermatid chromatin
CC and the production of functional spermatozoa.
CC {ECO:0000269|PubMed:17289567, ECO:0000269|PubMed:23318260,
CC ECO:0000269|PubMed:23948251, ECO:0000269|PubMed:24252660}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: May be part of a nucleosome remodeling and histone
CC deacetylation, NuRD-like, complex composed at least of GATAD2B, HDAC1,
CC HDAC2 and MTA3. {ECO:0000269|PubMed:21931736}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23318260,
CC ECO:0000269|PubMed:23948251}. Note=Associates with heterochromatin.
CC -!- TISSUE SPECIFICITY: Specifically expressed by neurons in brain, retina
CC and adrenal gland (at protein level). Also detected in testis.
CC {ECO:0000269|PubMed:21931736, ECO:0000269|PubMed:23948251,
CC ECO:0000269|PubMed:24252660}.
CC -!- DEVELOPMENTAL STAGE: Detected at 15.5 dpc, expression increases after
CC birth and to adulthood. Expression increases in late-stage neuronal
CC progenitor during their terminal differentiation.
CC {ECO:0000269|PubMed:21931736, ECO:0000269|PubMed:23948251}.
CC -!- DOMAIN: The PHD domains mediate specific binding to histone H3
CC unmethylated at 'Lys-4' and may preferentially recruit the protein to
CC transcriptionally inactive genes. {ECO:0000269|PubMed:23318260}.
CC -!- DOMAIN: The chromo domains mediate specific binding to histone H3
CC trimethylated at 'Lys-27' (H3K27me3) and may be required in neuron
CC differentiation for proper gene regulation.
CC {ECO:0000269|PubMed:23948251}.
CC -!- PTM: Methylated at Gln-1392 by N6AMT1. {ECO:0000250|UniProtKB:Q8TDI0}.
CC -!- DISRUPTION PHENOTYPE: Mutant males are infertile. Mating occurs, but
CC the males are sterile, displaying abnormal spermatogenesis. Disruption
CC of the gene has no effect on the fertility of females. Infertility is
CC due to sperm morphological abnormalities and complete immotility that
CC are observed in all mice. A variable sperm counts, with a complete
CC absence is some individuals is also observed. Spermatogenesis is normal
CC from spermatogonia through meiotic division of spermatocytes. However,
CC at stage IX, step 9, abnormal nuclear morphology of differentiating
CC spermatids appears. It is associated with increased histone retention
CC and decreased histone H4 hyperacetylation, an important step in
CC spermatid chromatid condensation. Finally, spermiation is also
CC affected. {ECO:0000269|PubMed:24252660}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AL611985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK129145; BAC97955.1; -; mRNA.
DR CCDS; CCDS89866.1; -.
DR RefSeq; XP_006538995.1; XM_006538932.2.
DR AlphaFoldDB; A2A8L1; -.
DR SMR; A2A8L1; -.
DR BioGRID; 234678; 12.
DR IntAct; A2A8L1; 1.
DR STRING; 10090.ENSMUSP00000030775; -.
DR iPTMnet; A2A8L1; -.
DR PhosphoSitePlus; A2A8L1; -.
DR jPOST; A2A8L1; -.
DR MaxQB; A2A8L1; -.
DR PaxDb; A2A8L1; -.
DR PeptideAtlas; A2A8L1; -.
DR PRIDE; A2A8L1; -.
DR ProteomicsDB; 281603; -.
DR Antibodypedia; 27125; 139 antibodies from 29 providers.
DR Ensembl; ENSMUST00000005175; ENSMUSP00000005175; ENSMUSG00000005045.
DR MGI; MGI:3036258; Chd5.
DR VEuPathDB; HostDB:ENSMUSG00000005045; -.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000159249; -.
DR OrthoDB; 709631at2759; -.
DR PhylomeDB; A2A8L1; -.
DR BioGRID-ORCS; 269610; 6 hits in 74 CRISPR screens.
DR PRO; PR:A2A8L1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2A8L1; protein.
DR Bgee; ENSMUSG00000005045; Expressed in subiculum and 112 other tissues.
DR ExpressionAtlas; A2A8L1; baseline and differential.
DR Genevisible; A2A8L1; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0061628; F:H3K27me3 modified histone binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0021895; P:cerebral cortex neuron differentiation; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:GO_Central.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IMP:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR028727; CHD5.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF6; PTHR45623:SF6; 1.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06461; DUF1086; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Differentiation; DNA-binding; Helicase;
KW Hydrolase; Metal-binding; Methylation; Neurogenesis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Spermatogenesis;
KW Transcription; Transcription regulation; Tumor suppressor; Zinc;
KW Zinc-finger.
FT CHAIN 1..1946
FT /note="Chromodomain-helicase-DNA-binding protein 5"
FT /id="PRO_0000429326"
FT DOMAIN 499..556
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 594..655
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 714..898
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1030..1195
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 345..392
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 418..465
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..655
FT /note="Histone-binding"
FT /evidence="ECO:0000250"
FT REGION 551..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1353..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1926..1946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 849..852
FT /note="DEAH box"
FT COMPBIAS 15..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 727..734
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1392
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250|UniProtKB:Q8TDI0"
FT MOD_RES 1556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 346
FT /note="D->A: No effect on interaction with histone H3
FT unmethylated at 'Lys-4'. No significant effect on the
FT ability to repress target genes expression. No effect on
FT regulation of cell proliferation."
FT /evidence="ECO:0000269|PubMed:23318260"
FT MUTAGEN 355
FT /note="G->A: Loss of the ability to negatively regulate
FT cell proliferation."
FT /evidence="ECO:0000269|PubMed:23318260"
FT MUTAGEN 361
FT /note="D->A: Loss of interaction with histone H3
FT unmethylated at 'Lys-4'. Loss of the ability to repress
FT target genes expression. Loss of the ability to negatively
FT regulate cell proliferation."
FT /evidence="ECO:0000269|PubMed:23318260"
FT MUTAGEN 415
FT /note="D->A: Loss of interaction with histone H3
FT unmethylated at 'Lys-4'. Loss of the ability to negatively
FT regulate cell proliferation."
FT /evidence="ECO:0000269|PubMed:23318260"
FT MUTAGEN 432
FT /note="C->W: Loss of the ability to negatively regulate
FT cell proliferation."
FT /evidence="ECO:0000269|PubMed:23318260"
FT MUTAGEN 434
FT /note="D->A: Loss of interaction with histone H3
FT unmethylated at 'Lys-4'. Loss of the ability to repress
FT target genes expression. Loss of the ability to negatively
FT regulate cell proliferation."
FT /evidence="ECO:0000269|PubMed:23318260"
SQ SEQUENCE 1946 AA; 222515 MW; 5B94AB11A9C9BB03 CRC64;
MRGPLGTEEE LPRLFAEEME NEEEMSEEED GGLEGFEDFF PAEPVSLPKK KPKKLKESKS
SKGKRKKKEG SNDEMSDNEE DLEEKSESEG SDYSPTKKKK KKLKEKKEKK EKKEKRKKRG
EDEDDNDDGG LKEPKSSGQL MAEWGLDDVD YLFSEDDYHT LTNYKAFSQF LRPLIAKKNP
KIPMSKMMTV LGAKWREFSA NNPFKGSSAA AAAAAVAAAV ETVTIAPPLA ISPQQVPQTL
PIRKAKTKEG KGPGVRKKNK GAKDSKKKGR GKRVAGLKFR FGGISKRKKG SSSEEDERED
SDLDNASIHS SSVRSECSAA LGKKNKRRRK KKRIDDGDGY ETDHQDYCEV CQQGGEIILC
DTCPRAYHLV CLDPELEKAP EGKWSCPHCE KEGIQWEPKD DDEEEEEGGC EEEEDDHMEF
CRVCKDGGEL LCCDACPSSY HLHCLNPPLP EIPNGEWLCP RCTCPPLKGK VQRILHWRWT
EPPAPFVVGL PGPEVEPGMP PPRPLEGIPE REFFVKWAGL SYWHCSWVKE LQLELYHTVM
YRNYQRKNDM DEPPPFDYGS GDEDGKSEKR KNKDPLYAKM EERFYRYGIK PEWMMVHRIL
NHSFDKKGDI HYLIKWKDLP YDQCTWEIDE IDIPYYDNLK QAYWGHRELM LGEDARLPKR
LVKKGKKLKD DKQEKPPDTP IVDPTVKFDK QPWYIDATGG TLHPYQLEGL NWLRFSWAQG
TDTILADEMG LGKTVQTIVF LYSLYKEGHS KGPYLVSAPL STIINWEREF EMWAPDFYVV
TYTGDKESRS VIRENEFSFE DNAIRGGKKV FRMKKEVQIK FHVLLTSYEL ITIDQAILGS
IEWACLVVDE AHRLKNNQSK FFRVLNSYKI DYKLLLTGTP LQNNLEELFH LLNFLTPERF
NNLEGFLEEF ADISKEDQIK KLHDLLGPHM LRRLKADVFK NMPAKTELIV RVELSQMQKK
YYKFILTRNF EALNSKGGGN QVSLLNIMMD LKKCCNHPYL FPVAAVEAPV LPNGSYDGSS
LVKSSGKLML LQKMLKKLRD EGHRVLIFSQ MTKMLDLLED FLEYEGYKYE RIDGGITGGL
RQEAIDRFNA PGAQQFCFLL STRAGGLGIN LATADTVIIY DSDWNPHNDI QAFSRAHRIG
QNKKVMIYRF VTRASVEERI TQVAKRKMML THLVVRPGLG SKSGSMTKQE LDDILKFGTE
ELFKDDVEGM MSQGQRPTTP IPDIQSTKGG SLTAGAKKKH GSTPPGDNKD VEDSSVIHYD
DAAISKLLDR NQDATDDTEL QNMNEYLSSF KVAQYVVREE DGVEEVEREV IKQEENVDPD
YWEKLLRHHY EQQQEDLARN LGKGKRIRKQ VNYNDASQED QEWQDELSDN QSEYSIGSED
EDEDFEERPE GQSGRRQSRR QLKSDRDKPL PPLLARVGGN IEVLGFNARQ RKAFLNAIMR
WGMPPQDAFN SHWLVRDLRG KSEKEFRAYV SLFMRHLCEP GADGAETFAD GVPREGLSRQ
HVLTRIGVMS LVRKKVQEFE HVNGKYSTPD LVPEGAEGKK PGEVISSDPN TPVPASPAQL
PPAPLGLTDK MEAQLGYTDE KESGMQKPKK SLEIQTLPTA LDRVEGEDKH QSSDSKDRAR
EERTEEVEKA QGSPEQPLKE EVLPDKEPIP DKPELSLGHS GDFRPDDPKT EEKEPGETQQ
NGDREEDEEG KKEDKNGKFK FMFNIADGGF TELHTLWQNE ERAAVSSGKI YEIWHRRHDY
WLLAGIVTHG YARWQDIQND PRYMILNEPF KSEIHKGNYL EMKNKFLARR FKLLEQALVI
EEQLRRAAYL NMTQDPNHPA MALNARLAEV ECLAESHQHL SKESLAGNKP ANAVLHKVLN
QLEELLSDMK ADVTRLPSML SRIPPVAARL QMSERSILSR LTNRAGDPTI QQTSSRRRDF
PLFQRSFPAE PSHLPNPRGR EKLQPF
