CHD6_MOUSE
ID CHD6_MOUSE Reviewed; 2711 AA.
AC A3KFM7; B9EKA7; Q3UQS6; Q80TE9;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 6;
DE Short=CHD-6;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase CHD6;
GN Name=Chd6; Synonyms=Kiaa1335;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1733 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-283 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17027977; DOI=10.1016/j.febslet.2006.09.049;
RA Lutz T., Stoger R., Nieto A.;
RT "CHD6 is a DNA-dependent ATPase and localizes at nuclear sites of mRNA
RT synthesis.";
RL FEBS Lett. 580:5851-5857(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1865, 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 [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=20111866; DOI=10.1007/s00335-010-9248-8;
RA Lathrop M.J., Chakrabarti L., Eng J., Rhodes C.H., Lutz T., Nieto A.,
RA Liggitt H.D., Warner S., Fields J., Stoger R., Fiering S.;
RT "Deletion of the Chd6 exon 12 affects motor coordination.";
RL Mamm. Genome 21:130-142(2010).
CC -!- FUNCTION: DNA-dependent ATPase that plays a role in chromatin
CC remodeling. Regulates transcription by disrupting nucleosomes in a
CC largely non-sliding manner which strongly increases the accessibility
CC of chromatin. Activates transcription of specific genes in response to
CC oxidative stress through interaction with NFE2L2.
CC {ECO:0000250|UniProtKB:Q8TD26}.
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 Evidence={ECO:0000250|UniProtKB:Q8TD26};
CC -!- SUBUNIT: Interacts with NFE2L2; involved in activation of the
CC transcription. {ECO:0000250|UniProtKB:Q8TD26}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q8TD26}. Note=Enriched at sites of mRNA
CC synthesis. {ECO:0000250|UniProtKB:Q8TD26}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A3KFM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A3KFM7-2; Sequence=VSP_054901;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17027977}.
CC -!- DISRUPTION PHENOTYPE: Mice with targeted deletion of exon 12 lacking
CC part of the Helicase ATP-binding domain are born in normal Mendelian
CC ratios and are viable. They are fertile and exhibit no obvious
CC morphological or histological difference. However, they display a
CC coordination deficiency which is not due to muscle weakness or
CC bradykinesia. {ECO:0000269|PubMed:20111866}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65778.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65778.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. Spurious priming from an intronic poly-A tract.; Evidence={ECO:0000305};
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DR EMBL; AL590430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150806; AAI50807.1; -; mRNA.
DR EMBL; AK142177; BAE24963.1; -; mRNA.
DR EMBL; AK122496; BAC65778.2; ALT_SEQ; mRNA.
DR CCDS; CCDS17000.1; -. [A3KFM7-1]
DR RefSeq; NP_775544.2; NM_173368.3. [A3KFM7-1]
DR RefSeq; XP_011238078.1; XM_011239776.2. [A3KFM7-2]
DR RefSeq; XP_017174747.1; XM_017319258.1. [A3KFM7-1]
DR SMR; A3KFM7; -.
DR BioGRID; 214679; 3.
DR IntAct; A3KFM7; 2.
DR MINT; A3KFM7; -.
DR STRING; 10090.ENSMUSP00000042291; -.
DR iPTMnet; A3KFM7; -.
DR PhosphoSitePlus; A3KFM7; -.
DR EPD; A3KFM7; -.
DR MaxQB; A3KFM7; -.
DR PaxDb; A3KFM7; -.
DR PeptideAtlas; A3KFM7; -.
DR PRIDE; A3KFM7; -.
DR ProteomicsDB; 281209; -. [A3KFM7-1]
DR ProteomicsDB; 281210; -. [A3KFM7-2]
DR Antibodypedia; 27058; 52 antibodies from 15 providers.
DR DNASU; 71389; -.
DR Ensembl; ENSMUST00000039782; ENSMUSP00000042291; ENSMUSG00000057133. [A3KFM7-1]
DR GeneID; 71389; -.
DR KEGG; mmu:71389; -.
DR UCSC; uc008nrn.2; mouse. [A3KFM7-1]
DR UCSC; uc008nrp.2; mouse. [A3KFM7-2]
DR CTD; 84181; -.
DR MGI; MGI:1918639; Chd6.
DR VEuPathDB; HostDB:ENSMUSG00000057133; -.
DR eggNOG; KOG0384; Eukaryota.
DR GeneTree; ENSGT00940000158986; -.
DR HOGENOM; CLU_000315_5_1_1; -.
DR InParanoid; A3KFM7; -.
DR OMA; SLENMMY; -.
DR OrthoDB; 7181at2759; -.
DR PhylomeDB; A3KFM7; -.
DR TreeFam; TF313572; -.
DR BioGRID-ORCS; 71389; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Chd6; mouse.
DR PRO; PR:A3KFM7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A3KFM7; protein.
DR Bgee; ENSMUSG00000057133; Expressed in substantia nigra and 243 other tissues.
DR ExpressionAtlas; A3KFM7; baseline and differential.
DR Genevisible; A3KFM7; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006576; BRK_domain.
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; 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 Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromatin regulator; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..2711
FT /note="Chromodomain-helicase-DNA-binding protein 6"
FT /id="PRO_0000429353"
FT DOMAIN 291..342
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 374..438
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 472..646
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 786..955
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1448..1502
FT /note="Myb-like"
FT REGION 1..746
FT /note="Required for DNA-dependent ATPase activity"
FT /evidence="ECO:0000250"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1951..1978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1997..2059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2124..2147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2321..2350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2373..2419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2550..2602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2641..2711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 597..600
FT /note="DEAH box"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2018..2037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2124..2145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2563..2581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2646..2662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2675..2691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2693..2711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 485..492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1865
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 184
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_054901"
FT CONFLICT 756
FT /note="K -> R (in Ref. 3; BAE24963)"
FT /evidence="ECO:0000305"
FT CONFLICT 1305
FT /note="L -> H (in Ref. 3; BAE24963)"
FT /evidence="ECO:0000305"
FT CONFLICT 1741
FT /note="I -> V (in Ref. 2; AAI50807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2711 AA; 305397 MW; 256A4983B8EA3544 CRC64;
MKMKIQKKEK QLSKLRALNH SPMSDASVNF DYKSPSPFDC SPDQGENIEE AANHCLPHKN
LYTTEEEADT LFSRKLTSHN GMEDSGGRGT GVKKKRKKKE PGEQEGTKGS KDREPKPKRK
REPKEPKEPR RAKEPKRAKE PKETKQKDGV KKPRKHREAS GTKEGKEKRS CTDYGSRTKS
KKASREQGPT PVERKKKGKR KNETTVESLE LDHSLPNPSL QSPEEPSESA DSQKRRSGRQ
VKRRKYNEDL DFKVVDDDGE TIAVLGAGRT SALSASTLAW QAEEPPEDDA NIIEKILASK
TVQEVHPGEP PFDLELFYVK YRNFSYLHCK WATMEELEKD PRIAQKIKRF RNKQAQMKHI
FTEPDEDLFN PDYIEIDRIL EVAHTKDAET GEEVTHYLVK WCSLPYEEST WELEEDVDPA
KVKEFESLQI LPEVKHVERP ASDAWQKLET SREYRNSNRL REYQLEGMNW LLFNWYNRKN
CILADEMGLG KTIQSIAFLS EIFVRGIHGP FLIIAPLSTI TNWEREFRTW TEMNAIVYHG
SQISRQMIQQ YEMVYRDAQG NPLSGVFKFH VVITTFEMIL ADCPELKKIH WSCVIIDEAH
RLKNRNCKLL EGLKLMALEH KVLLTGTPLQ NSVEELFSLL NFLEPSQFPS ETAFLEEFGD
LKTEEQVKKL QSILKPMMLR RLKDDVEKNL APKQETIIEV ELTNIQKKYY RAILEKNFSF
LTKGANQHNM PNLINTMMEL RKCCNHPYLI NGAEEKILED FRKAHSSEAS DFQLQAMIQA
AGKLVLIDKL LPKLIAGGHK VLIFSQMVRC LDILEDYLIQ RRYTYERIDG RVRGNLRQAA
IDRFCKPDSD RFVFLLCTRA GGLGINLTAA DTCIIFDSDW NPQNDLQAQA RCHRIGQSKA
VKVYRLITRN SYEREMFDKA SLKLGLDKAI LQDINRKGST NGVQQLSKME VEDLLRKGAY
GALMDEEDEG SKFCEEDIDQ ILQRRTHTIT IQSEGKGSTF AKASFVASGN RTDISLDDPN
FWQKWAKIAE LDTEANNEKE SLVIDRPRVR KQTKHYNSFE EDELMEFSEL DSDSDERPTR
SRRLSDRARR YLRAECFRVE KNLLIFGWGR WKDILTHGRF KWPLNEKDME MICRALLVYC
VKHYKGDEKI KSFIWELITP SKDGQVQTLQ NHSGLSAPVP RGRKGKKTKN QLLLPELKNA
DWLATCNPEV VLHDDGYKKH LKQHCNKVLL RVRMLYYLKA EILGEAADKA FEGTPARELD
VLLPDIDYVE IPVDWWDAEA DKSLLIGVFK HGYERYNAMR ADPALCFLEK VGMPDEKSLS
AEQGVTDGTS DIPERGNIDK EDSAEDKLDG LQKQTASPSD GSDGIFGEKK DDSQAAQDGS
DPDKSPWPVS SALTARLRRL VTIYQRCNRK ELCRPEILGP GNQGYWVQEE VFRRTSEMDL
INKEAQKRWT RREQADFYRT VSSFGVVYDQ EKKAFDWTQF RIISRLDKKS DESLEHYFYS
FVAMCRNVCR LPAWKDDGPP DASIYVEPIT EERAAKTLYR IELLRKVREQ VLMCPQLHER
LQLCRPSLYL PVWWECGKHD RDLLIGTAKH GLNRTDYYIM NDPQLSFLDA YRNYAQHKRT
DTQAPGSLCC LYQSNSKLYE SLTYTPVSRT SESLESEPEN LMRMESRDDH LCLPEGGLPD
ITCENFVSKV QEVISLDHDE NLLPESLENM IYGKTGLSQE PHSFQEAPTT NTQSRKNTIT
ISASRNESCQ PPGIEAEITS ASSLMSSLEA GVAKMNIKNG KHLLVSISKE GEPCCSETGR
RPETIGHREA KCLVSPTLDT GHESGFVDLC SLSVYDPKRN FSSDQQLIDL LENKSLESKL
ILNQSDEEEE ENEDETLAIV ASATEKPEVL DFPKPTVNIP RGKNLSFHQD EAKKGRLEVV
SKTAGPQRVF PPPANQCHCK HIERWAHGLG SEDSEVEKPK AYQPDLYRSK ANNSTVEGET
AVIPTEPFKL KHELLKEPWK ESSEGGKSFS MYAPEGSEPK PEDMDFENKD DYEKDGTCLS
QDYPGKYSEE ESKSSASGIA GDLGEEAQEV RAPTIAQLLQ EKTLYSFSEW PKDRVIINRL
DNICHVVLKG KWPCSHQYEP SGALPTPVLS SSAGSRSSLS EPEATEHGFS NGAALAAQIQ
KESFLAPVFT KDEQKHRRPY EFEVERDAKA RSLEEYSATH GRPPIVLNGW HGESAIDLSC
SSEGSPGATS PFPVSASTPK IGAISSLQGA LGMDLSGILQ AGLIHPVTGQ IVNGSLRRDD
AAMRRRRGRR KHIEGGMDLI FLKEQTLQAG ILEVHEDAGQ TTLSTTHPEV PGATSSAPEP
TAAASSQAEK AVPSKSLLDW LRQQADYSLD VPGFGTSFSD KPKQRRPRCK EPGKLDISSL
GGEERVPAVP KEPGLRGFLP ESKFNHTLAE PVLRDAGPRR RGRRPRNELL KAPAIVADSP
SGMGPLFMNG LIAGMDLVGL QNVRNIPGIP LTGLVGFPAG FATMPTGEEV KNTLSMLPMM
LPGMAAVPQM FGVGGLLNTP MATTCTTTAS ASLASTKSGT SATEKSTEDK LSGHDVNTDA
LVDDKPGPSP FSDQSEPTIT TSSPVAFNPF LIPGVSPGLI YPSMFLSPGM GMALPAMQQA
RHSEMVGLET QKRKKKKTKG DSPTQEPASV CEKEPGSDQN CTESSATVSP EREHVAQARE
EGLKDSNEDT N
