EZH1_MOUSE
ID EZH1_MOUSE Reviewed; 747 AA.
AC P70351; A2A4K5; Q3TPR1; Q3U3V5; Q3UU02; Q8BR85; Q922L1; Q9R089;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Histone-lysine N-methyltransferase EZH1;
DE EC=2.1.1.356 {ECO:0000269|PubMed:19026780};
DE AltName: Full=ENX-2;
DE AltName: Full=Enhancer of zeste homolog 1;
GN Name=Ezh1; Synonyms=Enx2;
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] (ISOFORM 1).
RX PubMed=9214638; DOI=10.1093/emboj/16.11.3219;
RA Laible G., Wolf A., Dorn R., Reuter G., Nislow C., Lebersorger A.,
RA Popkin D., Pillus L., Jenuwein T.;
RT "Mammalian homologues of the Polycomb-group gene Enhancer of zeste mediate
RT gene silencing in Drosophila heterochromatin and at S. cerevisiae
RT telomeres.";
RL EMBO J. 16:3219-3232(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=9473645; DOI=10.1016/s0167-4781(97)00156-5;
RA Ogawa M., Hiraoka Y., Taniguchi K., Aiso S.;
RT "Cloning and expression of a human/mouse Polycomb group gene, ENX-2/Enx-
RT 2.";
RL Biochim. Biophys. Acta 1395:151-158(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10051331; DOI=10.1007/s003359900993;
RA Laible G., Haynes A.R., Lebersorger A., O'Carroll D., Mattei M.-G.,
RA Denny P., Brown S.D.M., Jenuwein T.;
RT "The murine polycomb-group genes ezh1 and ezh2 map close to hox gene
RT clusters on mouse chromosomes 11 and 6.";
RL Mamm. Genome 10:311-314(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Aorta, Cerebellum, Corpora quadrigemina, Hippocampus, and Vein;
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
RX PubMed=19026780; DOI=10.1016/j.molcel.2008.10.016;
RA Shen X., Liu Y., Hsu Y.-J., Fujiwara Y., Kim J., Mao X., Yuan G.-C.,
RA Orkin S.H.;
RT "EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in
RT maintaining stem cell identity and executing pluripotency.";
RL Mol. Cell 32:491-502(2008).
RN [10]
RP IDENTIFICATION IN THE PRC2 COMPLEX.
RX PubMed=20144788; DOI=10.1016/j.stem.2009.12.014;
RA Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K., Torchia J.,
RA Krogan N.J., Reiter J.F., Stanford W.L.;
RT "Polycomb-like 2 associates with PRC2 and regulates transcriptional
RT networks during mouse embryonic stem cell self-renewal and
RT differentiation.";
RL Cell Stem Cell 6:153-166(2010).
RN [11]
RP INTERACTION WITH EZHIP.
RX PubMed=31451685; DOI=10.1038/s41467-019-11800-x;
RA Ragazzini R., Perez-Palacios R., Baymaz I.H., Diop S., Ancelin K.,
RA Zielinski D., Michaud A., Givelet M., Borsos M., Aflaki S., Legoix P.,
RA Jansen P.W.T.C., Servant N., Torres-Padilla M.E., Bourc'his D., Fouchet P.,
RA Vermeulen M., Margueron R.;
RT "EZHIP constrains Polycomb Repressive Complex 2 activity in germ cells.";
RL Nat. Commun. 10:3858-3858(2019).
CC -!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of the
CC PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading
CC to transcriptional repression of the affected target gene. Able to
CC mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1,
CC H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell
CC derivation and self-renewal, suggesting that it is involved in
CC safeguarding embryonic stem cell identity. Compared to EZH2-containing
CC complexes, it is less abundant in embryonic stem cells, has weak
CC methyltransferase activity and plays a less critical role in forming
CC H3K27me3, which is required for embryonic stem cell identity and proper
CC differentiation. {ECO:0000269|PubMed:19026780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-
CC COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356;
CC Evidence={ECO:0000269|PubMed:19026780};
CC -!- SUBUNIT: Component of the PRC2/EED-EZH1 complex, which includes EED,
CC EZH1, SUZ12, RBBP4 and AEBP2. The PRC2/EED-EZH1 is less abundant than
CC the PRC2/EED-EZH2 complex, has weak methyltransferase activity and
CC compacts chromatin in the absence of the methyltransferase cofactor S-
CC adenosyl-L-methionine (SAM). Interacts with EZHIP; the interaction
CC blocks EZH1 methyltransferase activity (PubMed:31451685).
CC {ECO:0000269|PubMed:19026780, ECO:0000269|PubMed:20144788,
CC ECO:0000269|PubMed:31451685}.
CC -!- INTERACTION:
CC P70351; Q62315: Jarid2; NbExp=4; IntAct=EBI-2531737, EBI-493592;
CC P70351; Q02395: Mtf2; NbExp=3; IntAct=EBI-2531737, EBI-2531578;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalizes with
CC trimethylated 'Lys-27' of histone H3. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P70351-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70351-2; Sequence=VSP_036388;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in kidney, adrenal gland,
CC testis and brain. {ECO:0000269|PubMed:9473645}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. EZ subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07135.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL90764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL90765.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA25018.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE23827.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE24446.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE32680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE37674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EDL03899.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U60453; AAC53279.1; -; mRNA.
DR EMBL; AB004817; BAA25018.1; ALT_INIT; mRNA.
DR EMBL; AF104360; AAD54021.1; -; Genomic_DNA.
DR EMBL; AF483490; AAL90764.1; ALT_INIT; mRNA.
DR EMBL; AF483491; AAL90765.1; ALT_INIT; mRNA.
DR EMBL; AK045374; BAC32334.1; -; mRNA.
DR EMBL; AK138942; BAE23827.1; ALT_INIT; mRNA.
DR EMBL; AK140694; BAE24446.1; ALT_INIT; mRNA.
DR EMBL; AK154565; BAE32680.1; ALT_INIT; mRNA.
DR EMBL; AK164192; BAE37674.1; ALT_INIT; mRNA.
DR EMBL; AL590969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466677; EDL03899.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC007135; AAH07135.1; ALT_INIT; mRNA.
DR RefSeq; NP_031996.1; NM_007970.3.
DR RefSeq; XP_006532241.1; XM_006532178.3. [P70351-1]
DR AlphaFoldDB; P70351; -.
DR SMR; P70351; -.
DR BioGRID; 199563; 19.
DR DIP; DIP-56992N; -.
DR IntAct; P70351; 8.
DR STRING; 10090.ENSMUSP00000102906; -.
DR iPTMnet; P70351; -.
DR PhosphoSitePlus; P70351; -.
DR EPD; P70351; -.
DR MaxQB; P70351; -.
DR PaxDb; P70351; -.
DR PeptideAtlas; P70351; -.
DR PRIDE; P70351; -.
DR ProteomicsDB; 275809; -. [P70351-1]
DR ProteomicsDB; 275810; -. [P70351-2]
DR Antibodypedia; 1432; 417 antibodies from 38 providers.
DR DNASU; 14055; -.
DR Ensembl; ENSMUST00000100417; ENSMUSP00000097984; ENSMUSG00000006920. [P70351-2]
DR Ensembl; ENSMUST00000107284; ENSMUSP00000102905; ENSMUSG00000006920. [P70351-1]
DR GeneID; 14055; -.
DR KEGG; mmu:14055; -.
DR UCSC; uc007lnw.3; mouse. [P70351-2]
DR UCSC; uc011yfk.2; mouse. [P70351-1]
DR CTD; 2145; -.
DR MGI; MGI:1097695; Ezh1.
DR VEuPathDB; HostDB:ENSMUSG00000006920; -.
DR eggNOG; KOG1079; Eukaryota.
DR GeneTree; ENSGT00940000156604; -.
DR HOGENOM; CLU_011342_0_0_1; -.
DR InParanoid; P70351; -.
DR OrthoDB; 875190at2759; -.
DR PhylomeDB; P70351; -.
DR TreeFam; TF314509; -.
DR BioGRID-ORCS; 14055; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Ezh1; mouse.
DR PRO; PR:P70351; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P70351; protein.
DR Bgee; ENSMUSG00000006920; Expressed in ciliary body and 249 other tissues.
DR ExpressionAtlas; P70351; baseline and differential.
DR Genevisible; P70351; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IGI:ARUK-UCL.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; IDA:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0046976; F:histone methyltransferase activity (H3-K27 specific); IDA:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:ARUK-UCL.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ARUK-UCL.
DR GO; GO:0036333; P:hepatocyte homeostasis; IGI:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:ARUK-UCL.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IGI:MGI.
DR GO; GO:0097421; P:liver regeneration; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1904772; P:response to tetrachloromethane; IGI:MGI.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IGI:ARUK-UCL.
DR CDD; cd00167; SANT; 1.
DR CDD; cd19217; SET_EZH1; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR026489; CXC_dom.
DR InterPro; IPR032926; EZH1.
DR InterPro; IPR045318; EZH1/2-like.
DR InterPro; IPR021654; EZH1/EZH2.
DR InterPro; IPR044438; EZH1_SET.
DR InterPro; IPR041343; PRC2_HTH_1.
DR InterPro; IPR041355; Pre-SET_CXC.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR033467; Tesmin/TSO1-like_CXC.
DR PANTHER; PTHR45747; PTHR45747; 1.
DR PANTHER; PTHR45747:SF1; PTHR45747:SF1; 1.
DR Pfam; PF11616; EZH2_WD-Binding; 1.
DR Pfam; PF18118; PRC2_HTH_1; 1.
DR Pfam; PF18264; preSET_CXC; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01114; CXC; 1.
DR SMART; SM00717; SANT; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51633; CXC; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Isopeptide bond;
KW Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation.
FT CHAIN 1..747
FT /note="Histone-lysine N-methyltransferase EZH1"
FT /id="PRO_0000213991"
FT DOMAIN 504..606
FT /note="CXC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00970"
FT DOMAIN 613..728
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 188..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 491..496
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 188..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92800"
FT VAR_SEQ 555..747
FT /note="QNRFPGCRCKTQCNTKQCPCYLAVRECDPDLCLTCGASEHWDCKVVSCKNCS
FT IQRGLKKHLLLAPSDVAGWGTFIKESVQKNEFISEYCGELISQDEADRRGKVYDKYMSS
FT FLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVVMVNGDHRIGIFAKRAIQAGEELF
FT FDYRYSQADALKYVGIERETDVF -> KSTLLSPSSTQVVGLGVPRLFSPAP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036388"
FT CONFLICT 84
FT /note="T -> A (in Ref. 5; BAE32680)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="H -> Y (in Ref. 2; AAD54021)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="N -> Y (in Ref. 2; AAD54021)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 85188 MW; 43CECFBDF3E49192 CRC64;
MDIASPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ EKTQILNEEW
KKLRVQPVQP MKPVSGHPFL KKCTIESIFP GFDSQDMLMR SLNTVALVPI MYSWSPLQQN
FMVEDETVLC NIPYMGDEVK EEDETFIEEL INNYDGKVHG EEEMIPGSVL ISDAVFLELV
DALNQYSDEE EDGHNDPSDG KQDDSKEDLP VTRKRKRHAI EGNKKSSKKQ FPNDMIFSAI
ASMFPENGVP DDMKERYREL TEMSDPNALP PQCTPNIDGP NAKSVQREQS LHSFHTLFCR
RCFKYDCFLH PFHATPNVYK RKNKEIKIEP EPCGTDCFLL LEGAKEYAML HNPRSKCSGR
RRRRHPVVSA SCSNASASAM AETKEGDSDR DTGNDWASSS SEANSRCQTP TKQKASPAPA
QLCVVEAPSE PVEWTGAEES LFRVFHGTYF NNFCSIARLL GTKTCKQVFQ FAVKESLILK
LPTDELMNPA QKKKRKHRLW AAHCRKIQLK KDNNSTQVYN YQPCDHPDRP CDSTCPCIMT
QNFCEKFCQC SPDCQNRFPG CRCKTQCNTK QCPCYLAVRE CDPDLCLTCG ASEHWDCKVV
SCKNCSIQRG LKKHLLLAPS DVAGWGTFIK ESVQKNEFIS EYCGELISQD EADRRGKVYD
KYMSSFLFNL NNDFVVDATR KGNKIRFANH SVNPNCYAKV VMVNGDHRIG IFAKRAIQAG
EELFFDYRYS QADALKYVGI ERETDVF
