SMYD1_HUMAN
ID SMYD1_HUMAN Reviewed; 490 AA.
AC Q8NB12; A0AV30; A6NE13;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Histone-lysine N-methyltransferase SMYD1;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:P97443};
DE AltName: Full=SET and MYND domain-containing protein 1;
GN Name=SMYD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000312|EMBL:BAC03732.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP TISSUE SPECIFICITY, AND INDUCTION BY SRF.
RX PubMed=19783823; DOI=10.1093/nar/gkp773;
RA Li D., Niu Z., Yu W., Qian Y., Wang Q., Li Q., Yi Z., Luo J., Wu X.,
RA Wang Y., Schwartz R.J., Liu M.;
RT "SMYD1, the myogenic activator, is a direct target of serum response factor
RT and myogenin.";
RL Nucleic Acids Res. 37:7059-7071(2009).
CC -!- FUNCTION: Methylates histone H3 at 'Lys-4' (H3K4me), seems able to
CC perform both mono-, di-, and trimethylation. Acts as a transcriptional
CC repressor. Essential for cardiomyocyte differentiation and cardiac
CC morphogenesis. {ECO:0000250|UniProtKB:P97443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000250|UniProtKB:P97443};
CC -!- SUBUNIT: Interacts with HDAC1, HDAC2 and HDAC3. Interacts (via MYND-
CC type zinc finger) with NACA isoform skNAC.
CC {ECO:0000250|UniProtKB:P97443}.
CC -!- INTERACTION:
CC Q8NB12; P30520: ADSS2; NbExp=4; IntAct=EBI-8463848, EBI-1042898;
CC Q8NB12; Q03989: ARID5A; NbExp=3; IntAct=EBI-8463848, EBI-948603;
CC Q8NB12; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-8463848, EBI-1642333;
CC Q8NB12; O14503: BHLHE40; NbExp=8; IntAct=EBI-8463848, EBI-711810;
CC Q8NB12; Q9H5F2: C11orf1; NbExp=3; IntAct=EBI-8463848, EBI-718615;
CC Q8NB12; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-8463848, EBI-11988027;
CC Q8NB12; Q86TH3: DVL1; NbExp=3; IntAct=EBI-8463848, EBI-10185025;
CC Q8NB12; Q6J272: FAM166A; NbExp=3; IntAct=EBI-8463848, EBI-12811067;
CC Q8NB12; Q9H8W3: FAM204A; NbExp=4; IntAct=EBI-8463848, EBI-8465160;
CC Q8NB12; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-8463848, EBI-1384254;
CC Q8NB12; Q9NVL1-2: FAM86C1P; NbExp=3; IntAct=EBI-8463848, EBI-12845222;
CC Q8NB12; Q9BSH5: HDHD3; NbExp=3; IntAct=EBI-8463848, EBI-745201;
CC Q8NB12; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-8463848, EBI-740641;
CC Q8NB12; Q8IX15-3: HOMEZ; NbExp=3; IntAct=EBI-8463848, EBI-10172004;
CC Q8NB12; Q96L93-6: KIF16B; NbExp=3; IntAct=EBI-8463848, EBI-10988217;
CC Q8NB12; Q92764: KRT35; NbExp=3; IntAct=EBI-8463848, EBI-1058674;
CC Q8NB12; Q99750: MDFI; NbExp=3; IntAct=EBI-8463848, EBI-724076;
CC Q8NB12; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-8463848, EBI-16439278;
CC Q8NB12; A7E2Y1: MYH7B; NbExp=2; IntAct=EBI-8463848, EBI-2880253;
CC Q8NB12; A7E2Y1-2: MYH7B; NbExp=3; IntAct=EBI-8463848, EBI-12813813;
CC Q8NB12; P07196: NEFL; NbExp=3; IntAct=EBI-8463848, EBI-475646;
CC Q8NB12; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-8463848, EBI-11022007;
CC Q8NB12; P78424: POU6F2; NbExp=3; IntAct=EBI-8463848, EBI-12029004;
CC Q8NB12; Q9BQ04: RBM4B; NbExp=2; IntAct=EBI-8463848, EBI-715531;
CC Q8NB12; Q9H0K4: RSPH6A; NbExp=3; IntAct=EBI-8463848, EBI-12169267;
CC Q8NB12; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-8463848, EBI-6257312;
CC Q8NB12; Q9Y5W9: SNX11; NbExp=3; IntAct=EBI-8463848, EBI-10329449;
CC Q8NB12; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-8463848, EBI-11959123;
CC Q8NB12; Q3YBR2: TBRG1; NbExp=3; IntAct=EBI-8463848, EBI-2800552;
CC Q8NB12; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-8463848, EBI-11975223;
CC Q8NB12; Q9BVJ6: UTP14A; NbExp=4; IntAct=EBI-8463848, EBI-473284;
CC Q8NB12; Q9H5J0: ZBTB3; NbExp=3; IntAct=EBI-8463848, EBI-7229473;
CC Q8NB12; Q8NCP5: ZBTB44; NbExp=5; IntAct=EBI-8463848, EBI-5658292;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expression seems mostly restricted to heart and
CC skeletal muscle. {ECO:0000269|PubMed:19783823}.
CC -!- INDUCTION: By serum response factor SRF and myogenin. SRF binds to the
CC CArG site and MYOG binds to the E-box element on SMYD1 promoter.
CC {ECO:0000269|PubMed:19783823}.
CC -!- DOMAIN: The SET domain is split between the S-sequence (residues 1-49)
CC and the core SET domain (residues 181-258), however the two segments
CC still come together to form a conserved SET domain fold. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AK091724; BAC03732.1; -; mRNA.
DR EMBL; AL832035; CAI46139.1; -; mRNA.
DR EMBL; AC092836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126191; AAI26192.1; -; mRNA.
DR CCDS; CCDS33240.1; -.
DR RefSeq; NP_938015.1; NM_198274.3.
DR AlphaFoldDB; Q8NB12; -.
DR SMR; Q8NB12; -.
DR BioGRID; 127308; 59.
DR IntAct; Q8NB12; 49.
DR MINT; Q8NB12; -.
DR STRING; 9606.ENSP00000393453; -.
DR iPTMnet; Q8NB12; -.
DR PhosphoSitePlus; Q8NB12; -.
DR BioMuta; SMYD1; -.
DR DMDM; 34925329; -.
DR jPOST; Q8NB12; -.
DR MassIVE; Q8NB12; -.
DR PaxDb; Q8NB12; -.
DR PeptideAtlas; Q8NB12; -.
DR PRIDE; Q8NB12; -.
DR ProteomicsDB; 72714; -.
DR Antibodypedia; 47498; 233 antibodies from 27 providers.
DR DNASU; 150572; -.
DR Ensembl; ENST00000419482.7; ENSP00000393453.2; ENSG00000115593.15.
DR GeneID; 150572; -.
DR KEGG; hsa:150572; -.
DR MANE-Select; ENST00000419482.7; ENSP00000393453.2; NM_198274.4; NP_938015.1.
DR UCSC; uc002ssr.4; human.
DR CTD; 150572; -.
DR DisGeNET; 150572; -.
DR GeneCards; SMYD1; -.
DR HGNC; HGNC:20986; SMYD1.
DR HPA; ENSG00000115593; Group enriched (heart muscle, skeletal muscle, tongue).
DR MIM; 606846; gene.
DR neXtProt; NX_Q8NB12; -.
DR OpenTargets; ENSG00000115593; -.
DR PharmGKB; PA134862943; -.
DR VEuPathDB; HostDB:ENSG00000115593; -.
DR eggNOG; KOG2084; Eukaryota.
DR GeneTree; ENSGT00940000156114; -.
DR HOGENOM; CLU_018406_1_1_1; -.
DR InParanoid; Q8NB12; -.
DR OMA; YAHGVFP; -.
DR OrthoDB; 981799at2759; -.
DR PhylomeDB; Q8NB12; -.
DR TreeFam; TF106487; -.
DR BioCyc; MetaCyc:ENSG00000115593-MON; -.
DR PathwayCommons; Q8NB12; -.
DR SignaLink; Q8NB12; -.
DR BioGRID-ORCS; 150572; 8 hits in 1083 CRISPR screens.
DR GenomeRNAi; 150572; -.
DR Pharos; Q8NB12; Tbio.
DR PRO; PR:Q8NB12; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NB12; protein.
DR Bgee; ENSG00000115593; Expressed in left ventricle myocardium and 114 other tissues.
DR ExpressionAtlas; Q8NB12; baseline and differential.
DR Genevisible; Q8NB12; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0034968; P:histone lysine methylation; IBA:GO_Central.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:BHF-UCL.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IDA:BHF-UCL.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR CDD; cd10526; SET_SMYD1; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044418; SMYD1_SET.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..490
FT /note="Histone-lysine N-methyltransferase SMYD1"
FT /id="PRO_0000218307"
FT DOMAIN 7..253
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 52..90
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 17..19
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 205..206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 270..272
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT VARIANT 164
FT /note="Q -> P (in dbSNP:rs1542087)"
FT /id="VAR_052990"
SQ SEQUENCE 490 AA; 56617 MW; 1AE2FAE62D2B28C6 CRC64;
MTIGRMENVE VFTAEGKGRG LKATKEFWAA DIIFAERAYS AVVFDSLVNF VCHTCFKRQE
KLHRCGQCKF AHYCDRTCQK DAWLNHKNEC SAIKRYGKVP NENIRLAARI MWRVEREGTG
LTEGCLVSVD DLQNHVEHFG EEEQKDLRVD VDTFLQYWPP QSQQFSMQYI SHIFGVINCN
GFTLSDQRGL QAVGVGIFPN LGLVNHDCWP NCTVIFNNGN HEAVKSMFHT QMRIELRALG
KISEGEELTV SYIDFLNVSE ERKRQLKKQY YFDCTCEHCQ KKLKDDLFLG VKDNPKPSQE
VVKEMIQFSK DTLEKIDKAR SEGLYHEVVK LCRECLEKQE PVFADTNIYM LRMLSIVSEV
LSYLQAFEEA SFYARRMVDG YMKLYHPNNA QLGMAVMRAG LTNWHAGNIE VGHGMICKAY
AILLVTHGPS HPITKDLEAM RVQTEMELRM FRQNEFMYYK MREAALNNQP MQVMAEPSNE
PSPALFHKKQ
