MT21A_HUMAN
ID MT21A_HUMAN Reviewed; 218 AA.
AC Q8WXB1; Q53RV0; Q8N1Z9; Q96GH6;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein N-lysine methyltransferase METTL21A;
DE EC=2.1.1.- {ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:23921388};
DE AltName: Full=HSPA lysine methyltransferase {ECO:0000303|PubMed:23921388};
DE AltName: Full=HSPA-KMT {ECO:0000303|PubMed:23921388};
DE AltName: Full=Hepatocellular carcinoma-associated antigen 557b {ECO:0000303|Ref.1};
DE AltName: Full=Methyltransferase-like protein 21A;
GN Name=METTL21A; Synonyms=FAM119A, HCA557B {ECO:0000303|Ref.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-192.
RA Dong X.-Y., Chen W.-F.;
RT "HCA557b, a transcription factor associated with hepatocellular
RT carcinoma.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-192.
RC TISSUE=Thymus;
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 [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] (ISOFORMS 1 AND 2), AND VARIANT
RP ILE-192.
RC TISSUE=Brain, and Lymph;
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 FUNCTION, MUTAGENESIS OF ASP-94, AND CATALYTIC ACTIVITY.
RX PubMed=22948820; DOI=10.1038/ncomms2041;
RA Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S.,
RA Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.;
RT "Lysine methylation of VCP by a member of a novel human protein
RT methyltransferase family.";
RL Nat. Commun. 3:1038-1038(2012).
RN [6]
RP FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=23921388; DOI=10.1074/jbc.m113.483248;
RA Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
RA Melki R., Falnes P.O.;
RT "Identification and characterization of a novel human methyltransferase
RT modulating Hsp70 function through lysine methylation.";
RL J. Biol. Chem. 288:27752-27763(2013).
RN [7]
RP FUNCTION, INTERACTION WITH HSP70 FAMILY MEMBERS, SUBCELLULAR LOCATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT "A newly uncovered group of distantly related lysine methyltransferases
RT preferentially interact with molecular chaperones to regulate their
RT activity.";
RL PLoS Genet. 9:E1003210-E1003210(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 8-218 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RG Structural genomics consortium (SGC);
RT "The crystal structure of human methyltransferase-like protein 21A in
RT complex with SAH.";
RL Submitted (JUL-2013) to the PDB data bank.
CC -!- FUNCTION: Protein-lysine methyltransferase that selectively
CC trimethylates residues in heat shock protein 70 (HSP70) family members.
CC Contributes to the in vivo trimethylation of Lys residues in HSPA1 and
CC HSPA8. In vitro methylates 'Lys-561' in HSPA1, 'Lys-564' in HSPA2,
CC 'Lys-585' in HSPA5, 'Lys-563' in HSPA6 and 'Lys-561' in HSPA8.
CC {ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634,
CC ECO:0000269|PubMed:23921388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC Evidence={ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634,
CC ECO:0000269|PubMed:23921388};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC Evidence={ECO:0000305|PubMed:23349634};
CC -!- SUBUNIT: Interacts with heat shock protein 70 family members; at least
CC some of these proteins are methylation substrates (PubMed:23349634 and
CC PubMed:23921388). {ECO:0000269|PubMed:23349634,
CC ECO:0000269|PubMed:23921388, ECO:0000269|Ref.8}.
CC -!- INTERACTION:
CC Q8WXB1; P59998: ARPC4; NbExp=3; IntAct=EBI-8652459, EBI-351872;
CC Q8WXB1; Q8WXE1: ATRIP; NbExp=3; IntAct=EBI-8652459, EBI-747353;
CC Q8WXB1; Q8TBB1: LNX1; NbExp=4; IntAct=EBI-8652459, EBI-739832;
CC Q8WXB1; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-8652459, EBI-1216080;
CC Q8WXB1; A8MW99: MEI4; NbExp=3; IntAct=EBI-8652459, EBI-19944212;
CC Q8WXB1; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-8652459, EBI-16439278;
CC Q8WXB1; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-8652459, EBI-10699187;
CC Q8WXB1; Q99471: PFDN5; NbExp=3; IntAct=EBI-8652459, EBI-357275;
CC Q8WXB1; Q8IZ13: ZBED8; NbExp=8; IntAct=EBI-8652459, EBI-7186123;
CC Q8WXB1; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-8652459, EBI-4395669;
CC Q8WXB1; Q8N720: ZNF655; NbExp=3; IntAct=EBI-8652459, EBI-625509;
CC Q8WXB1; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-8652459, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23349634}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WXB1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WXB1-2; Sequence=VSP_026379, VSP_026380;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL21
CC family. {ECO:0000305}.
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DR EMBL; AF455817; AAL66295.1; -; mRNA.
DR EMBL; AK093812; BAC04229.1; -; mRNA.
DR EMBL; AC079767; AAX93175.1; -; Genomic_DNA.
DR EMBL; BC009462; AAH09462.1; -; mRNA.
DR EMBL; BC033720; AAH33720.1; -; mRNA.
DR CCDS; CCDS2376.1; -. [Q8WXB1-1]
DR CCDS; CCDS82562.1; -. [Q8WXB1-2]
DR RefSeq; NP_001120867.1; NM_001127395.3. [Q8WXB1-1]
DR RefSeq; NP_001294950.1; NM_001308021.2.
DR RefSeq; NP_001317059.1; NM_001330130.1. [Q8WXB1-1]
DR RefSeq; NP_001317060.1; NM_001330131.1. [Q8WXB1-2]
DR RefSeq; NP_001317062.1; NM_001330133.1. [Q8WXB1-2]
DR RefSeq; NP_001317063.1; NM_001330134.1. [Q8WXB1-1]
DR RefSeq; NP_001317064.1; NM_001330135.1. [Q8WXB1-2]
DR RefSeq; NP_660323.3; NM_145280.6. [Q8WXB1-1]
DR RefSeq; XP_005246396.1; XM_005246339.3. [Q8WXB1-1]
DR RefSeq; XP_005246397.1; XM_005246340.3. [Q8WXB1-1]
DR PDB; 4LEC; X-ray; 2.28 A; A/B=8-218.
DR PDBsum; 4LEC; -.
DR AlphaFoldDB; Q8WXB1; -.
DR SMR; Q8WXB1; -.
DR BioGRID; 127352; 40.
DR IntAct; Q8WXB1; 16.
DR MINT; Q8WXB1; -.
DR STRING; 9606.ENSP00000415115; -.
DR ChEMBL; CHEMBL3588741; -.
DR iPTMnet; Q8WXB1; -.
DR PhosphoSitePlus; Q8WXB1; -.
DR BioMuta; METTL21A; -.
DR DMDM; 150382834; -.
DR EPD; Q8WXB1; -.
DR jPOST; Q8WXB1; -.
DR MassIVE; Q8WXB1; -.
DR MaxQB; Q8WXB1; -.
DR PaxDb; Q8WXB1; -.
DR PeptideAtlas; Q8WXB1; -.
DR PRIDE; Q8WXB1; -.
DR ProteomicsDB; 75001; -. [Q8WXB1-1]
DR ProteomicsDB; 75002; -. [Q8WXB1-2]
DR Antibodypedia; 34188; 181 antibodies from 21 providers.
DR DNASU; 151194; -.
DR Ensembl; ENST00000406927.6; ENSP00000385481.2; ENSG00000144401.14. [Q8WXB1-1]
DR Ensembl; ENST00000411432.5; ENSP00000415115.1; ENSG00000144401.14. [Q8WXB1-1]
DR Ensembl; ENST00000425132.5; ENSP00000400730.1; ENSG00000144401.14. [Q8WXB1-2]
DR Ensembl; ENST00000426075.5; ENSP00000403317.1; ENSG00000144401.14. [Q8WXB1-1]
DR Ensembl; ENST00000442521.1; ENSP00000392062.1; ENSG00000144401.14. [Q8WXB1-1]
DR Ensembl; ENST00000448007.6; ENSP00000407622.2; ENSG00000144401.14. [Q8WXB1-1]
DR Ensembl; ENST00000458426.5; ENSP00000389684.1; ENSG00000144401.14. [Q8WXB1-2]
DR GeneID; 151194; -.
DR KEGG; hsa:151194; -.
DR MANE-Select; ENST00000411432.6; ENSP00000415115.1; NM_001127395.5; NP_001120867.1.
DR UCSC; uc002vce.4; human. [Q8WXB1-1]
DR CTD; 151194; -.
DR DisGeNET; 151194; -.
DR GeneCards; METTL21A; -.
DR HGNC; HGNC:30476; METTL21A.
DR HPA; ENSG00000144401; Low tissue specificity.
DR MIM; 615257; gene.
DR neXtProt; NX_Q8WXB1; -.
DR OpenTargets; ENSG00000144401; -.
DR PharmGKB; PA145008433; -.
DR VEuPathDB; HostDB:ENSG00000144401; -.
DR eggNOG; KOG2793; Eukaryota.
DR GeneTree; ENSGT00940000157249; -.
DR HOGENOM; CLU_055721_4_2_1; -.
DR InParanoid; Q8WXB1; -.
DR OrthoDB; 1588190at2759; -.
DR PhylomeDB; Q8WXB1; -.
DR TreeFam; TF313206; -.
DR PathwayCommons; Q8WXB1; -.
DR Reactome; R-HSA-8876725; Protein methylation.
DR SignaLink; Q8WXB1; -.
DR BioGRID-ORCS; 151194; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; METTL21A; human.
DR GenomeRNAi; 151194; -.
DR Pharos; Q8WXB1; Tbio.
DR PRO; PR:Q8WXB1; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WXB1; protein.
DR Bgee; ENSG00000144401; Expressed in oocyte and 175 other tissues.
DR ExpressionAtlas; Q8WXB1; baseline and differential.
DR Genevisible; Q8WXB1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:BHF-UCL.
DR GO; GO:0008276; F:protein methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IDA:BHF-UCL.
DR GO; GO:0006479; P:protein methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..218
FT /note="Protein N-lysine methyltransferase METTL21A"
FT /id="PRO_0000292033"
FT BINDING 47
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.8"
FT BINDING 73..75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.8"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.8"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.8"
FT BINDING 143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|Ref.8"
FT VAR_SEQ 88..90
FT /note="AHV -> GGI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026379"
FT VAR_SEQ 91..218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026380"
FT VARIANT 192
FT /note="T -> I (in dbSNP:rs2551949)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_032935"
FT MUTAGEN 94
FT /note="D->A: Abolishes methyltransferase activity."
FT /evidence="ECO:0000269|PubMed:22948820"
FT CONFLICT 33
FT /note="I -> T (in Ref. 2; BAC04229)"
FT /evidence="ECO:0000305"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:4LEC"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:4LEC"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:4LEC"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:4LEC"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:4LEC"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:4LEC"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4LEC"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:4LEC"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:4LEC"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:4LEC"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:4LEC"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:4LEC"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4LEC"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:4LEC"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:4LEC"
FT HELIX 152..162
FT /evidence="ECO:0007829|PDB:4LEC"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:4LEC"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:4LEC"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:4LEC"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:4LEC"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:4LEC"
SQ SEQUENCE 218 AA; 24600 MW; 18E7E39A1CDCC56E CRC64;
MALVPYEETT EFGLQKFHKP LATFSFANHT IQIRQDWRHL GVAAVVWDAA IVLSTYLEMG
AVELRGRSAV ELGAGTGLVG IVAALLGAHV TITDRKVALE FLKSNVQANL PPHIQTKTVV
KELTWGQNLG SFSPGEFDLI LGADIIYLEE TFTDLLQTLE HLCSNHSVIL LACRIRYERD
NNFLAMLERQ FTVRKVHYDP EKDVHIYEAQ KRNQKEDL
