H2AY_MOUSE
ID H2AY_MOUSE Reviewed; 372 AA.
AC Q9QZQ8; Q91VZ2; Q9QZQ7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Core histone macro-H2A.1;
DE Short=Histone macroH2A1;
DE Short=mH2A1;
DE AltName: Full=H2A.y;
DE AltName: Full=H2A/y;
GN Name=Macroh2a1 {ECO:0000312|MGI:MGI:1349392};
GN Synonyms=H2afy {ECO:0000312|MGI:MGI:1349392};
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 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 197-229 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=129/SvEvTacfBr;
RX PubMed=10471737; DOI=10.1093/nar/27.18.3685;
RA Rasmussen T.P., Huang T., Mastrangelo M.-A., Loring J., Panning B.,
RA Jaenisch R.;
RT "Messenger RNAs encoding mouse histone macroH2A1 isoforms are expressed at
RT similar levels in male and female cells and result from alternative
RT splicing.";
RL Nucleic Acids Res. 27:3685-3689(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH SPOP.
RC TISSUE=Brain;
RX PubMed=12183056; DOI=10.1016/s0167-4889(02)00249-5;
RA Takahashi I., Kameoka Y., Hashimoto K.;
RT "MacroH2A1.2 binds the nuclear protein Spop.";
RL Biochim. Biophys. Acta 1591:63-68(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9634239; DOI=10.1038/31275;
RA Costanzi C., Pehrson J.R.;
RT "Histone macroH2A1 is concentrated in the inactive X chromosome of female
RT mammals.";
RL Nature 393:599-601(1998).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=11262398; DOI=10.1074/jbc.m010919200;
RA Costanzi C., Pehrson J.R.;
RT "MACROH2A2, a new member of the MACROH2A core histone family.";
RL J. Biol. Chem. 276:21776-21784(2001).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15564378; DOI=10.1242/jcs.01537;
RA Grigoryev S.A., Nikitina T., Pehrson J.R., Singh P.B., Woodcock C.L.;
RT "Dynamic relocation of epigenetic chromatin markers reveals an active role
RT of constitutive heterochromatin in the transition from proliferation to
RT quiescence.";
RL J. Cell Sci. 117:6153-6162(2004).
RN [7]
RP INTERACTION WITH HDAC1 AND HDAC2, AND FUNCTION.
RX PubMed=16107708; DOI=10.1128/mcb.25.17.7616-7624.2005;
RA Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y., Pehrson J.R.,
RA Khochbin S., Luger K.;
RT "Structural characterization of the histone variant macroH2A.";
RL Mol. Cell. Biol. 25:7616-7624(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173 AND
RP THR-178, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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 [10]
RP FUNCTION (ISOFORMS 1 AND 2), AND ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RX PubMed=23022728; DOI=10.1038/nsmb.2390;
RA Dardenne E., Pierredon S., Driouch K., Gratadou L., Lacroix-Triki M.,
RA Espinoza M.P., Zonta E., Germann S., Mortada H., Villemin J.P.,
RA Dutertre M., Lidereau R., Vagner S., Auboeuf D.;
RT "Splicing switch of an epigenetic regulator by RNA helicases promotes
RT tumor-cell invasiveness.";
RL Nat. Struct. Mol. Biol. 19:1139-1146(2012).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-123, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes where it represses transcription. Nucleosomes
CC wrap and compact DNA into chromatin, limiting DNA accessibility to the
CC cellular machineries which require DNA as a template. Histones thereby
CC play a central role in transcription regulation, DNA repair, DNA
CC replication and chromosomal stability. DNA accessibility is regulated
CC via a complex set of post-translational modifications of histones, also
CC called histone code, and nucleosome remodeling. Involved in stable X
CC chromosome inactivation. Inhibits the binding of transcription factors,
CC including NF-kappa-B, and interferes with the activity of remodeling
CC SWI/SNF complexes (By similarity). Inhibits histone acetylation by
CC EP300 and recruits class I HDACs, which induces a hypoacetylated state
CC of chromatin (By similarity) (PubMed:16107708).
CC {ECO:0000250|UniProtKB:O75367, ECO:0000269|PubMed:16107708}.
CC -!- FUNCTION: [Isoform 1]: Binds ADP-ribose and O-acetyl-ADP-ribose, and
CC may be involved in ADP-ribose-mediated chromatin modulation (By
CC similarity). Increases the expression of genes involved in redox
CC metabolism, including SOD3 (PubMed:23022728).
CC {ECO:0000250|UniProtKB:O75367, ECO:0000269|PubMed:23022728}.
CC -!- FUNCTION: [Isoform 2]: Represses SOD3 gene expression.
CC {ECO:0000269|PubMed:23022728}.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. Interacts with SPOP. Part of a complex
CC consisting of MACROH2A1, CUL3 and SPOP. Interacts with HDAC1 and HDAC2
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15564378,
CC ECO:0000269|PubMed:9634239}. Chromosome {ECO:0000269|PubMed:15564378,
CC ECO:0000269|PubMed:9634239}. Note=Enriched in inactive X chromosome
CC chromatin and in senescence-associated heterochromatin
CC (PubMed:9634239). In quiescent lymphocytes, associated with centromeric
CC constitutive heterochromatin (PubMed:15564378).
CC {ECO:0000269|PubMed:15564378, ECO:0000269|PubMed:9634239}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=mH2A1.2 {ECO:0000303|PubMed:23022728};
CC IsoId=Q9QZQ8-1; Sequence=Displayed;
CC Name=1; Synonyms=mH2A1.1 {ECO:0000303|PubMed:23022728};
CC IsoId=Q9QZQ8-2; Sequence=VSP_017596, VSP_017597;
CC -!- TISSUE SPECIFICITY: Widely expressed, with high levels in testis.
CC Present in liver, kidney and adrenal gland (at protein level). In the
CC liver, present in hepatocytes and at a lesser extent in cells of the
CC bile ducts. In the kidney, expressed in proximal and distal convoluted
CC tubules and in straight proximal tubules. In the adrenal gland, present
CC in inner cells of the cortex and medulla. {ECO:0000269|PubMed:10471737,
CC ECO:0000269|PubMed:11262398}.
CC -!- PTM: Monoubiquitinated at either Lys-116 or Lys-117. May also be
CC polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3
CC complex and does not promote proteasomal degradation. Instead, it is
CC required for enrichment in inactive X chromosome chromatin (By
CC similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: Major form. The preferential expression of
CC isoform 2 over that of isoform 1 requires the presence of DDX5/DDX17.
CC {ECO:0000269|PubMed:23022728}.
CC -!- MISCELLANEOUS: [Isoform 1]: Preferentially expressed over isoform 2 in
CC the absence of DDX5/DDX17. {ECO:0000269|PubMed:23022728}.
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DR EMBL; AF171080; AAD53745.1; -; mRNA.
DR EMBL; AF171081; AAD53746.1; -; mRNA.
DR EMBL; AB071988; BAB68541.1; -; mRNA.
DR EMBL; BC006955; AAH06955.1; -; mRNA.
DR CCDS; CCDS26557.1; -. [Q9QZQ8-1]
DR CCDS; CCDS49278.1; -. [Q9QZQ8-2]
DR RefSeq; NP_001152985.1; NM_001159513.1.
DR RefSeq; NP_001152986.1; NM_001159514.1. [Q9QZQ8-2]
DR RefSeq; NP_001152987.1; NM_001159515.1.
DR RefSeq; NP_036145.1; NM_012015.2. [Q9QZQ8-1]
DR AlphaFoldDB; Q9QZQ8; -.
DR SMR; Q9QZQ8; -.
DR BioGRID; 205061; 11.
DR IntAct; Q9QZQ8; 8.
DR MINT; Q9QZQ8; -.
DR STRING; 10090.ENSMUSP00000016081; -.
DR iPTMnet; Q9QZQ8; -.
DR PhosphoSitePlus; Q9QZQ8; -.
DR SwissPalm; Q9QZQ8; -.
DR EPD; Q9QZQ8; -.
DR jPOST; Q9QZQ8; -.
DR MaxQB; Q9QZQ8; -.
DR PaxDb; Q9QZQ8; -.
DR PeptideAtlas; Q9QZQ8; -.
DR PRIDE; Q9QZQ8; -.
DR ProteomicsDB; 270915; -. [Q9QZQ8-1]
DR ProteomicsDB; 270916; -. [Q9QZQ8-2]
DR Antibodypedia; 26391; 213 antibodies from 31 providers.
DR DNASU; 26914; -.
DR Ensembl; ENSMUST00000016081; ENSMUSP00000016081; ENSMUSG00000015937. [Q9QZQ8-1]
DR Ensembl; ENSMUST00000045788; ENSMUSP00000038221; ENSMUSG00000015937. [Q9QZQ8-2]
DR GeneID; 26914; -.
DR KEGG; mmu:26914; -.
DR UCSC; uc007qsf.2; mouse. [Q9QZQ8-1]
DR UCSC; uc007qsg.2; mouse. [Q9QZQ8-2]
DR CTD; 9555; -.
DR MGI; MGI:1349392; Macroh2a1.
DR VEuPathDB; HostDB:ENSMUSG00000015937; -.
DR eggNOG; KOG1756; Eukaryota.
DR eggNOG; KOG2633; Eukaryota.
DR GeneTree; ENSGT00940000159541; -.
DR HOGENOM; CLU_062828_0_0_1; -.
DR InParanoid; Q9QZQ8; -.
DR OMA; GHNFPAK; -.
DR PhylomeDB; Q9QZQ8; -.
DR TreeFam; TF332276; -.
DR BioGRID-ORCS; 26914; 1 hit in 75 CRISPR screens.
DR ChiTaRS; H2afy; mouse.
DR PRO; PR:Q9QZQ8; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9QZQ8; protein.
DR Bgee; ENSMUSG00000015937; Expressed in saccule of membranous labyrinth and 280 other tissues.
DR Genevisible; Q9QZQ8; MM.
DR GO; GO:0001740; C:Barr body; ISO:MGI.
DR GO; GO:0005813; C:centrosome; TAS:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005721; C:pericentric heterochromatin; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; ISO:MGI.
DR GO; GO:0000182; F:rDNA binding; ISO:MGI.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0007549; P:dosage compensation; ISO:MGI.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; ISO:MGI.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; ISO:MGI.
DR GO; GO:1902750; P:negative regulation of cell cycle G2/M phase transition; ISO:MGI.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; ISO:MGI.
DR GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0033128; P:negative regulation of histone phosphorylation; ISO:MGI.
DR GO; GO:1904815; P:negative regulation of protein localization to chromosome, telomeric region; ISO:MGI.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:1902883; P:negative regulation of response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:1901837; P:negative regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:1903226; P:positive regulation of endodermal cell differentiation; ISO:MGI.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISO:MGI.
DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; ISO:MGI.
DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISO:MGI.
DR GO; GO:1902882; P:regulation of response to oxidative stress; IMP:UniProtKB.
DR CDD; cd00074; H2A; 1.
DR CDD; cd02904; Macro_H2A-like; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR021171; Core_histone_macro-H2A.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR035796; Macro_H2A.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR Pfam; PF01661; Macro; 1.
DR PIRSF; PIRSF037942; Core_histone_macro-H2A; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00506; A1pp; 1.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromatin regulator; Chromosome;
KW DNA-binding; Isopeptide bond; Methylation; Nucleosome core; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..372
FT /note="Core histone macro-H2A.1"
FT /id="PRO_0000227904"
FT DOMAIN 2..117
FT /note="Histone H2A"
FT DOMAIN 184..370
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT REGION 128..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..160
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 9
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 18
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75367"
FT MOD_RES 116
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 123
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75367"
FT MOD_RES 123
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75367"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:O75367"
FT CROSSLNK 123
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O75367"
FT CROSSLNK 167
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75367"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75367"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75367"
FT VAR_SEQ 198..217
FT /note="NLIHSEISNLAGFEVEAIIN -> QVVQADIASIDSDAVVH (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:10471737,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017596"
FT VAR_SEQ 221..229
FT /note="ADIDLKDDL -> TDFYTGGEV (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:10471737,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017597"
SQ SEQUENCE 372 AA; 39735 MW; 076CF76A34FACAA0 CRC64;
MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI
LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS
KGKLEAIITP PPAKKAKSPS QKKPVAKKTG GKKGARKSKK KQGEVSKAAS ADSTTEGTPT
DGFTVLSTKS LFLGQKLNLI HSEISNLAGF EVEAIINPTN ADIDLKDDLG NTLEKKGGKE
FVEAVLELRK KNGPLEVAGA AISAGHGLPA KFVIHCNSPV WGADKCEELL EKTVKNCLAL
ADDRKLKSIA FPSIGSGRNG FPKQTAAQLI LKAISSYFVS TMSSSIKTVY FMLFDSESIG
IYVQEMAKLD AN
