ID   EPM2A_RAT               Reviewed;         331 AA.
AC   Q91XQ2; F1LPW7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 2.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Laforin;
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:Q9WUA5};
DE            EC=3.1.3.16;
DE            EC=3.1.3.48 {ECO:0000250|UniProtKB:O95278};
DE   AltName: Full=Glucan phosphatase;
DE   AltName: Full=Lafora PTPase;
DE            Short=LAFPTPase;
GN   Name=Epm2a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 5-331, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain cortex;
RX   PubMed=11355878; DOI=10.1006/bbrc.2001.4914;
RA   Ganesh S., Agarwala K.L., Amano K., Suzuki T., Delgado-Escueta A.V.,
RA   Yamakawa K.;
RT   "Regional and developmental expression of Epm2a gene and its evolutionary
RT   conservation.";
RL   Biochem. Biophys. Res. Commun. 283:1046-1053(2001).
CC   -!- FUNCTION: Plays an important role in preventing glycogen
CC       hyperphosphorylation and the formation of insoluble aggregates, via its
CC       activity as glycogen phosphatase, and by promoting the ubiquitination
CC       of proteins involved in glycogen metabolism via its interaction with
CC       the E3 ubiquitin ligase NHLRC1/malin. Dephosphorylates phosphotyrosine
CC       and synthetic substrates, such as para-nitrophenylphosphate (pNPP), and
CC       has low activity with phosphoserine and phosphothreonine substrates (in
CC       vitro). Has also been shown to dephosphorylate MAPT. Shows strong
CC       phosphatase activity towards complex carbohydrates in vitro, avoiding
CC       glycogen hyperphosphorylation which is associated with reduced
CC       branching and formation of insoluble aggregates. Forms a complex with
CC       NHLRC1/malin and HSP70, which suppresses the cellular toxicity of
CC       misfolded proteins by promoting their degradation through the
CC       ubiquitin-proteasome system (UPS). Acts as a scaffold protein to
CC       facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes
CC       proteasome-independent protein degradation through the macroautophagy
CC       pathway. {ECO:0000250|UniProtKB:O95278, ECO:0000250|UniProtKB:Q9WUA5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- SUBUNIT: Homodimer. Interacts with itself. Interacts with PPP1R3B,
CC       PPP1R3C, PPP1R3D, HIRIP5, and EPM2AIP1. Binds glycogen and Lafora
CC       bodies. Interacts with NHLRC1/malin (via the NHL repeats). Forms a
CC       complex with NHLRC1/malin and HSP70. Interacts with PPP1R3D; in the
CC       presence of NHLC1/malin the interaction leads to ubiquitination and
CC       autophagic degradation of PPP1R3D. Interacts (via the phosphatase
CC       domain) with MAPT/Tau; the interaction dephosphorylates MAPT. Interacts
CC       with PRDM8. {ECO:0000250|UniProtKB:O95278}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95278}.
CC       Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95278};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:O95278}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:O95278}. Cell membrane
CC       {ECO:0000250|UniProtKB:O95278}. Note=Colocalizes with glycogen synthase
CC       in punctate structures in the cytoplasm. Primarily associated with
CC       polyribosomes at the rough endoplasmic reticulum, and also detected at
CC       the plasma membrane. Under glycogenolytic conditions localizes to the
CC       nucleus. {ECO:0000250|UniProtKB:O95278}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11355878}.
CC   -!- DOMAIN: The CBM20 domain mediates binding to cytoplasmic glycogen and
CC       to Lafora polyglucosan bodies. {ECO:0000250|UniProtKB:O95278}.
CC   -!- PTM: Polyubiquitinated by NHLRC1/malin. {ECO:0000250|UniProtKB:O95278}.
CC   -!- PTM: Phosphorylation on Ser-25 by AMPK affects the phosphatase activity
CC       of the enzyme and its ability to homodimerize and interact with NHLRC1,
CC       PPP1R3C or PRKAA2. {ECO:0000250|UniProtKB:O95278}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AABR06000316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06000328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473994; EDL93717.1; -; Genomic_DNA.
DR   EMBL; AF347030; AAK60619.1; -; mRNA.
DR   RefSeq; NP_001263691.1; NM_001276762.1.
DR   AlphaFoldDB; Q91XQ2; -.
DR   SMR; Q91XQ2; -.
DR   BioGRID; 250254; 1.
DR   STRING; 10116.ENSRNOP00000058646; -.
DR   PhosphoSitePlus; Q91XQ2; -.
DR   PaxDb; 10116-ENSRNOP00000058646; -.
DR   PeptideAtlas; Q91XQ2; -.
DR   Ensembl; ENSRNOT00000099572.1; ENSRNOP00000076978.1; ENSRNOG00000040242.5.
DR   Ensembl; ENSRNOT00055002894; ENSRNOP00055002176; ENSRNOG00055001787.
DR   Ensembl; ENSRNOT00060008042; ENSRNOP00060006018; ENSRNOG00060004833.
DR   Ensembl; ENSRNOT00065043273; ENSRNOP00065035469; ENSRNOG00065025151.
DR   GeneID; 114005; -.
DR   KEGG; rno:114005; -.
DR   AGR; RGD:71047; -.
DR   CTD; 7957; -.
DR   RGD; 71047; Epm2a.
DR   eggNOG; KOG1716; Eukaryota.
DR   GeneTree; ENSGT00390000010101; -.
DR   HOGENOM; CLU_076792_0_0_1; -.
DR   InParanoid; Q91XQ2; -.
DR   OrthoDB; 351254at2759; -.
DR   TreeFam; TF332841; -.
DR   PRO; PR:Q91XQ2; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Proteomes; UP000234681; Chromosome 1.
DR   Bgee; ENSRNOG00000040242; Expressed in quadriceps femoris and 17 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0098554; C:cytoplasmic side of endoplasmic reticulum membrane; ISO:RGD.
DR   GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0030425; C:dendrite; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0043204; C:perikaryon; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005844; C:polysome; ISO:RGD.
DR   GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR   GO; GO:0019203; F:carbohydrate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; ISO:RGD.
DR   GO; GO:2001069; F:glycogen binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016791; F:phosphatase activity; ISO:RGD.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:RGD.
DR   GO; GO:0030247; F:polysaccharide binding; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISO:RGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:RGD.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:2001070; F:starch binding; ISO:RGD.
DR   GO; GO:0000045; P:autophagosome assembly; ISO:RGD.
DR   GO; GO:0006914; P:autophagy; ISO:RGD.
DR   GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR   GO; GO:0046835; P:carbohydrate phosphorylation; ISO:RGD.
DR   GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0014009; P:glial cell proliferation; ISO:RGD.
DR   GO; GO:0005978; P:glycogen biosynthetic process; ISO:RGD.
DR   GO; GO:0005977; P:glycogen metabolic process; ISS:UniProtKB.
DR   GO; GO:0046959; P:habituation; ISO:RGD.
DR   GO; GO:0015813; P:L-glutamate transmembrane transport; ISO:RGD.
DR   GO; GO:0043170; P:macromolecule metabolic process; ISO:RGD.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR   GO; GO:0045786; P:negative regulation of cell cycle; ISO:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR   GO; GO:0032007; P:negative regulation of TOR signaling; ISO:RGD.
DR   GO; GO:0007399; P:nervous system development; ISO:RGD.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; ISO:RGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0001558; P:regulation of cell growth; ISO:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR   GO; GO:0042325; P:regulation of phosphorylation; ISO:RGD.
DR   GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:RGD.
DR   GO; GO:0042306; P:regulation of protein import into nucleus; ISO:RGD.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:RGD.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; ISO:RGD.
DR   GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
DR   CDD; cd05806; CBM20_laforin; 1.
DR   CDD; cd14526; DSP_laforin-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR034831; CBM20_laforin.
DR   InterPro; IPR002044; CBM_fam20.
DR   InterPro; IPR045204; DSP_laforin-like.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR042942; Laforin.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR46864; LAFORIN; 1.
DR   PANTHER; PTHR46864:SF1; LAFORIN; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM01065; CBM_2; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR   PROSITE; PS51166; CBM20; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Carbohydrate metabolism; Cell membrane; Cytoplasm;
KW   Endoplasmic reticulum; Glycogen metabolism; Hydrolase; Membrane;
KW   Phosphoprotein; Protein phosphatase; Reference proteome; Ubl conjugation.
FT   CHAIN           1..331
FT                   /note="Laforin"
FT                   /id="PRO_0000094840"
FT   DOMAIN          1..124
FT                   /note="CBM20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT   DOMAIN          156..323
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   MOTIF           266..272
FT                   /note="Glucan phosphatase signature motif CXAGXGR"
FT                   /evidence="ECO:0000250|UniProtKB:O95278"
FT   ACT_SITE        266
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O95278"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O95278"
FT   BINDING         103..107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O95278"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O95278"
FT   BINDING         235
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O95278"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O95278"
FT   BINDING         267..272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O95278"
FT   BINDING         304
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O95278"
FT   SITE            329
FT                   /note="Required for homodimerization"
FT                   /evidence="ECO:0000250|UniProtKB:O95278"
FT   MOD_RES         25
FT                   /note="Phosphoserine; by AMPK"
FT                   /evidence="ECO:0000250|UniProtKB:O95278"
FT   CONFLICT        9..10
FT                   /note="VP -> DQ (in Ref. 3; AAK60619)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   331 AA;  37144 MW;  C97D07AA55A534FC CRC64;
     MLFRFGVVVP PAVAGTRLEL LLAGSRPELG RWEPRGAVRL RPAGTAAGAA ALALQEPGLW
     LAEVELAPEE EAADGAEPGR IDTFWYKFLQ REPGGELHWE GNGPHHDRCC TYNENNLVDG
     VYCLPVGHWI EATGHTNEMK HTTDFYFNIA GHQAMHYSRI LPNIWLGSCP RQLEHVTIKL
     KHELGITAVM NFQTEWDIIQ NSSGCNRYPE PMTPDTMMKL YKEEGLAYIW MPTPDMSTEG
     RVQMLPQAVC LLHALLENGH TVYVHCNAGV GRSTAAVCGW LHYVIGWSLR KVQYFIMAKR
     PAVYIDEEAL AQAQQDFFQK FGKVHSSICT L
//