1433E_MOUSE
ID 1433E_MOUSE Reviewed; 255 AA.
AC P62259; P29360; P42655; Q63631;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=14-3-3 protein epsilon;
DE Short=14-3-3E;
GN Name=Ywhae;
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], AND DEVELOPMENTAL STAGE.
RC STRAIN=SWR/J; TISSUE=Kidney;
RX PubMed=7750640; DOI=10.1006/dbio.1995.1139;
RA McConnell J.E., Armstrong J.F., Bard J.B.;
RT "The mouse 14-3-3 epsilon isoform, a kinase regulator whose expression
RT pattern is modulated in mesenchyme and neuronal differentiation.";
RL Dev. Biol. 169:218-228(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv;
RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PROTEIN SEQUENCE OF 131-141; 154-170 AND 197-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Friebe K., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH KSR1.
RX PubMed=10409742; DOI=10.1128/mcb.19.8.5523;
RA Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.;
RT "Kinase suppressor of Ras forms a multiprotein signaling complex and
RT modulates MEK localization.";
RL Mol. Cell. Biol. 19:5523-5534(1999).
RN [7]
RP INTERACTION WITH BEX3.
RX PubMed=11278287; DOI=10.1074/jbc.m005453200;
RA Kimura M.T., Irie S., Shoji-Hoshino S., Mukai J., Nadano D., Oshimura M.,
RA Sato T.-A.;
RT "14-3-3 is involved in p75 neurotrophin receptor-mediated signal
RT transduction.";
RL J. Biol. Chem. 276:17291-17300(2001).
RN [8]
RP INTERACTION WITH ARHGEF28.
RX PubMed=11533041; DOI=10.1074/jbc.m107709200;
RA Zhai J., Lin H., Shamim M., Schlaepfer W.W., Canete-Soler R.;
RT "Identification of a novel interaction of 14-3-3 with p190RhoGEF.";
RL J. Biol. Chem. 276:41318-41324(2001).
RN [9]
RP INTERACTION WITH NDEL1.
RX PubMed=12796778; DOI=10.1038/ng1169;
RA Toyo-oka K., Shionoya A., Gambello M.J., Cardoso C., Leventer R.,
RA Ward H.L., Ayala R., Tsai L.-H., Dobyns W., Ledbetter D., Hirotsune S.,
RA Wynshaw-Boris A.;
RT "14-3-3epsilon is important for neuronal migration by binding to NUDEL: a
RT molecular explanation for Miller-Dieker syndrome.";
RL Nat. Genet. 34:274-285(2003).
RN [10]
RP INTERACTION WITH GRB10.
RX PubMed=15722337; DOI=10.1074/jbc.m501477200;
RA Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.;
RT "Phosphorylation of grb10 regulates its interaction with 14-3-3.";
RL J. Biol. Chem. 280:16987-16993(2005).
RN [11]
RP INTERACTION WITH TIAM2.
RX PubMed=17320046; DOI=10.1016/j.bbrc.2007.02.028;
RA Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T., Nakayama M.,
RA Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K., Amano M.;
RT "Rho-kinase modulates the function of STEF, a Rac GEF, through its
RT phosphorylation.";
RL Biochem. Biophys. Res. Commun. 355:788-794(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [13]
RP INTERACTION WITH ZFP36.
RX PubMed=21078877; DOI=10.1128/mcb.00717-10;
RA Clement S.L., Scheckel C., Stoecklin G., Lykke-Andersen J.;
RT "Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA
RT decay by preventing deadenylase recruitment.";
RL Mol. Cell. Biol. 31:256-266(2011).
RN [14]
RP INTERACTION WITH DAPK2.
RX PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
RA Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
RT "Suppression of death-associated protein kinase 2 by interaction with 14-3-
RT 3 proteins.";
RL Biochem. Biophys. Res. Commun. 464:70-75(2015).
RN [15]
RP INTERACTION WITH CRTC1; CRTC2 AND CRTC3.
RX PubMed=30611118; DOI=10.1016/j.isci.2018.12.012;
RA Sonntag T., Ostojic J., Vaughan J.M., Moresco J.J., Yoon Y.S.,
RA Yates J.R. III, Montminy M.;
RT "Mitogenic Signals Stimulate the CREB Coactivator CRTC3 through PP2A
RT Recruitment.";
RL IScience 11:134-145(2018).
RN [16]
RP DISRUPTION PHENOTYPE.
RX PubMed=30973865; DOI=10.1371/journal.pbio.3000194;
RA Ingham N.J., Pearson S.A., Vancollie V.E., Rook V., Lewis M.A., Chen J.,
RA Buniello A., Martelletti E., Preite L., Lam C.C., Weiss F.D., Powis Z.,
RA Suwannarat P., Lelliott C.J., Dawson S.J., White J.K., Steel K.P.;
RT "Mouse screen reveals multiple new genes underlying mouse and human hearing
RT loss.";
RL PLoS Biol. 17:E3000194-E3000194(2019).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds to a
CC large number of partners, usually by recognition of a phosphoserine or
CC phosphothreonine motif. Binding generally results in the modulation of
CC the activity of the binding partner. Positively regulates
CC phosphorylated protein HSF1 nuclear export to the cytoplasm.
CC {ECO:0000250|UniProtKB:P62258, ECO:0000250|UniProtKB:P62261}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimerizes with YWHAZ (By
CC similarity). Interacts with PKA-phosphorylated AANAT (By similarity).
CC Interacts with ABL1 (phosphorylated form); the interaction retains it
CC in the cytoplasm (By similarity). Interacts with ARHGEF28
CC (PubMed:11533041). Interacts with BEX3 (PubMed:11278287). Weakly
CC interacts with CDKN1B (By similarity). Interacts with the 'Thr-369'
CC phosphorylated form of DAPK2 (PubMed:26047703). Interacts with DENND1A
CC (By similarity). Interacts with GAB2 (By similarity). Interacts with
CC phosphorylated GRB10 (PubMed:15722337). Interacts with KSR1
CC (PubMed:10409742). Interacts with NDEL1 (PubMed:12796778). Interacts
CC with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with the
CC phosphorylated (by AKT1) form of SRPK2 (By similarity). Interacts with
CC TIAM2 (PubMed:17320046). Interacts with the 'Ser-1134' and 'Ser-1161'
CC phosphorylated form of SOS1 (By similarity). Interacts with ZFP36 (via
CC phosphorylated form) (PubMed:21078877). Interacts with SLITRK1 (By
CC similarity). Interacts with HSF1 (via phosphorylated form); this
CC interaction promotes HSF1 sequestration in the cytoplasm in a ERK-
CC dependent manner (By similarity). Interacts with RIPOR2 (By
CC similarity). Interacts with KLHL22; required for the nuclear
CC localization of KLHL22 upon amino acid starvation (By similarity).
CC Interacts with CRTC1 (PubMed:30611118). Interacts with CRTC2 (probably
CC when phosphorylated at 'Ser-171') (PubMed:30611118). Interacts with
CC CRTC3 (probably when phosphorylated at 'Ser-162' and/or 'Ser-273')
CC (PubMed:30611118). Interacts with ATP2B1 and ATP2B3; this interaction
CC inhibits calcium-transporting ATPase activity (By similarity).
CC Interacts with MEFV (By similarity). {ECO:0000250|UniProtKB:P62258,
CC ECO:0000250|UniProtKB:P62260, ECO:0000269|PubMed:10409742,
CC ECO:0000269|PubMed:11278287, ECO:0000269|PubMed:11533041,
CC ECO:0000269|PubMed:12796778, ECO:0000269|PubMed:15722337,
CC ECO:0000269|PubMed:17320046, ECO:0000269|PubMed:21078877,
CC ECO:0000269|PubMed:26047703, ECO:0000269|PubMed:30611118}.
CC -!- INTERACTION:
CC P62259; Q8CHQ0: Fbxo4; NbExp=2; IntAct=EBI-356480, EBI-3895153;
CC P62259; Q8C2B3: Hdac7; NbExp=5; IntAct=EBI-356480, EBI-643830;
CC P62259; Q5S006: Lrrk2; NbExp=4; IntAct=EBI-356480, EBI-2693710;
CC P62259; Q9ERR1: Ndel1; NbExp=7; IntAct=EBI-356480, EBI-646668;
CC P62259; Q64163-4: Tfdp2; NbExp=6; IntAct=EBI-356480, EBI-8077763;
CC P62259; O35244: Prdx6; Xeno; NbExp=2; IntAct=EBI-356480, EBI-915490;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62258}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62258}. Melanosome
CC {ECO:0000250|UniProtKB:P62258}.
CC -!- DEVELOPMENTAL STAGE: In the 8.5 dpc embryo, expressed throughout the
CC embryo. Within a day, expression was more marked in mesenchyme than
CC elsewhere (e.g. epithelial tissue, where it was generally low),
CC although levels in neural tissue rose again by about 12.5 dpc. This
CC difference was maintained until 15.5 dpc when expression levels started
CC to drop in most tissues, with those of the nervous system, tooth, and
CC kidney being exceptions. Strongly expressed in early mesenchyme. The
CC expression decreased as the mesenchyme differentiated.
CC {ECO:0000269|PubMed:7750640}.
CC -!- DISRUPTION PHENOTYPE: Knockouts show reduced viability with reduced
CC growth and a shortened skull (PubMed:30973865). Mutants show increased
CC thresholds across all frequencies associated with variable amounts of
CC accumulated fluid and exudate containing inflammatory cells in the
CC middle ear, suggesting predisposition to otitis media. The middle ear
CC mucosa appear thickened with granulation tissue in sections and the
CC luminal surface show an open Eustachian tube but abundant clusters of
CC goblet cells with fewer ciliated epithelial cells (PubMed:30973865).
CC {ECO:0000269|PubMed:30973865}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z19599; CAA79659.1; -; mRNA.
DR EMBL; D87663; BAA13424.1; -; mRNA.
DR EMBL; AF483478; AAL90752.1; -; mRNA.
DR EMBL; AF483479; AAL90753.1; -; mRNA.
DR EMBL; BC058686; AAH58686.1; -; mRNA.
DR CCDS; CCDS25056.1; -.
DR PIR; I48337; S31975.
DR RefSeq; NP_033562.3; NM_009536.4.
DR AlphaFoldDB; P62259; -.
DR SMR; P62259; -.
DR BioGRID; 204619; 324.
DR IntAct; P62259; 43.
DR MINT; P62259; -.
DR STRING; 10090.ENSMUSP00000070993; -.
DR iPTMnet; P62259; -.
DR PhosphoSitePlus; P62259; -.
DR SwissPalm; P62259; -.
DR REPRODUCTION-2DPAGE; P62259; -.
DR EPD; P62259; -.
DR jPOST; P62259; -.
DR PaxDb; P62259; -.
DR PeptideAtlas; P62259; -.
DR PRIDE; P62259; -.
DR ProteomicsDB; 285810; -.
DR Antibodypedia; 1898; 498 antibodies from 40 providers.
DR DNASU; 22627; -.
DR Ensembl; ENSMUST00000067664; ENSMUSP00000070993; ENSMUSG00000020849.
DR GeneID; 22627; -.
DR KEGG; mmu:22627; -.
DR UCSC; uc007ket.2; mouse.
DR CTD; 7531; -.
DR MGI; MGI:894689; Ywhae.
DR VEuPathDB; HostDB:ENSMUSG00000020849; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244964; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; P62259; -.
DR OMA; IPCATTG; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P62259; -.
DR TreeFam; TF102003; -.
DR Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-MMU-2028269; Signaling by Hippo.
DR Reactome; R-MMU-205025; NADE modulates death signalling.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-3371511; HSF1 activation.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 22627; 19 hits in 110 CRISPR screens.
DR ChiTaRS; Ywhae; mouse.
DR PRO; PR:P62259; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P62259; protein.
DR Bgee; ENSMUSG00000020849; Expressed in metanephric ureteric bud and 276 other tissues.
DR ExpressionAtlas; P62259; baseline and differential.
DR Genevisible; P62259; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0090724; C:central region of growth cone; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; ISO:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0050815; F:phosphoserine residue binding; ISO:MGI.
DR GO; GO:0015459; F:potassium channel regulator activity; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:1905913; P:negative regulation of calcium ion export across plasma membrane; ISO:MGI.
DR GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:1902309; P:negative regulation of peptidyl-serine dephosphorylation; ISO:MGI.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:MGI.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IDA:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0060306; P:regulation of membrane repolarization; ISO:MGI.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; ISO:MGI.
DR GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..255
FT /note="14-3-3 protein epsilon"
FT /id="PRO_0000058619"
FT REGION 234..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 57
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 130
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 50
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62260"
FT MOD_RES 69
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62260"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62260"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 232
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P62258"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62258"
SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64;
MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW
RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF
YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF
YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE
EQNKEALQDV EDENQ
