EPHA8_MOUSE
ID EPHA8_MOUSE Reviewed; 1004 AA.
AC O09127; A3KG07;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Ephrin type-A receptor 8;
DE EC=2.7.10.1;
DE AltName: Full=EPH- and ELK-related kinase;
DE AltName: Full=Tyrosine-protein kinase receptor EEK;
DE Flags: Precursor;
GN Name=Epha8; Synonyms=Eek;
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], INTERACTION WITH EFNA2; EFNA3 AND EFNA5,
RP PHOSPHORYLATION, TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=9053851; DOI=10.1038/sj.onc.1200857;
RA Park S., Sanchez M.P.;
RT "The Eek receptor, a member of the Eph family of tyrosine protein kinases,
RT can be activated by three different Eph family ligands.";
RL Oncogene 14:533-542(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION IN AXON GUIDANCE, AND DEVELOPMENTAL STAGE.
RX PubMed=9214628; DOI=10.1093/emboj/16.11.3106;
RA Park S., Frisen J., Barbacid M.;
RT "Aberrant axonal projections in mice lacking EphA8 (Eek) tyrosine protein
RT kinase receptors.";
RL EMBO J. 16:3106-3114(1997).
RN [4]
RP FUNCTION IN CELL ADHESION, INTERACTION WITH FYN, PHOSPHORYLATION AT TYR-615
RP AND TYR-838, AND MUTAGENESIS OF TYR-615 AND TYR-838.
RX PubMed=10498895; DOI=10.1038/sj.onc.1202917;
RA Choi S., Park S.;
RT "Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn
RT binding to the Tyr-615 site by enhancing tyrosine kinase activity.";
RL Oncogene 18:5413-5422(1999).
RN [5]
RP FUNCTION IN INTEGRIN-MEDIATED CELL ADHESION, MUTAGENESIS OF TYR-615;
RP LYS-666 AND TYR-792, AND INTERACTION WITH PIK3CG.
RX PubMed=11416136; DOI=10.1128/mcb.21.14.4579-4597.2001;
RA Gu C., Park S.;
RT "The EphA8 receptor regulates integrin activity through p110gamma
RT phosphatidylinositol-3 kinase in a tyrosine kinase activity-independent
RT manner.";
RL Mol. Cell. Biol. 21:4579-4597(2001).
RN [6]
RP FUNCTION IN CELL MIGRATION.
RX PubMed=12681484; DOI=10.1016/s0014-5793(03)00223-0;
RA Gu C., Park S.;
RT "The p110 gamma PI-3 kinase is required for EphA8-stimulated cell
RT migration.";
RL FEBS Lett. 540:65-70(2003).
RN [7]
RP FUNCTION IN MAP KINASE ACTIVATION AND NEURITE OUTGROWTH, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15782114; DOI=10.1038/sj.onc.1208584;
RA Gu C., Shim S., Shin J., Kim J., Park J., Han K., Park S.;
RT "The EphA8 receptor induces sustained MAP kinase activation to promote
RT neurite outgrowth in neuronal cells.";
RL Oncogene 24:4243-4256(2005).
RN [8]
RP FUNCTION IN CELL MIGRATION AND NEURITE RETRACTION NOTICE OF
RP PUBMED:15782114, INTERACTION WITH ANKS1A AND ANKS1B, AND SUBCELLULAR
RP LOCATION.
RX PubMed=17875921; DOI=10.1128/mcb.00794-07;
RA Shin J., Gu C., Park E., Park S.;
RT "Identification of phosphotyrosine binding domain-containing proteins as
RT novel downstream targets of the EphA8 signaling function.";
RL Mol. Cell. Biol. 27:8113-8126(2007).
RN [9]
RP UBIQUITINATION BY CBL, AND INTERACTION WITH ANKS1A.
RX PubMed=20100865; DOI=10.1128/mcb.01605-09;
RA Kim J., Lee H., Kim Y., Yoo S., Park E., Park S.;
RT "The SAM domains of Anks family proteins are critically involved in
RT modulating the degradation of EphA receptors.";
RL Mol. Cell. Biol. 30:1582-1592(2010).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TIAM1.
RX PubMed=20496116; DOI=10.1007/s10059-010-0075-2;
RA Yoo S., Shin J., Park S.;
RT "EphA8-ephrinA5 signaling and clathrin-mediated endocytosis is regulated by
RT Tiam-1, a Rac-specific guanine nucleotide exchange factor.";
RL Mol. Cells 29:603-609(2010).
CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI-
CC anchored ephrin-A family ligands residing on adjacent cells, leading to
CC contact-dependent bidirectional signaling into neighboring cells. The
CC signaling pathway downstream of the receptor is referred to as forward
CC signaling while the signaling pathway downstream of the ephrin ligand
CC is referred to as reverse signaling. The GPI-anchored ephrin-A EFNA2,
CC EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation.
CC With EFNA5 may regulate integrin-mediated cell adhesion and migration
CC on fibronectin substrate but also neurite outgrowth. During development
CC of the nervous system also plays a role in axon guidance. Downstream
CC effectors of the EPHA8 signaling pathway include FYN which promotes
CC cell adhesion upon activation by EPHA8 and the MAP kinases in the
CC stimulation of neurite outgrowth. {ECO:0000269|PubMed:10498895,
CC ECO:0000269|PubMed:11416136, ECO:0000269|PubMed:12681484,
CC ECO:0000269|PubMed:15782114, ECO:0000269|PubMed:17875921,
CC ECO:0000269|PubMed:9214628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer
CC is composed of an ephrin dimer and a receptor dimer. Oligomerization is
CC probably required to induce biological responses (By similarity). May
CC also form heterodimers with other ephrin receptors. Interacts with FYN;
CC possible downstream effector of EPHA8 in regulation of cell adhesion.
CC Interacts with PIK3CG; regulates integrin-mediated cell adhesion to
CC substrate. Interacts with TIAM1; regulates clathrin-mediated
CC endocytosis of EPHA8. Interacts with ANKS1A and ANKS1B; EPHA8 kinase
CC activity-independent but stimulated by EPHA8 ubiquitination.
CC {ECO:0000250, ECO:0000269|PubMed:10498895, ECO:0000269|PubMed:11416136,
CC ECO:0000269|PubMed:17875921, ECO:0000269|PubMed:20100865,
CC ECO:0000269|PubMed:20496116, ECO:0000269|PubMed:9053851}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9053851};
CC Single-pass type I membrane protein {ECO:0000255}. Cell projection
CC {ECO:0000269|PubMed:17875921}. Early endosome membrane
CC {ECO:0000269|PubMed:20496116}. Note=Undergoes clathrin-mediated
CC endocytosis upon EFNA5-binding and is targeted to early endosomes
CC (PubMed:20496116). {ECO:0000269|PubMed:20496116}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the central nervous
CC system.
CC -!- DEVELOPMENTAL STAGE: First detected at 10.5 dpc with high levels near
CC the midline region of the tectum and to a lower extent in discrete
CC regions of hindbrain, the dorsal horn, of the spinal cord and in the
CC naso-lacrimal groove. The expression decreases at 12.5 dpc and is
CC barely detectable at 17.5 dpc. Not detected at postnatal stages.
CC {ECO:0000269|PubMed:9214628}.
CC -!- PTM: Phosphorylated. Phosphorylation is stimulated upon binding of its
CC ligands including EFNA2, EFNA3 and EFNA5. Autophosphorylation on Tyr-
CC 615 is critical for association with FYN. Autophosphorylation on Tyr-
CC 838 modulates tyrosine kinase activity. {ECO:0000269|PubMed:10498895,
CC ECO:0000269|PubMed:9053851}.
CC -!- PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor
CC stability and activity through proteasomal degradation. ANKS1A prevents
CC ubiquitination and degradation. {ECO:0000269|PubMed:20100865}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; U72207; AAB39218.1; -; mRNA.
DR EMBL; AL627214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18813.1; -.
DR RefSeq; NP_031965.2; NM_007939.2.
DR AlphaFoldDB; O09127; -.
DR BMRB; O09127; -.
DR SMR; O09127; -.
DR BioGRID; 199475; 11.
DR IntAct; O09127; 1.
DR MINT; O09127; -.
DR STRING; 10090.ENSMUSP00000030420; -.
DR BindingDB; O09127; -.
DR ChEMBL; CHEMBL4739670; -.
DR GuidetoPHARMACOLOGY; 1828; -.
DR GlyGen; O09127; 3 sites.
DR iPTMnet; O09127; -.
DR PhosphoSitePlus; O09127; -.
DR MaxQB; O09127; -.
DR PaxDb; O09127; -.
DR PeptideAtlas; O09127; -.
DR PRIDE; O09127; -.
DR ProteomicsDB; 277885; -.
DR Antibodypedia; 4046; 172 antibodies from 33 providers.
DR DNASU; 13842; -.
DR Ensembl; ENSMUST00000030420; ENSMUSP00000030420; ENSMUSG00000028661.
DR GeneID; 13842; -.
DR KEGG; mmu:13842; -.
DR UCSC; uc008vis.1; mouse.
DR CTD; 2046; -.
DR MGI; MGI:109378; Epha8.
DR VEuPathDB; HostDB:ENSMUSG00000028661; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000160469; -.
DR HOGENOM; CLU_000288_141_4_1; -.
DR InParanoid; O09127; -.
DR OMA; MRMNIDD; -.
DR OrthoDB; 933071at2759; -.
DR PhylomeDB; O09127; -.
DR TreeFam; TF315608; -.
DR BRENDA; 2.7.10.1; 3474.
DR Reactome; R-MMU-2682334; EPH-Ephrin signaling.
DR Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR BioGRID-ORCS; 13842; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Epha8; mouse.
DR PRO; PR:O09127; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O09127; protein.
DR Bgee; ENSMUSG00000028661; Expressed in future diencephalon and 69 other tissues.
DR Genevisible; O09127; MM.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005004; F:GPI-linked ephrin receptor activity; IDA:UniProtKB.
DR GO; GO:0019838; F:growth factor binding; IPI:ARUK-UCL.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IDA:MGI.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
DR GO; GO:0016322; P:neuron remodeling; IDA:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IDA:UniProtKB.
DR GO; GO:0006929; P:substrate-dependent cell migration; IDA:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd10486; EphR_LBD_A8; 1.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034287; EphA8_rcpt_lig-bd.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR020691; EphrinA_rcpt8.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR PANTHER; PTHR24416:SF339; PTHR24416:SF339; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell adhesion; Cell membrane; Cell projection;
KW Developmental protein; Endosome; Glycoprotein; Kinase; Membrane;
KW Neurogenesis; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1004
FT /note="Ephrin type-A receptor 8"
FT /id="PRO_0000016823"
FT TOPO_DOM 27..541
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..1004
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..208
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 327..437
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 438..533
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 634..895
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 929..993
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 563..569
FT /note="Mediates interaction with ANKS1A and ANKS1B"
FT /evidence="ECO:0000269|PubMed:17875921"
FT REGION 588..643
FT /note="Mediates interaction with PIK3CG and required for
FT endocytosis"
FT /evidence="ECO:0000269|PubMed:11416136"
FT MOTIF 1002..1004
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 759
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 640..648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 666
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 615
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10498895"
FT MOD_RES 838
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:10498895"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 615
FT /note="Y->F: Reduced phosphorylation and reduced
FT association with FYN."
FT /evidence="ECO:0000269|PubMed:10498895,
FT ECO:0000269|PubMed:11416136"
FT MUTAGEN 666
FT /note="K->M,R: Kinase-dead. Loss of autophosphorylation but
FT has no effect on regulation of cell adhesion."
FT /evidence="ECO:0000269|PubMed:11416136"
FT MUTAGEN 792
FT /note="Y->F: Reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:11416136"
FT MUTAGEN 838
FT /note="Y->F: Reduced tyrosine kinase activity."
FT /evidence="ECO:0000269|PubMed:10498895"
FT CONFLICT 1000
FT /note="P -> R (in Ref. 1; AAB39218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1004 AA; 110705 MW; 8530E8002A6FE502 CRC64;
MAPARARLSP ALWVVTAAAA ATCVSAGRGE VNLLDTSTIH GDWGWLTYPA HGWDSINEVD
ESFRPIHTYQ VCNVMSPNQN NWLRTNWVPR DGARRVYAEI KFTLRDCNSI PGVLGTCKET
FNLHYLESDR DLGASTQESQ FLKIDTIAAD ESFTGADLGV RRLKLNTEVR GVGPLSKRGF
YLAFQDIGAC LAILSLRIYY KKCPAMVRNL AAFSEAVTGA DSSSLVEVRG QCVRHSEERD
TPKMYCSAEG EWLVPIGKCV CSAGYEERRD ACMACELGFY KSAPGDQLCA RCPPHSHSAT
PAAQTCRCDL SYYRAALDPP SAACTRPPSA PVNLISSVNG TSVTLEWAPP LDPGGRSDIT
YNAVCRRCPW ALSHCEACGS GTRFVPQQTS LAQASLLVAN LLAHMNYSFW IEAVNGVSNL
SPEPRSAAVV NITTNQAAPS QVVVIRQERA GQTSVSLLWQ EPEQPNGIIL EYEIKYYEKD
KEMQSYSTLK AVTTRATVSG LKPGTRYVFQ VRARTSAGCG RFSQAMEVET GKPRPRYDTR
TIVWICLTLI TGLVVLLLLL ICKKRHCGYS KAFQDSDEEK MHYQNGQAPP PVFLPLNHPP
GKFPETQFSA EPHTYEEPGR AGRSFTREIE ASRIHIEKII GSGESGEVCY GRLQVPGQRD
VPVAIKALKA GYTERQRQDF LSEAAIMGQF DHPNIIRLEG VVTRGRLAMI VTEYMENGSL
DAFLRTHDGQ FTIVQLVGML RGVGAGMRYL SDLGYIHRDL AARNVLVDGR LVCKVSDFGL
SRALEDDPEA AYTTAGGKIP IRWTAPEAIA FRTFSSASDV WSFGVVMWEV LAYGERPYWN
MTNQDVISSV EEGYRLPAPM GCPRALHQLM LDCWHKDRAQ RPRFAHVVSV LDALVHSPES
LRATATVSRC PPPAFARSCF DLRAGGSGNG DLTVGDWLDS IRMGRYRDHF AAGGYSSLGM
VLRMNAQDVR ALGITLMGHQ KKILGSIQTM RAQLSSTQGP RRHL
