ID EPHA3_MOUSE Reviewed; 983 AA.
AC P29319;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 08-NOV-2023, entry version 191.
DE RecName: Full=Ephrin type-A receptor 3;
DE EC=2.7.10.1;
DE AltName: Full=EPH-like kinase 4;
DE Short=EK4;
DE Short=mEK4;
DE AltName: Full=Tyrosine-protein kinase TYRO4;
DE AltName: Full=Tyrosine-protein kinase receptor ETK1;
DE Flags: Precursor;
GN Name=Epha3; Synonyms=Etk1, Mek4, Tyro4;
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] (ISOFORMS LONG AND SHORT).
RC STRAIN=ICR X Swiss Webster; TISSUE=Embryo;
RX PubMed=1657122;
RA Sajjadi F.G., Pasquale E.B., Subramani S.;
RT "Identification of a new eph-related receptor tyrosine kinase gene from
RT mouse and chicken that is developmentally regulated and encodes at least
RT two forms of the receptor.";
RL New Biol. 3:769-778(1991).
RN [2]
RP INTERACTION WITH CRK.
RX PubMed=11870224; DOI=10.1242/jcs.115.5.1059;
RA Lawrenson I.D., Wimmer-Kleikamp S.H., Lock P., Schoenwaelder S.M., Down M.,
RA Boyd A.W., Alewood P.F., Lackmann M.;
RT "Ephrin-A5 induces rounding, blebbing and de-adhesion of EphA3-expressing
RT 293T and melanoma cells by CrkII and Rho-mediated signalling.";
RL J. Cell Sci. 115:1059-1072(2002).
RN [3]
RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=14585969; DOI=10.1128/mcb.23.22.8092-8098.2003;
RA Vaidya A., Pniak A., Lemke G., Brown A.;
RT "EphA3 null mutants do not demonstrate motor axon guidance defects.";
RL Mol. Cell. Biol. 23:8092-8098(2003).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION IN HEART DEVELOPMENT, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17046737; DOI=10.1016/j.ydbio.2006.08.058;
RA Stephen L.J., Fawkes A.L., Verhoeve A., Lemke G., Brown A.;
RT "A critical role for the EphA3 receptor tyrosine kinase in heart
RT development.";
RL Dev. Biol. 302:66-79(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-937, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [6]
RP FUNCTION IN MOTOR AND SENSORY AXONS SEGREGATION.
RX PubMed=18403711; DOI=10.1126/science.1153758;
RA Gallarda B.W., Bonanomi D., Mueller D., Brown A., Alaynick W.A.,
RA Andrews S.E., Lemke G., Pfaff S.L., Marquardt T.;
RT "Segregation of axial motor and sensory pathways via heterotypic trans-
RT axonal signaling.";
RL Science 320:233-236(2008).
RN [7]
RP FUNCTION IN CELL MIGRATION, AND INTERACTION WITH NCK1.
RX PubMed=19505147; DOI=10.1021/bi900831k;
RA Hu T., Shi G., Larose L., Rivera G.M., Mayer B.J., Zhou R.;
RT "Regulation of process retraction and cell migration by EphA3 is mediated
RT by the adaptor protein Nck1.";
RL Biochemistry 48:6369-6378(2009).
RN [8]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT "Gene expression profiling of muscle stem cells identifies novel regulators
RT of postnatal myogenesis.";
RL Front. Cell Dev. Biol. 4:58-58(2016).
CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-
CC bound ephrin 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. Highly promiscuous for ephrin-A
CC ligands it binds preferentially EFNA5. Upon activation by EFNA5
CC regulates cell-cell adhesion, cytoskeletal organization and cell
CC migration. Plays a role in cardiac cells migration and differentiation
CC and regulates the formation of the atrioventricular canal and septum
CC during development probably through activation by EFNA1. Involved in
CC the retinotectal mapping of neurons. May also control the segregation
CC but not the guidance of motor and sensory axons during neuromuscular
CC circuit development. {ECO:0000269|PubMed:17046737,
CC ECO:0000269|PubMed:18403711, ECO:0000269|PubMed:19505147}.
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. Forms a ternary
CC EFNA5-EPHA3-ADAM10 complex mediating EFNA5 extracellular domain
CC shedding by ADAM10 which regulates the EFNA5-EPHA3 complex
CC internalization and function. Interacts (phosphorylated) with PTPN1;
CC dephosphorylates EPHA3 and may regulate its trafficking and function
CC (By similarity). Interacts (phosphorylated) with CRK; mediates EFNA5-
CC EPHA3 signaling through RHOA GTPase activation. Interacts with NCK1
CC (via SH2 domain); mediates EFNA5-EPHA3 signaling. {ECO:0000250,
CC ECO:0000269|PubMed:11870224, ECO:0000269|PubMed:19505147}.
CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane
CC {ECO:0000250|UniProtKB:P29320}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Isoform Short]: Secreted
CC {ECO:0000250|UniProtKB:P29320}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P29319-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P29319-3; Sequence=VSP_041882, VSP_041883;
CC -!- TISSUE SPECIFICITY: Greatest levels of expression occurring in the
CC brain, also detected in testis. Expressed in myogenic progenitor cells
CC (PubMed:27446912). {ECO:0000269|PubMed:27446912}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in heart during its
CC development by mesenchymal cells of the endocardial cushions. Expressed
CC in motor neurons at 11.5 dpc. In myogenic progenitor cells, highly
CC expressed, at least as early as 11.5 dpc, expression decreases until 4
CC weeks after birth (PubMed:27446912). {ECO:0000269|PubMed:14585969,
CC ECO:0000269|PubMed:17046737, ECO:0000269|PubMed:27446912}.
CC -!- PTM: Autophosphorylates upon activation by EFNA5. Phosphorylation on
CC Tyr-602 mediates interaction with NCK1. Dephosphorylated by PTPN1 (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice die perinatally due to cardiac failure.
CC {ECO:0000269|PubMed:14585969, ECO:0000269|PubMed:17046737}.
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; M68513; AAA39521.1; -; mRNA.
DR EMBL; M68515; AAA39522.1; -; mRNA.
DR PIR; A45583; A45583.
DR AlphaFoldDB; P29319; -.
DR SMR; P29319; -.
DR STRING; 10090.ENSMUSP00000066554; -.
DR BindingDB; P29319; -.
DR ChEMBL; CHEMBL2034794; -.
DR GuidetoPHARMACOLOGY; 1823; -.
DR GlyCosmos; P29319; 5 sites, No reported glycans.
DR GlyGen; P29319; 5 sites.
DR iPTMnet; P29319; -.
DR PhosphoSitePlus; P29319; -.
DR MaxQB; P29319; -.
DR PaxDb; 10090-ENSMUSP00000066554; -.
DR ProteomicsDB; 275753; -. [P29319-1]
DR ProteomicsDB; 275754; -. [P29319-3]
DR AGR; MGI:99612; -.
DR MGI; MGI:99612; Epha3.
DR eggNOG; KOG0196; Eukaryota.
DR InParanoid; P29319; -.
DR PhylomeDB; P29319; -.
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 ChiTaRS; Epha3; mouse.
DR PRO; PR:P29319; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P29319; Protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005003; F:ephrin receptor activity; IDA:MGI.
DR GO; GO:0005004; F:GPI-linked ephrin receptor activity; ISS:UniProtKB.
DR GO; GO:0019838; F:growth factor binding; IPI:ARUK-UCL.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IDA:MGI.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISO:MGI.
DR GO; GO:0003197; P:endocardial cushion development; IMP:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0097156; P:fasciculation of motor neuron axon; IMP:UniProtKB.
DR GO; GO:0097155; P:fasciculation of sensory neuron axon; IMP:UniProtKB.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISO:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IGI:MGI.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR CDD; cd10481; EphR_LBD_A3; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05066; PTKc_EphR_A; 1.
DR CDD; cd09544; SAM_EPH-A3; 1.
DR Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034266; EphA3_rcpt_lig-bd.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_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; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
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; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF12; EPHRIN TYPE-A RECEPTOR 3; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 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 Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Secreted; Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..983
FT /note="Ephrin type-A receptor 3"
FT /id="PRO_0000016803"
FT TOPO_DOM 21..540
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..983
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..206
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 324..434
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 435..530
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 621..882
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 911..975
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT MOTIF 981..983
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 746
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 628..633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 700..706
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 750..751
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 596
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P29320"
FT MOD_RES 602
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P29320"
FT MOD_RES 701
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P29320"
FT MOD_RES 779
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P29320"
FT MOD_RES 937
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 531..537
FT /note="SFSISGE -> CMYYFSF (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:1657122"
FT /id="VSP_041882"
FT VAR_SEQ 538..983
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:1657122"
FT /id="VSP_041883"
SQ SEQUENCE 983 AA; 109955 MW; BE44A6655D8107A2 CRC64;
MDCHLSILVL LGCCVLSCSG ELSPQPSNEV NLLDSKTIQG ELGWISYPSH GWEEISGVDE
HYTPIRTYQV CNVMDHSQNN WLRTNWVPRN SAQKIYVELK FTLRDCNSIP LVLGTCKETF
NLYYMESDDH GVKFREHQFT KIDTIAADES FTQMDLGDRI LKLNTEIREV GPVNKKGFYL
AFQDVGACVA LVSVRVYFKK CPFTVKNLAM FPDTVPMDSQ SLVEVRGSCV NNSKEEDPPR
MYCSTEGEWL VPIGKCTCNA GYEERGFICQ ACRPGFYKAS DGAAKCAKCP PHSSTQEDGS
MNCRCENNYF RAEKDPPSMA CARPPSAPRN VISNINETSV ILDWSWPLDT GGRKDITFNI
ICKKCGWNVR QCEPCSPNVR FLPRQLGLTN TTVTVTDLLA HTNYTFEIDA VNGVSELSSP
PRQYAAVSIT TNQAAPSPVM TIKKDRTSRN SISLSWQEPE HPNGIILDYE VKYYQKQEQE
TSYTILRARG TNVTISSLKP DTTYVFQIRA RTAAGYGTNS RKFEFETSPD SFSISGENSH
VVMIAISAAV AIIVLTVVTY VLVGRFCGYH KSKHSAEEKR LHFGNGHLKL PGLRTYVDPH
TYEDPTQAVH EFAKELDATN ISIDKVVGAG EFGEVCSGRL KLPSKKEISV AIKTLKVGYT
EKQRRDFLGE ASIMGQFDHP NIIRLEGVVT KSKPEMIVTE YMENGSLDSF LRKHDAQFTV
IQLVGMLRGI ASGMKYLSDM GYVHRDLAAR NILINSNLVC KVSDFGLSRV LEDDPEAAYT
TRGGKIPIRW TSPEAMSYRK FTSASDVWSY GIVLWEVMSY GERPYSQMSN QDVIKAVDER
YRLPPPMDCP AALYQLMLDC WQKDRNNRPK FEQIVSILDK LIRNPGSLKI ITSAAARPSN
LLLDQSNVDI ATFHTTGDWL NGMRTAHCKE IFTGVEYSSC DTIAKISTDD MKKVGVTVVG
PQKKIISTIK ALETQSKNGP VPV
//
