ID EPHB3_MOUSE Reviewed; 993 AA. AC P54754; Q62214; Q91YS9; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 24-JAN-2024, entry version 204. DE RecName: Full=Ephrin type-B receptor 3; DE EC=2.7.10.1; DE AltName: Full=Developmental kinase 5; DE Short=mDK-5; DE AltName: Full=Tyrosine-protein kinase receptor SEK-4; DE Flags: Precursor; GN Name=Ephb3; Synonyms=Etk2, Mdk5, Sek4; 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]. RC STRAIN=BALB/cJ; TISSUE=Embryo; RX PubMed=7478528; RA Ciossek T., Lerch M.M., Ullrich A.; RT "Cloning, characterization, and differential expression of MDK2 and MDK5, RT two novel receptor tyrosine kinases of the eck/eph family."; RL Oncogene 11:2085-2095(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 719-993. RC STRAIN=BALB/cJ; TISSUE=Brain; RX PubMed=7947319; DOI=10.1016/0925-4773(94)90091-4; RA Becker N., Seitanidou T., Murphy P., Mattei M.-G., Topilko P., Nieto A., RA Wilkinson D.G., Charnay P., Gilardi P.; RT "Several receptor tyrosine kinase genes of the Eph family are segmentally RT expressed in the developing hindbrain."; RL Mech. Dev. 47:3-17(1994). RN [4] RP DISRUPTION PHENOTYPE, FUNCTION IN AXON GUIDANCE, AND FUNCTION IN PALATE RP DEVELOPMENT. RX PubMed=8947026; DOI=10.1002/j.1460-2075.1996.tb00992.x; RA Orioli D., Henkemeyer M., Lemke G., Klein R., Pawson T.; RT "Sek4 and Nuk receptors cooperate in guidance of commissural axons and in RT palate formation."; RL EMBO J. 15:6035-6049(1996). RN [5] RP FUNCTION IN ANGIOGENESIS, AND DEVELOPMENTAL STAGE. RX PubMed=9990854; DOI=10.1101/gad.13.3.295; RA Adams R.H., Wilkinson G.A., Weiss C., Diella F., Gale N.W., Deutsch U., RA Risau W., Klein R.; RT "Roles of ephrinB ligands and EphB receptors in cardiovascular development: RT demarcation of arterial/venous domains, vascular morphogenesis, and RT sprouting angiogenesis."; RL Genes Dev. 13:295-306(1999). RN [6] RP TISSUE SPECIFICITY. RX PubMed=10704386; DOI=10.1242/dev.127.7.1397; RA Imondi R., Wideman C., Kaprielian Z.; RT "Complementary expression of transmembrane ephrins and their receptors in RT the mouse spinal cord: a possible role in constraining the orientation of RT longitudinally projecting axons."; RL Development 127:1397-1410(2000). RN [7] RP FUNCTION IN INTESTINAL EPITHELIUM DIFFERENTIATION, DEVELOPMENTAL STAGE, AND RP TISSUE SPECIFICITY. RX PubMed=12408869; DOI=10.1016/s0092-8674(02)01015-2; RA Batlle E., Henderson J.T., Beghtel H., van den Born M.M., Sancho E., RA Huls G., Meeldijk J., Robertson J., van de Wetering M., Pawson T., RA Clevers H.; RT "Beta-catenin and TCF mediate cell positioning in the intestinal epithelium RT by controlling the expression of EphB/ephrinB."; RL Cell 111:251-263(2002). RN [8] RP FUNCTION IN DENDRITIC SPINE DEVELOPMENT, FUNCTION IN EXCITATORY SYNAPSE RP FORMATION, AND SUBCELLULAR LOCATION. RX PubMed=14691139; DOI=10.1083/jcb.200306033; RA Henkemeyer M., Itkis O.S., Ngo M., Hickmott P.W., Ethell I.M.; RT "Multiple EphB receptor tyrosine kinases shape dendritic spines in the RT hippocampus."; RL J. Cell Biol. 163:1313-1326(2003). RN [9] RP FUNCTION IN URORECTAL DEVELOPMENT. RX PubMed=15223334; DOI=10.1016/j.ydbio.2004.03.027; RA Dravis C., Yokoyama N., Chumley M.J., Cowan C.A., Silvany R.E., Shay J., RA Baker L.A., Henkemeyer M.; RT "Bidirectional signaling mediated by ephrin-B2 and EphB2 controls urorectal RT development."; RL Dev. Biol. 271:272-290(2004). RN [10] RP FUNCTION IN THYMUS DEVELOPMENT. RX PubMed=19598115; DOI=10.1387/ijdb.082702jg; RA Garcia-Ceca J., Jimenez E., Alfaro D., Cejalvo T., Chumley M.J., RA Henkemeyer M., Munoz J.J., Zapata A.G.; RT "On the role of Eph signalling in thymus histogenesis; EphB2/B3 and the RT organizing of the thymic epithelial network."; RL Int. J. Dev. Biol. 53:971-982(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; 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 [12] 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 CC transmembrane ephrin-B family ligands residing on adjacent cells, CC leading to contact-dependent bidirectional signaling into neighboring CC cells. The signaling pathway downstream of the receptor is referred to CC as forward signaling while the signaling pathway downstream of the CC ephrin ligand is referred to as reverse signaling. Generally has an CC overlapping and redundant function with EPHB2. Like EPHB2, functions in CC axon guidance during development regulating for instance the neurons CC forming the corpus callosum and the anterior commissure, 2 major CC interhemispheric connections between the temporal lobes of the cerebral CC cortex. In addition to its role in axon guidance also plays an CC important redundant role with other ephrin-B receptors in development CC and maturation of dendritic spines and the formation of excitatory CC synapses. Controls other aspects of development through regulation of CC cell migration and positioning. This includes angiogenesis, palate CC development and thymic epithelium development for instance. Forward and CC reverse signaling through the EFNB2/EPHB3 complex also regulate CC migration and adhesion of cells that tubularize the urethra and septate CC the cloaca. Finally, plays an important role in intestinal epithelium CC differentiation segregating progenitor from differentiated cells in the CC crypt. {ECO:0000269|PubMed:12408869, ECO:0000269|PubMed:14691139, CC ECO:0000269|PubMed:15223334, ECO:0000269|PubMed:19598115, CC ECO:0000269|PubMed:8947026, ECO:0000269|PubMed:9990854}. 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). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14691139}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:14691139}. Cell CC projection, dendrite {ECO:0000269|PubMed:14691139}. CC -!- TISSUE SPECIFICITY: Expressed in cells of the retinal ganglion cell CC layer during retinal axon guidance to the optic disk. Expressed by CC Paneth and progenitor cells in the crypts of the intestinal epithelium CC (at protein level). Expressed in myogenic progenitor cells CC (PubMed:27446912). {ECO:0000269|PubMed:10704386, CC ECO:0000269|PubMed:12408869, ECO:0000269|PubMed:27446912}. CC -!- DEVELOPMENTAL STAGE: Expressed during development in yolk sacs and by CC embryonic endothelial cells. Expressed in the developing intestinal CC epithelium at the bottom of the intervillus pockets where CC undifferentiated cells are allocated (at protein level). In myogenic CC progenitor cells, highly expressed during early development (11.5 dpc) CC and progressively repressed as developments proceeds (PubMed:27446912). CC {ECO:0000269|PubMed:12408869, ECO:0000269|PubMed:27446912, CC ECO:0000269|PubMed:9990854}. CC -!- PTM: Phosphorylated. Autophosphorylates upon ligand-binding. CC Autophosphorylation on Tyr-609 is required for interaction with SH2 CC domain-containing proteins (By similarity). {ECO:0000250}. CC -!- PTM: Ubiquitinated by RNF186, mainly through 'Lys-48' and 'Lys-63'- CC linked polyubiquitin chains. {ECO:0000250|UniProtKB:P54753}. CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile and show no obvious CC abnormal behavior. The corpus callosum, the main axon tract connecting CC the left and right cerebral hemispheres, is not formed in a significant CC fraction of newborns. This is associated with defects in guidance of CC callosal axons across the midline. {ECO:0000269|PubMed:8947026}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159}. 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; Z49086; CAA88910.1; -; mRNA. DR EMBL; BC014822; AAH14822.1; -; mRNA. DR EMBL; BC053085; AAH53085.1; -; mRNA. DR EMBL; X76012; CAA53599.1; -; mRNA. DR CCDS; CCDS28060.1; -. DR PIR; I48653; I48653. DR PIR; I48761; I48761. DR RefSeq; NP_034273.1; NM_010143.1. DR AlphaFoldDB; P54754; -. DR SMR; P54754; -. DR BioGRID; 199477; 13. DR STRING; 10090.ENSMUSP00000006112; -. DR BindingDB; P54754; -. DR ChEMBL; CHEMBL4739678; -. DR GuidetoPHARMACOLOGY; 1832; -. DR GlyCosmos; P54754; 2 sites, No reported glycans. DR GlyGen; P54754; 2 sites. DR iPTMnet; P54754; -. DR PhosphoSitePlus; P54754; -. DR MaxQB; P54754; -. DR PaxDb; 10090-ENSMUSP00000006112; -. DR PeptideAtlas; P54754; -. DR ProteomicsDB; 275627; -. DR Pumba; P54754; -. DR Antibodypedia; 2107; 658 antibodies from 37 providers. DR DNASU; 13845; -. DR Ensembl; ENSMUST00000006112.7; ENSMUSP00000006112.7; ENSMUSG00000005958.16. DR GeneID; 13845; -. DR KEGG; mmu:13845; -. DR UCSC; uc007yrg.1; mouse. DR AGR; MGI:104770; -. DR CTD; 2049; -. DR MGI; MGI:104770; Ephb3. DR VEuPathDB; HostDB:ENSMUSG00000005958; -. DR eggNOG; KOG0196; Eukaryota. DR GeneTree; ENSGT00940000158024; -. DR HOGENOM; CLU_000288_141_0_1; -. DR InParanoid; P54754; -. DR OMA; TSACSRC; -. DR OrthoDB; 1614410at2759; -. DR PhylomeDB; P54754; -. DR TreeFam; TF315608; -. DR BRENDA; 2.7.10.1; 3474. DR Reactome; R-MMU-2682334; EPH-Ephrin signaling. DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling. DR Reactome; R-MMU-3928664; Ephrin signaling. DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells. DR BioGRID-ORCS; 13845; 2 hits in 81 CRISPR screens. DR ChiTaRS; Ephb3; mouse. DR PRO; PR:P54754; -. DR Proteomes; UP000000589; Chromosome 16. DR RNAct; P54754; Protein. DR Bgee; ENSMUSG00000005958; Expressed in saccule of membranous labyrinth and 238 other cell types or tissues. DR ExpressionAtlas; P54754; baseline and differential. DR GO; GO:0030425; C:dendrite; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008046; F:axon guidance receptor activity; IDA:MGI. DR GO; GO:0005003; F:ephrin receptor activity; ISS:UniProtKB. DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central. DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB. DR GO; GO:0007411; P:axon guidance; IDA:MGI. DR GO; GO:0007413; P:axonal fasciculation; IMP:UniProtKB. DR GO; GO:0016477; P:cell migration; IMP:UniProtKB. DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IDA:MGI. DR GO; GO:0022038; P:corpus callosum development; IMP:UniProtKB. DR GO; GO:0060996; P:dendritic spine development; IMP:UniProtKB. DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:UniProtKB. DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:UniProtKB. DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB. DR GO; GO:0050770; P:regulation of axonogenesis; IDA:UniProtKB. DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB. DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB. DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:MGI. DR GO; GO:0060021; P:roof of mouth development; IMP:UniProtKB. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB. DR GO; GO:0048538; P:thymus development; IMP:UniProtKB. DR GO; GO:0001655; P:urogenital system development; IMP:UniProtKB. DR CDD; cd10478; EphR_LBD_B3; 1. DR CDD; cd00063; FN3; 2. DR CDD; cd05065; PTKc_EphR_B; 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; IPR034245; EphB3_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; 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:SF6; EPHRIN TYPE-B 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; PF00536; SAM_1; 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; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 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. DR Genevisible; P54754; MM. PE 1: Evidence at protein level; KW Angiogenesis; ATP-binding; Cell membrane; Cell projection; KW Developmental protein; Disulfide bond; 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..29 FT /evidence="ECO:0000255" FT CHAIN 30..993 FT /note="Ephrin type-B receptor 3" FT /id="PRO_0000016832" FT TOPO_DOM 30..554 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 555..575 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 576..993 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 31..209 FT /note="Eph LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883" FT DOMAIN 331..446 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 447..540 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 628..891 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 920..984 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT MOTIF 991..993 FT /note="PDZ-binding" FT /evidence="ECO:0000255" FT ACT_SITE 753 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 634..642 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 660 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 609 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P54753" FT CARBOHYD 343 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 440 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 73..191 FT /evidence="ECO:0000250" FT CONFLICT 200..201 FT /note="FY -> GD (in Ref. 1; CAA88910)" FT /evidence="ECO:0000305" FT CONFLICT 331 FT /note="V -> E (in Ref. 1; CAA88910)" FT /evidence="ECO:0000305" FT CONFLICT 567 FT /note="V -> M (in Ref. 1; CAA88910)" FT /evidence="ECO:0000305" FT CONFLICT 719 FT /note="R -> Q (in Ref. 3; CAA53599)" FT /evidence="ECO:0000305" SQ SEQUENCE 993 AA; 109662 MW; 07C6EF2AC98AE1B4 CRC64; MAGARPPPGL LPLLAPLLLP LLLPAGCWAL EETLMDTKWV TSELAWTSHP ESGWEEVSGY DEAMNPIRTY QVCNVRESSQ NNWLRTGFIW RREVQRVYVE LKFTVRDCNS IPNIPGSCKE TFNLFYYEAD SDVASASSPF WMENPYVKVD TIAPDESFSR LDAGRVNTKV RSFGPLSKAG FYLAFQDQGA CMSLISVRAF YKKCASTTAG FALFPETLTG AEPTSLVIAP GTCIANAVEV SVPLKLYCNG DGEWMVPVGA CTCATGHEPA AKESQCRACP PGSYKAKQGE GPCLPCPPNS RTTSPAASIC TCHNNFYRAD SDSADSACTT VPSPPRGVIS NVNETSLILE WSEPRDLGGR DDLLYNVICK KCRGSSGAGG PATCSRCDDN VEFVPRQLGL TERRVHISHL LAHTRYTFEV QAVNGVSGKS PLPPRYAAVN ITTNQAAPSE VPTLHLHSSS GSSLTLSWAP PERPNGVILD YEMKYFEKSK GIASTVTSQK NSVQLDGLQP DARYVVQVRA RTVAGYGQYS HPAEFETTSE RGSGAQQLQE QLPLIVGSTV AGFVFMVVVV VIALVCLRKQ RHGPDAEYTE KLQQYIAPGM KVYIDPFTYE DPNEAVREFA KEIDVSCVKI EEVIGAGEFG EVCRGRLKLP GRREVFVAIK TLKVGYTERQ RRDFLSEASI MGQFDHPNII RLEGVVTKSR PVMILTEFME NCALDSFLRL NDGQFTVIQL VGMLRGIAAG MKYLSEMNYV HRDLAARNIL VNSNLVCKVS DFGLSRFLED DPSDPTYTSS LGGKIPIRWT APEAIAYRKF TSASDVWSYG IVMWEVMSYG ERPYWDMSNQ DVINAVEQDY RLPPPMDCPT ALHQLMLDCW VRDRNLRPKF SQIVNTLDKL IRNAASLKVT ASAPSGMSQP LLDRTVPDYT TFTTVGDWLD AIKMGRYKES FVGAGFASFD LVAQMTAEDL LRIGVTLAGH QKKILCSIQD MRLQMNQTLP VQV //