EPHB3_MOUSE
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 03-AUG-2022, entry version 196.
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}.
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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 GlyGen; P54754; 2 sites.
DR iPTMnet; P54754; -.
DR PhosphoSitePlus; P54754; -.
DR MaxQB; P54754; -.
DR PaxDb; P54754; -.
DR PeptideAtlas; P54754; -.
DR PRIDE; P54754; -.
DR ProteomicsDB; 275627; -.
DR Antibodypedia; 2107; 590 antibodies from 37 providers.
DR DNASU; 13845; -.
DR Ensembl; ENSMUST00000006112; ENSMUSP00000006112; ENSMUSG00000005958.
DR GeneID; 13845; -.
DR KEGG; mmu:13845; -.
DR UCSC; uc007yrg.1; mouse.
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; 933071at2759; -.
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 76 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 234 other tissues.
DR ExpressionAtlas; P54754; baseline and differential.
DR Genevisible; P54754; MM.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
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: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: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:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0001655; P:urogenital system development; IMP:UniProtKB.
DR CDD; cd10478; EphR_LBD_B3; 1.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
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 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; 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; 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 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
