ID EPHB2_MOUSE Reviewed; 986 AA. AC P54763; A3KG00; A3KG01; A3KG02; A3KG89; A3KG90; Q62213; Q6GTQ7; Q6P5F1; AC Q9QVY4; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2015, sequence version 3. DT 24-JAN-2024, entry version 225. DE RecName: Full=Ephrin type-B receptor 2 {ECO:0000305}; DE EC=2.7.10.1; DE AltName: Full=Neural kinase; DE AltName: Full=Nuk receptor tyrosine kinase; DE AltName: Full=Tyrosine-protein kinase receptor EPH-3; DE AltName: Full=Tyrosine-protein kinase receptor SEK-3; DE Contains: DE RecName: Full=EphB2/CTF1 {ECO:0000303|PubMed:17428795}; DE Contains: DE RecName: Full=EphB2/CTF2 {ECO:0000303|PubMed:17428795}; DE Flags: Precursor; GN Name=Ephb2 {ECO:0000312|MGI:MGI:99611}; GN Synonyms=Epth3, Nuk {ECO:0000303|PubMed:8134103}, Sek3 GN {ECO:0000312|MGI:MGI:99611}; 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 [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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-986 (ISOFORM 3). RX PubMed=8134103; RA Henkemeyer M., Marengere L.E., McGlade J., Olivier J.P., Conlon R.A., RA Holmyard D.P., Letwin K., Pawson T.; RT "Immunolocalization of the Nuk receptor tyrosine kinase suggests roles in RT segmental patterning of the brain and axonogenesis."; RL Oncogene 9:1001-1014(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 508-986 (ISOFORM 2). 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 [5] RP DISRUPTION PHENOTYPE, FUNCTION IN COMMISSURAL AXON GUIDANCE, SUBCELLULAR RP LOCATION, AND DEVELOPMENTAL STAGE. RX PubMed=8689685; DOI=10.1016/s0092-8674(00)80075-6; RA Henkemeyer M., Orioli D., Henderson J.T., Saxton T.M., Roder J., Pawson T., RA Klein R.; RT "Nuk controls pathfinding of commissural axons in the mammalian central RT nervous system."; RL Cell 86:35-46(1996). RN [6] RP FUNCTION IN AXON GUIDANCE, AND FUNCTION IN PALATE 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 [7] RP INTERACTION WITH PICK1 AND GRIP1, AND IDENTIFICATION OF PDZ-BINDING MOTIF. RX PubMed=9883737; DOI=10.1016/s0896-6273(00)80663-7; RA Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N., RA Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.; RT "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors RT and their ephrin ligands."; RL Neuron 21:1453-1463(1998). RN [8] 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 [9] RP INTERACTION WITH SH2D3C. RX PubMed=10542222; DOI=10.1074/jbc.274.45.31941; RA Dodelet V.C., Pazzagli C., Zisch A.H., Hauser C.A., Pasquale E.B.; RT "A novel signaling intermediate, SHEP1, directly couples Eph receptors to RT R-Ras and Rap1A."; RL J. Biol. Chem. 274:31941-31946(1999). RN [10] RP DEVELOPMENTAL STAGE. 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 [11] RP DISRUPTION PHENOTYPE, FUNCTION IN AXON GUIDANCE, FUNCTION IN INNER EAR RP DEVELOPMENT, INTERACTION WITH AQP1, TISSUE SPECIFICITY, AND DEVELOPMENTAL RP STAGE. RX PubMed=10839360; DOI=10.1016/s0896-6273(00)81174-5; RA Cowan C.A., Yokoyama N., Bianchi L.M., Henkemeyer M., Fritzsch B.; RT "EphB2 guides axons at the midline and is necessary for normal vestibular RT function."; RL Neuron 26:417-430(2000). RN [12] 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 [13] 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 [14] RP PROTEIN SEQUENCE OF 536-545, UBIQUITINATION, PHOSPHORYLATION, PROTEOLYTIC RP PROCESSING, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17428795; DOI=10.1074/jbc.m611449200; RA Litterst C., Georgakopoulos A., Shioi J., Ghersi E., Wisniewski T., RA Wang R., Ludwig A., Robakis N.K.; RT "Ligand binding and calcium influx induce distinct ectodomain/gamma- RT secretase-processing pathways of EphB2 receptor."; RL J. Biol. Chem. 282:16155-16163(2007). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-482. RC TISSUE=Myoblast; RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200; RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.; RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome: RT identification, glycosite occupancy, and membrane orientation."; RL Mol. Cell. Proteomics 8:2555-2569(2009). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-265. RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Kidney; 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 [18] RP FUNCTION IN EXCITATORY SYNAPSE FORMATION, FUNCTION IN PHOSPHORYLATION OF RP ARHGEF15, AND INTERACTION WITH ARHGEF15. RX PubMed=21029865; DOI=10.1016/j.cell.2010.09.038; RA Margolis S.S., Salogiannis J., Lipton D.M., Mandel-Brehm C., Wills Z.P., RA Mardinly A.R., Hu L., Greer P.L., Bikoff J.B., Ho H.Y., Soskis M.J., RA Sahin M., Greenberg M.E.; RT "EphB-mediated degradation of the RhoA GEF Ephexin5 relieves a RT developmental brake on excitatory synapse formation."; RL Cell 143:442-455(2010). RN [19] 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). RN [20] RP POLYUBIQUITINATION, INTERACTION WITH SPSB4, AND MUTAGENESIS OF TYR-596 AND RP TYR-602. RX PubMed=28931592; DOI=10.1091/mbc.e17-07-0450; RA Okumura F., Joo-Okumura A., Obara K., Petersen A., Nishikimi A., Fukui Y., RA Nakatsukasa K., Kamura T.; RT "Ubiquitin ligase SPSB4 diminishes cell repulsive responses mediated by RT EphB2."; RL Mol. Biol. Cell 28:3532-3541(2017). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-196. RX PubMed=9853759; DOI=10.1038/24904; RA Himanen J.-P., Henkemeyer M., Nikolov D.B.; RT "Crystal structure of the ligand-binding domain of the receptor tyrosine RT kinase EphB2."; RL Nature 396:486-491(1998). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-200 IN COMPLEX WITH EFNB2, RP DISULFIDE BOND, AND SUBUNIT. RX PubMed=11780069; DOI=10.1038/414933a; RA Himanen J.-P., Rajashankar K.R., Lackmann M., Cowan C.A., Henkemeyer M., RA Nikolov D.B.; RT "Crystal structure of an Eph receptor-ephrin complex."; RL Nature 414:933-938(2001). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-199 IN COMPLEX WITH EFNA5, AND RP INTERACTION WITH EFNA5. RX PubMed=15107857; DOI=10.1038/nn1237; RA Himanen J.P., Chumley M.J., Lackmann M., Li C., Barton W.A., Jeffrey P.D., RA Vearing C., Geleick D., Feldheim D.A., Boyd A.W., Henkemeyer M., RA Nikolov D.B.; RT "Repelling class discrimination: ephrin-A5 binds to and activates EphB2 RT receptor signaling."; RL Nat. Neurosci. 7:501-509(2004). 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. Functions in axon CC guidance during development. Involved in the guidance of commissural CC axons, that form a major interhemispheric connection between the 2 CC temporal lobes of the cerebral cortex. Also involved in guidance of CC contralateral inner ear efferent growth cones at the midline and of CC retinal ganglion cell axons to the optic disk. In addition to axon CC guidance, also regulates dendritic spines development and maturation CC and stimulates the formation of excitatory synapses. Upon activation by CC EFNB1, abolishes the ARHGEF15-mediated negative regulation on CC excitatory synapse formation. Controls other aspects of development CC including angiogenesis, palate development and in inner ear development CC through regulation of endolymph production. Forward and reverse CC signaling through the EFNB2/EPHB2 complex regulate movement and CC adhesion of cells that tubularize the urethra and septate the cloaca. CC May function as a tumor suppressor. May be involved in the regulation CC of platelet activation and blood coagulation (By similarity). CC {ECO:0000250|UniProtKB:P29323, ECO:0000269|PubMed:10839360, CC ECO:0000269|PubMed:14691139, ECO:0000269|PubMed:15223334, CC ECO:0000269|PubMed:21029865, ECO:0000269|PubMed:8689685, 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 (PubMed:11780069). CC The heterotetramer is composed of an ephrin dimer and a receptor dimer CC (PubMed:11780069). Interacts (via PDZ-binding motif) with GRIP1 and CC PICK1 (via PDZ domain) (PubMed:9883737). Interacts with ARHGEF15; CC mediates ARHGEF15 phosphorylation, ubiquitination and degradation by CC the proteasome (PubMed:21029865). Interacts with AQP1; involved in CC endolymph production in the inner ear (PubMed:10839360). Interacts with CC EFNA5 (PubMed:15107857). Interacts with SPSB1 (By similarity). CC Interacts with SPSB4 (PubMed:28931592). Interacts with SH2D3C CC (PubMed:10542222). {ECO:0000250|UniProtKB:P29323, CC ECO:0000269|PubMed:10542222, ECO:0000269|PubMed:10839360, CC ECO:0000269|PubMed:11780069, ECO:0000269|PubMed:15107857, CC ECO:0000269|PubMed:21029865, ECO:0000269|PubMed:28931592, CC ECO:0000269|PubMed:9883737}. CC -!- INTERACTION: CC P54763; PRO_0000000118 [P12023]: App; NbExp=4; IntAct=EBI-537711, EBI-14022231; CC P54763; Q5FWH6-2: Arhgef15; NbExp=3; IntAct=EBI-537711, EBI-2943608; CC P54763; Q03137: Epha4; NbExp=3; IntAct=EBI-537711, EBI-1539152; CC P54763; P54763: Ephb2; NbExp=2; IntAct=EBI-537711, EBI-537711; CC P54763; Q925T6: Grip1; NbExp=2; IntAct=EBI-537711, EBI-537752; CC P54763; P34152: Ptk2; NbExp=3; IntAct=EBI-537711, EBI-77070; CC P54763; P05480: Src; NbExp=3; IntAct=EBI-537711, EBI-298680; CC P54763; Q13009: TIAM1; Xeno; NbExp=3; IntAct=EBI-537711, EBI-1050007; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Cell projection, axon. Cell projection, dendrite. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=3 {ECO:0000305}; CC IsoId=P54763-3; Sequence=Displayed; CC Name=2 {ECO:0000305}; CC IsoId=P54763-2; Sequence=VSP_057933; CC Name=4 {ECO:0000305}; CC IsoId=P54763-4; Sequence=VSP_057932; CC -!- TISSUE SPECIFICITY: Expressed in the epithelial dark cells of the inner CC ear. Expressed in the region of the proximal tubules of the kidney CC nephron. Expressed in myogenic progenitor cells (PubMed:27446912). CC {ECO:0000269|PubMed:10839360, ECO:0000269|PubMed:27446912}. CC -!- DEVELOPMENTAL STAGE: Highly expressed in ventral cells of the neural CC tube and within axons of the peripheral nervous system during CC development. Expressed in the vestibulo-acoustic system and hindbrain CC as early as 11.5 dpc. Detected in the spinal cord at 12 dpc. Expressed CC in cells of the developing outer retina. Also expressed in mesenchyme CC adjacent to vessels. In myogenic progenitor cells, highly expressed CC during early development (11.5 dpc) and progressively repressed as CC developments proceeds (PubMed:27446912). {ECO:0000269|PubMed:10704386, CC ECO:0000269|PubMed:10839360, ECO:0000269|PubMed:27446912, CC ECO:0000269|PubMed:8689685, ECO:0000269|PubMed:9990854}. CC -!- PTM: Autophosphorylated; ligand binding stimulates autophosphorylation CC on tyrosine residues. {ECO:0000269|PubMed:17428795}. CC -!- PTM: Ligand binding induces cleavage by matrix metalloproteinases CC (MMPs) such as MMP7/MMP9, producing an EphB2/N-terminal fragment (NTF) CC and a C-terminal long fragment (EphB2-LF). EphB2-LF is further cleaved CC by MMPs, producing EphB2/CTF1 which is further cleaved by the CC PS1/gamma-secretase producing EphB2/CTF2. CC {ECO:0000269|PubMed:17428795}. CC -!- PTM: Polyubiquitinated; ligand binding stimulates ubiquitination CC (PubMed:17428795, PubMed:28931592). Ubiquitinated by RNF186 at Lys-891, CC mainly through 'Lys-27'-linked polyubiquitin chains (By similarity). CC {ECO:0000250|UniProtKB:P29323, ECO:0000269|PubMed:17428795, CC ECO:0000269|PubMed:28931592}. CC -!- DISRUPTION PHENOTYPE: Mice are long-lived and fertile. They display CC strain-specific circling behavior, are hyperactive and exhibit rapid CC head bobbing and twirled excessively when picked-up by the tail. This CC is probably due to abnormal vestibular function. CC {ECO:0000269|PubMed:10839360, ECO:0000269|PubMed:8689685}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE- CC ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA72411.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH62924.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; JH584273; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC043088; AAH43088.2; -; mRNA. DR EMBL; BC062924; AAH62924.1; ALT_INIT; mRNA. DR EMBL; L25890; AAA72411.1; ALT_INIT; mRNA. DR EMBL; X76011; CAA53598.1; -; mRNA. DR RefSeq; NP_001277682.1; NM_001290753.2. [P54763-4] DR RefSeq; NP_034272.1; NM_010142.4. [P54763-3] DR RefSeq; XP_006538594.1; XM_006538531.3. [P54763-2] DR PDB; 1JPA; X-ray; 1.91 A; A/B=587-898. DR PDB; 1KGY; X-ray; 2.70 A; A/B/C/D=20-199. DR PDB; 1NUK; X-ray; 2.90 A; A=20-202. DR PDB; 1SHW; X-ray; 2.20 A; B=19-199. DR PDB; 2HEN; X-ray; 2.60 A; A/B/C/D=614-898. DR PDB; 3ETP; X-ray; 2.00 A; A=20-199. DR PDB; 7S7K; X-ray; 3.15 A; A=19-543. DR PDBsum; 1JPA; -. DR PDBsum; 1KGY; -. DR PDBsum; 1NUK; -. DR PDBsum; 1SHW; -. DR PDBsum; 2HEN; -. DR PDBsum; 3ETP; -. DR PDBsum; 7S7K; -. DR AlphaFoldDB; P54763; -. DR BMRB; P54763; -. DR SMR; P54763; -. DR CORUM; P54763; -. DR DIP; DIP-34917N; -. DR IntAct; P54763; 15. DR MINT; P54763; -. DR STRING; 10090.ENSMUSP00000058135; -. DR BindingDB; P54763; -. DR ChEMBL; CHEMBL5961; -. DR GuidetoPHARMACOLOGY; 1831; -. DR GlyCosmos; P54763; 4 sites, No reported glycans. DR GlyGen; P54763; 4 sites. DR iPTMnet; P54763; -. DR PhosphoSitePlus; P54763; -. DR SwissPalm; P54763; -. DR jPOST; P54763; -. DR MaxQB; P54763; -. DR PaxDb; 10090-ENSMUSP00000101472; -. DR ProteomicsDB; 275934; -. [P54763-3] DR ProteomicsDB; 275935; -. [P54763-2] DR ProteomicsDB; 275936; -. [P54763-4] DR Pumba; P54763; -. DR Antibodypedia; 30106; 748 antibodies from 41 providers. DR DNASU; 13844; -. DR Ensembl; ENSMUST00000059287.14; ENSMUSP00000058135.8; ENSMUSG00000028664.15. [P54763-4] DR Ensembl; ENSMUST00000105845.9; ENSMUSP00000101471.3; ENSMUSG00000028664.15. [P54763-3] DR Ensembl; ENSMUST00000105846.9; ENSMUSP00000101472.3; ENSMUSG00000028664.15. [P54763-2] DR GeneID; 13844; -. DR KEGG; mmu:13844; -. DR UCSC; uc008vim.2; mouse. DR UCSC; uc008vin.2; mouse. DR AGR; MGI:99611; -. DR CTD; 2048; -. DR MGI; MGI:99611; Ephb2. DR VEuPathDB; HostDB:ENSMUSG00000028664; -. DR eggNOG; KOG0196; Eukaryota. DR GeneTree; ENSGT00940000155503; -. DR InParanoid; P54763; -. DR OMA; GAINCIC; -. DR OrthoDB; 1614410at2759; -. 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; 13844; 2 hits in 80 CRISPR screens. DR ChiTaRS; Ephb2; mouse. DR EvolutionaryTrace; P54763; -. DR PRO; PR:P54763; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; P54763; Protein. DR Bgee; ENSMUSG00000028664; Expressed in floor plate of midbrain and 254 other cell types or tissues. DR ExpressionAtlas; P54763; baseline and differential. DR GO; GO:0030424; C:axon; IDA:UniProtKB. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0030425; C:dendrite; IDA:UniProtKB. DR GO; GO:0043197; C:dendritic spine; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO. DR GO; GO:0043025; C:neuronal cell body; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0098794; C:postsynapse; ISO:MGI. DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO. DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO. DR GO; GO:0045202; C:synapse; NAS:UniProtKB. DR GO; GO:0001540; F:amyloid-beta binding; IPI:ARUK-UCL. 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; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IPI:ARUK-UCL. DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI. DR GO; GO:0005102; F:signaling receptor binding; IPI:MGI. DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IDA:UniProtKB. DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB. DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI. DR GO; GO:0007411; P:axon guidance; IDA:MGI. DR GO; GO:0007413; P:axonal fasciculation; IMP:UniProtKB. DR GO; GO:0007409; P:axonogenesis; IDA:MGI. DR GO; GO:0042113; P:B cell activation; ISO:MGI. DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI. DR GO; GO:0000902; P:cell morphogenesis; IGI:MGI. DR GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:MGI. DR GO; GO:0071679; P:commissural neuron axon guidance; IMP:UniProtKB. 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; IDA:MGI. DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0021934; P:hindbrain tangential cell migration; ISO:MGI. DR GO; GO:0042472; P:inner ear morphogenesis; IMP:UniProtKB. DR GO; GO:0007612; P:learning; IMP:MGI. DR GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL. DR GO; GO:0050771; P:negative regulation of axonogenesis; IDA:MGI. DR GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI. DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISO:MGI. DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:ARUK-UCL. DR GO; GO:1904782; P:negative regulation of NMDA glutamate receptor activity; IMP:ARUK-UCL. DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:ARUK-UCL. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:ARUK-UCL. DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IDA:ARUK-UCL. DR GO; GO:0106028; P:neuron projection retraction; IDA:ARUK-UCL. DR GO; GO:0021631; P:optic nerve morphogenesis; IMP:MGI. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB. DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI. DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI. DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:MGI. DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IMP:MGI. DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:ARUK-UCL. DR GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; IMP:ARUK-UCL. DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI. DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI. DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:UniProtKB. DR GO; GO:0031915; P:positive regulation of synaptic plasticity; IGI:ARUK-UCL. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI. DR GO; GO:0097104; P:postsynaptic membrane assembly; ISO:MGI. DR GO; GO:2000785; P:regulation of autophagosome assembly; ISO:MGI. DR GO; GO:0050770; P:regulation of axonogenesis; IDA:MGI. DR GO; GO:2000822; P:regulation of behavioral fear response; ISO:MGI. DR GO; GO:0030193; P:regulation of blood coagulation; ISS:UniProtKB. DR GO; GO:0050878; P:regulation of body fluid levels; IMP:UniProtKB. DR GO; GO:0051489; P:regulation of filopodium assembly; ISO:MGI. DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI. DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; ISO:MGI. DR GO; GO:0051963; P:regulation of synapse assembly; IDA:SynGO. DR GO; GO:2000316; P:regulation of T-helper 17 type immune response; ISO:MGI. 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:0120192; P:tight junction assembly; ISO:MGI. DR GO; GO:0099557; P:trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; IMP:SynGO. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:MGI. DR GO; GO:0001655; P:urogenital system development; IMP:UniProtKB. DR GO; GO:0110077; P:vesicle-mediated intercellular transport; ISO:MGI. DR CDD; cd10477; EphR_LBD_B2; 1. DR CDD; cd00063; FN3; 2. DR CDD; cd05065; PTKc_EphR_B; 1. DR CDD; cd09552; SAM_EPH-B2; 1. DR CDD; cd00185; TNFRSF; 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; IPR034238; EphB2_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:SF11; EPHRIN TYPE-B RECEPTOR 2; 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; SSF57184; Growth factor receptor domain; 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. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; KW Cell projection; Developmental protein; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Isopeptide bond; 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..18 FT /evidence="ECO:0000255" FT CHAIN 19..986 FT /note="Ephrin type-B receptor 2" FT /evidence="ECO:0000255" FT /id="PRO_0000016828" FT CHAIN 536..986 FT /note="EphB2/CTF1" FT /evidence="ECO:0000269|PubMed:17428795" FT /id="PRO_0000445963" FT CHAIN 562..986 FT /note="EphB2/CTF2" FT /evidence="ECO:0000269|PubMed:17428795" FT /id="PRO_0000445964" FT TOPO_DOM 19..543 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 544..564 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 565..986 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 20..202 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..884 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 913..977 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT MOTIF 984..986 FT /note="PDZ-binding" FT ACT_SITE 746 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 627..635 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 SITE 535..536 FT /note="Cleavage; by a metalloproteinase" FT /evidence="ECO:0000269|PubMed:17428795" FT SITE 561..562 FT /note="Cleavage; by gamma-secretase/PS1" FT /evidence="ECO:0000269|PubMed:17428795" FT CARBOHYD 265 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 336 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 428 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 482 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19656770" FT DISULFID 62..184 FT /evidence="ECO:0000269|PubMed:11780069" FT DISULFID 97..107 FT /evidence="ECO:0000269|PubMed:11780069" FT CROSSLNK 891 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P29323" FT VAR_SEQ 476 FT /note="K -> KQ (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_057932" FT VAR_SEQ 566 FT /note="N -> NR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7947319" FT /id="VSP_057933" FT MUTAGEN 596 FT /note="Y->F: No loss of interaction with SPSB4; when FT associated with F-602." FT /evidence="ECO:0000269|PubMed:28931592" FT MUTAGEN 602 FT /note="Y->F: No loss of interaction with SPSB4; when FT associated with F-596." FT /evidence="ECO:0000269|PubMed:28931592" FT STRAND 20..25 FT /evidence="ECO:0007829|PDB:3ETP" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 36..39 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 55..61 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 71..74 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 84..94 FT /evidence="ECO:0007829|PDB:3ETP" FT HELIX 97..99 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:1SHW" FT STRAND 110..121 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 125..128 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 135..142 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 147..152 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 155..166 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 171..182 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 185..195 FT /evidence="ECO:0007829|PDB:3ETP" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 228..241 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 251..256 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 260..263 FT /evidence="ECO:0007829|PDB:7S7K" FT TURN 264..267 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 268..271 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 296..302 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 329..336 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 339..345 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 357..365 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 381..383 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 385..395 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 403..411 FT /evidence="ECO:0007829|PDB:7S7K" FT HELIX 415..417 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 424..430 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 442..447 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 452..456 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 466..478 FT /evidence="ECO:0007829|PDB:7S7K" FT HELIX 480..482 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 484..495 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 503..512 FT /evidence="ECO:0007829|PDB:7S7K" FT STRAND 523..526 FT /evidence="ECO:0007829|PDB:7S7K" FT HELIX 530..540 FT /evidence="ECO:0007829|PDB:7S7K" FT HELIX 599..601 FT /evidence="ECO:0007829|PDB:1JPA" FT STRAND 602..604 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 605..612 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 618..620 FT /evidence="ECO:0007829|PDB:1JPA" FT STRAND 621..629 FT /evidence="ECO:0007829|PDB:1JPA" FT STRAND 631..640 FT /evidence="ECO:0007829|PDB:1JPA" FT STRAND 643..645 FT /evidence="ECO:0007829|PDB:2HEN" FT STRAND 648..654 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 661..674 FT /evidence="ECO:0007829|PDB:1JPA" FT STRAND 685..689 FT /evidence="ECO:0007829|PDB:1JPA" FT STRAND 691..694 FT /evidence="ECO:0007829|PDB:1JPA" FT STRAND 696..700 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 707..712 FT /evidence="ECO:0007829|PDB:1JPA" FT TURN 713..716 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 720..739 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 749..751 FT /evidence="ECO:0007829|PDB:1JPA" FT STRAND 752..754 FT /evidence="ECO:0007829|PDB:1JPA" FT STRAND 760..762 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 790..792 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 795..799 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 805..820 FT /evidence="ECO:0007829|PDB:1JPA" FT TURN 821..823 FT /evidence="ECO:0007829|PDB:2HEN" FT TURN 826..829 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 832..840 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 853..862 FT /evidence="ECO:0007829|PDB:1JPA" FT TURN 867..869 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 873..885 FT /evidence="ECO:0007829|PDB:1JPA" FT HELIX 887..890 FT /evidence="ECO:0007829|PDB:1JPA" SQ SEQUENCE 986 AA; 109899 MW; 92DB5234F18758A7 CRC64; MAVRRLGAAL LLLPLLAAVE ETLMDSTTAT AELGWMVHPP SGWEEVSGYD ENMNTIRTYQ VCNVFESSQN NWLRTKFIRR RGAHRIHVEM KFSVRDCSSI PSVPGSCKET FNLYYYEADF DLATKTFPNW MENPWVKVDT IAADESFSQV DLGGRVMKIN TEVRSFGPVS RNGFYLAFQD YGGCMSLIAV RVFYRKCPRI IQNGAIFQET LSGAESTSLV AARGSCIANA EEVDVPIKLY CNGDGEWLVP IGRCMCKAGF EAVENGTVCR GCPSGTFKAN QGDEACTHCP INSRTTSEGA TNCVCRNGYY RADLDPLDMP CTTIPSAPQA VISSVNETSL MLEWTPPRDS GGREDLVYNI ICKSCGSGRG ACTRCGDNVQ YAPRQLGLTE PRIYISDLLA HTQYTFEIQA VNGVTDQSPF SPQFASVNIT TNQAAPSAVS IMHQVSRTVD SITLSWSQPD QPNGVILDYE LQYYEKELSE YNATAIKSPT NTVTVQGLKA GAIYVFQVRA RTVAGYGRYS GKMYFQTMTE AEYQTSIKEK LPLIVGSSAA GLVFLIAVVV IAIVCNRRGF ERADSEYTDK LQHYTSGHMT PGMKIYIDPF TYEDPNEAVR EFAKEIDISC VKIEQVIGAG EFGEVCSGHL KLPGKREIFV AIKTLKSGYT EKQRRDFLSE ASIMGQFDHP NVIHLEGVVT KSTPVMIITE FMENGSLDSF LRQNDGQFTV IQLVGMLRGI AAGMKYLADM NYVHRDLAAR NILVNSNLVC KVSDFGLSRF LEDDTSDPTY TSALGGKIPI RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM TNQDVINAIE QDYRLPPPMD CPSALHQLML DCWQKDRNHR PKFGQIVNTL DKMIRNPNSL KAMAPLSSGI NLPLLDRTIP DYTSFNTVDE WLEAIKMGQY KESFANAGFT SFDVVSQMMM EDILRVGVTL AGHQKKILNS IQVMRAQMNQ IQSVEV //