EPHB2_MOUSE
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 03-AUG-2022, entry version 217.
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},
GN Sek3 {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};
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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.ENSMUSP00000101472; -.
DR BindingDB; P54763; -.
DR ChEMBL; CHEMBL5961; -.
DR GuidetoPHARMACOLOGY; 1831; -.
DR GlyGen; P54763; 4 sites.
DR iPTMnet; P54763; -.
DR PhosphoSitePlus; P54763; -.
DR SwissPalm; P54763; -.
DR jPOST; P54763; -.
DR MaxQB; P54763; -.
DR PaxDb; P54763; -.
DR PRIDE; P54763; -.
DR ProteomicsDB; 275934; -. [P54763-3]
DR ProteomicsDB; 275935; -. [P54763-2]
DR ProteomicsDB; 275936; -. [P54763-4]
DR Antibodypedia; 30106; 673 antibodies from 41 providers.
DR DNASU; 13844; -.
DR Ensembl; ENSMUST00000059287; ENSMUSP00000058135; ENSMUSG00000028664. [P54763-4]
DR Ensembl; ENSMUST00000105845; ENSMUSP00000101471; ENSMUSG00000028664. [P54763-3]
DR Ensembl; ENSMUST00000105846; ENSMUSP00000101472; ENSMUSG00000028664. [P54763-2]
DR GeneID; 13844; -.
DR KEGG; mmu:13844; -.
DR UCSC; uc008vim.2; mouse.
DR UCSC; uc008vin.2; mouse.
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; 933071at2759; -.
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; 1 hit in 75 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 252 other 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:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
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; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
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:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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: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:0006468; P:protein phosphorylation; IDA: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 Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
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 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 SUPFAM; SSF57184; SSF57184; 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
