ID EPHB4_HUMAN Reviewed; 987 AA.
AC P54760; Q9BTA5; Q9BXP0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 29-MAY-2013, entry version 150.
DE RecName: Full=Ephrin type-B receptor 4;
DE EC=2.7.10.1;
DE AltName: Full=Hepatoma transmembrane kinase;
DE AltName: Full=Tyrosine-protein kinase TYRO11;
DE Flags: Precursor;
GN Name=EPHB4; Synonyms=HTK, MYK1, TYRO11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=8188704;
RA Bennett B.D., Wang Z., Kuang W.J., Wang A., Groopman J.E.,
RA Goeddel D.V., Scadden D.T.;
RT "Cloning and characterization of HTK, a novel transmembrane tyrosine
RT kinase of the EPH subfamily.";
RL J. Biol. Chem. 269:14211-14218(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C.,
RA Miller W., Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 143-987.
RC TISSUE=Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NOMENCLATURE.
RX PubMed=9267020;
RG Eph nomenclature committee;
RT "Unified nomenclature for Eph family receptors and their ligands, the
RT ephrins.";
RL Cell 90:403-404(1997).
RN [5]
RP FUNCTION IN ANGIOGENESIS, FUNCTION IN CELL ADHESION, AND FUNCTION IN
RP CELL MIGRATION.
RX PubMed=12734395; DOI=10.1242/jcs.00426;
RA Fueller T., Korff T., Kilian A., Dandekar G., Augustin H.G.;
RT "Forward EphB4 signaling in endothelial cells controls cellular
RT repulsion and segregation from ephrinB2 positive cells.";
RL J. Cell Sci. 116:2461-2470(2003).
RN [6]
RP FUNCTION IN POSTNATAL AND TUMOR ANGIOGENESIS.
RX PubMed=16424904; DOI=10.1038/sj.emboj.7600949;
RA Erber R., Eichelsbacher U., Powajbo V., Korn T., Djonov V., Lin J.,
RA Hammes H.P., Grobholz R., Ullrich A., Vajkoczy P.;
RT "EphB4 controls blood vascular morphogenesis during postnatal
RT angiogenesis.";
RL EMBO J. 25:628-641(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911 AND THR-976, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-976, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911; THR-976 AND
RP TYR-987, AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 17-196 IN COMPLEX WITH
RP EFNB2, MUTAGENESIS OF LEU-95, AND DISULFIDE BOND.
RX PubMed=16867992; DOI=10.1074/jbc.M605766200;
RA Chrencik J.E., Brooun A., Kraus M.L., Recht M.I., Kolatkar A.R.,
RA Han G.W., Seifert J.M., Widmer H., Auer M., Kuhn P.;
RT "Structural and biophysical characterization of the EphB4*ephrinB2
RT protein-protein interaction and receptor specificity.";
RL J. Biol. Chem. 281:28185-28192(2006).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 17-196 IN COMPLEX WITH
RP ANTAGONISTIC PEPTIDE, AND DISULFIDE BOND.
RX PubMed=16472751; DOI=10.1016/j.str.2005.11.011;
RA Chrencik J.E., Brooun A., Recht M.I., Kraus M.L., Koolpe M.,
RA Kolatkar A.R., Bruce R.H., Martiny-Baron G., Widmer H., Pasquale E.B.,
RA Kuhn P.;
RT "Structure and thermodynamic characterization of the EphB4/Ephrin-B2
RT antagonist peptide complex reveals the determinants for receptor
RT specificity.";
RL Structure 14:321-330(2006).
RN [13]
RP STRUCTURE BY NMR OF 434-529.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second FN3 domain from human ephrin type-B
RT receptor 4.";
RL Submitted (JUL-2007) to the PDB data bank.
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-67; ILE-113; LEU-346; VAL-371;
RP GLU-576; HIS-678; THR-882; TRP-889 AND ASP-890.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
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
CC neighboring cells. The signaling pathway downstream of the
CC receptor is referred to as forward signaling while the signaling
CC pathway downstream of the ephrin ligand is referred to as reverse
CC signaling. Together with its cognate ligand/functional ligand
CC EFNB2 plays a central role in heart morphogenesis and angiogenesis
CC through regulation of cell adhesion and cell migration. EPHB4-
CC mediated forward signaling controls cellular repulsion and
CC segregation form EFNB2-expressing cells. Plays also a role in
CC postnatal blood vessel remodeling, morphogenesis and permeability
CC and is thus important in the context of tumor angiogenesis.
CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC [protein]-L-tyrosine phosphate.
CC -!- SUBUNIT: Heterotetramer upon binding of the ligand. The
CC heterotetramer is composed of an ephrin dimer and a receptor
CC dimer. Oligomerization is probably required to induce biological
CC responses (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in placenta but also
CC detected in kidney, liver, lung, pancreas, skeletal muscle and
CC heart. Expressed in primitive and myeloid, but not lymphoid,
CC hematopoietic cells. Also observed in cell lines derived from
CC liver, breast, colon, lung, melanocyte and cervix.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal heart, lung, liver and to
CC a lower extent in brain. Not expressed in adult brain.
CC -!- PTM: Phosphorylated; autophosphorylation is stimulated by EFNB2.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily.
CC -!- SIMILARITY: Contains 1 Eph LBD (Eph ligand-binding) domain.
CC -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
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DR EMBL; U07695; AAA20598.1; -; mRNA.
DR EMBL; AF312032; AAK21010.1; -; Genomic_DNA.
DR EMBL; BC004264; AAH04264.1; -; mRNA.
DR IPI; IPI00289342; -.
DR PIR; A54092; A54092.
DR RefSeq; NP_004435.3; NM_004444.4.
DR UniGene; Hs.437008; -.
DR PDB; 2BBA; X-ray; 1.65 A; A=17-196.
DR PDB; 2E7H; NMR; -; A=434-529.
DR PDB; 2HLE; X-ray; 2.05 A; A=17-196.
DR PDB; 2QKQ; X-ray; 2.10 A; A/B=896-977.
DR PDB; 2VWU; X-ray; 2.00 A; A=598-887.
DR PDB; 2VWV; X-ray; 1.90 A; A=598-899.
DR PDB; 2VWW; X-ray; 1.90 A; A=598-899.
DR PDB; 2VWX; X-ray; 1.65 A; A=598-899.
DR PDB; 2VWY; X-ray; 1.65 A; A=598-899.
DR PDB; 2VWZ; X-ray; 1.65 A; A=598-899.
DR PDB; 2VX0; X-ray; 2.10 A; A=598-899.
DR PDB; 2VX1; X-ray; 1.65 A; A=598-899.
DR PDB; 2X9F; X-ray; 1.75 A; A=598-899.
DR PDB; 2XVD; X-ray; 1.70 A; A=598-899.
DR PDB; 4AW5; X-ray; 2.33 A; A=605-890.
DR PDB; 4BB4; X-ray; 1.65 A; A=598-899.
DR PDBsum; 2BBA; -.
DR PDBsum; 2E7H; -.
DR PDBsum; 2HLE; -.
DR PDBsum; 2QKQ; -.
DR PDBsum; 2VWU; -.
DR PDBsum; 2VWV; -.
DR PDBsum; 2VWW; -.
DR PDBsum; 2VWX; -.
DR PDBsum; 2VWY; -.
DR PDBsum; 2VWZ; -.
DR PDBsum; 2VX0; -.
DR PDBsum; 2VX1; -.
DR PDBsum; 2X9F; -.
DR PDBsum; 2XVD; -.
DR PDBsum; 4AW5; -.
DR PDBsum; 4BB4; -.
DR ProteinModelPortal; P54760; -.
DR IntAct; P54760; 2.
DR STRING; 9606.ENSP00000350896; -.
DR PhosphoSite; P54760; -.
DR DMDM; 19860819; -.
DR DOSAC-COBS-2DPAGE; P54760; -.
DR PaxDb; P54760; -.
DR PRIDE; P54760; -.
DR DNASU; 2050; -.
DR Ensembl; ENST00000358173; ENSP00000350896; ENSG00000196411.
DR GeneID; 2050; -.
DR KEGG; hsa:2050; -.
DR UCSC; uc003uwm.1; human.
DR CTD; 2050; -.
DR GeneCards; GC07M100402; -.
DR H-InvDB; HIX0025312; -.
DR HGNC; HGNC:3395; EPHB4.
DR HPA; CAB013537; -.
DR MIM; 600011; gene.
DR neXtProt; NX_P54760; -.
DR PharmGKB; PA27827; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000233856; -.
DR HOVERGEN; HBG062180; -.
DR InParanoid; P54760; -.
DR KO; K05113; -.
DR OMA; CVADAVP; -.
DR OrthoDB; EOG408N7B; -.
DR PhylomeDB; P54760; -.
DR BRENDA; 2.7.10.1; 2681.
DR Pathway_Interaction_DB; ephbfwdpathway; EPHB forward signaling.
DR Pathway_Interaction_DB; ephrinbrevpathway; Ephrin B reverse signaling.
DR Pathway_Interaction_DB; ephrinb_ephbpathway; EphrinB-EPHB pathway.
DR SignaLink; P54760; -.
DR BindingDB; P54760; -.
DR ChEMBL; CHEMBL5147; -.
DR ChiTaRS; EPHB4; human.
DR EvolutionaryTrace; P54760; -.
DR GenomeRNAi; 2050; -.
DR NextBio; 8335; -.
DR ArrayExpress; P54760; -.
DR Bgee; P54760; -.
DR CleanEx; HS_EPHB4; -.
DR Genevestigator; P54760; -.
DR GermOnline; ENSG00000196411; Homo sapiens.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005003; F:ephrin receptor activity; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IDA:UniProtKB.
DR GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.120.260; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR008979; Galactose-bd-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_cat_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed.
DR InterPro; IPR021129; SAM_type1.
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; PF01404; Ephrin_lbd; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07699; GCC2_GCC3; 1.
DR Pfam; PF07714; Pkinase_Tyr; 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; SSF49265; FN_III-like; 2.
DR SUPFAM; SSF49785; Gal_bind_like; 1.
DR SUPFAM; SSF56112; Kinase_like; 1.
DR SUPFAM; SSF47769; SAM_homology; 1.
DR PROSITE; PS01186; EGF_2; UNKNOWN_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; Angiogenesis; ATP-binding; Cell membrane;
KW Complete proteome; Developmental protein; Disulfide bond;
KW Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Receptor; Reference proteome; Repeat; Signal;
KW Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1 15 Potential.
FT CHAIN 16 987 Ephrin type-B receptor 4.
FT /FTId=PRO_0000016834.
FT TOPO_DOM 16 539 Extracellular (Potential).
FT TRANSMEM 540 560 Helical; (Potential).
FT TOPO_DOM 561 987 Cytoplasmic (Potential).
FT DOMAIN 17 202 Eph LBD.
FT DOMAIN 323 428 Fibronectin type-III 1.
FT DOMAIN 434 526 Fibronectin type-III 2.
FT DOMAIN 615 899 Protein kinase.
FT DOMAIN 907 971 SAM.
FT NP_BIND 621 629 ATP (By similarity).
FT MOTIF 985 987 PDZ-binding (Potential).
FT COMPBIAS 184 320 Cys-rich.
FT ACT_SITE 740 740 Proton acceptor (By similarity).
FT BINDING 647 647 ATP (By similarity).
FT MOD_RES 911 911 Phosphoserine.
FT MOD_RES 976 976 Phosphothreonine.
FT MOD_RES 987 987 Phosphotyrosine.
FT CARBOHYD 203 203 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 335 335 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 426 426 N-linked (GlcNAc...) (Potential).
FT DISULFID 61 184
FT DISULFID 97 107
FT VARIANT 67 67 P -> L (in dbSNP:rs34653459).
FT /FTId=VAR_042181.
FT VARIANT 113 113 V -> I (in dbSNP:rs55866373).
FT /FTId=VAR_042182.
FT VARIANT 346 346 P -> L (in a metastatic melanoma sample;
FT somatic mutation).
FT /FTId=VAR_042183.
FT VARIANT 371 371 A -> V (in dbSNP:rs55720981).
FT /FTId=VAR_042184.
FT VARIANT 576 576 D -> E (in dbSNP:rs36050247).
FT /FTId=VAR_042185.
FT VARIANT 678 678 R -> H (in dbSNP:rs55692440).
FT /FTId=VAR_042186.
FT VARIANT 882 882 A -> T (in dbSNP:rs34918225).
FT /FTId=VAR_042187.
FT VARIANT 889 889 R -> W (in a gastric adenocarcinoma
FT sample; somatic mutation).
FT /FTId=VAR_042188.
FT VARIANT 890 890 E -> D (in dbSNP:rs35638378).
FT /FTId=VAR_042189.
FT MUTAGEN 95 95 L->R: Reduces binding affinity for EFNB2.
FT CONFLICT 62 62 D -> E (in Ref. 1; AAA20598).
FT CONFLICT 308 308 Y -> D (in Ref. 1; AAA20598).
FT CONFLICT 464 464 V -> W (in Ref. 1; AAA20598).
FT CONFLICT 926 927 ES -> AR (in Ref. 1; AAA20598).
FT STRAND 17 22
FT HELIX 23 25
FT STRAND 33 36
FT STRAND 43 48
FT STRAND 54 61
FT STRAND 63 65
FT STRAND 70 74
FT STRAND 84 95
FT HELIX 97 99
FT STRAND 109 121
FT STRAND 130 132
FT STRAND 135 142
FT STRAND 147 150
FT TURN 151 153
FT STRAND 154 156
FT STRAND 160 166
FT STRAND 171 182
FT STRAND 184 196
FT STRAND 441 446
FT STRAND 449 453
FT STRAND 460 462
FT STRAND 466 473
FT TURN 479 481
FT STRAND 482 496
FT STRAND 503 510
FT HELIX 612 614
FT STRAND 615 623
FT STRAND 625 634
FT STRAND 637 639
FT STRAND 642 649
FT HELIX 655 668
FT STRAND 679 683
FT STRAND 685 694
FT HELIX 701 707
FT TURN 708 710
FT HELIX 714 733
FT HELIX 743 745
FT STRAND 746 748
FT STRAND 754 756
FT HELIX 765 767
FT HELIX 784 786
FT HELIX 789 794
FT HELIX 799 814
FT TURN 815 817
FT TURN 820 823
FT HELIX 826 834
FT HELIX 847 856
FT HELIX 861 863
FT HELIX 867 879
FT HELIX 881 885
FT HELIX 912 918
FT HELIX 922 924
FT HELIX 925 930
FT HELIX 936 939
FT HELIX 944 950
FT HELIX 955 965
SQ SEQUENCE 987 AA; 108270 MW; 11A004622F194706 CRC64;
MELRVLLCWA SLAAALEETL LNTKLETADL KWVTFPQVDG QWEELSGLDE EQHSVRTYEV
CDVQRAPGQA HWLRTGWVPR RGAVHVYATL RFTMLECLSL PRAGRSCKET FTVFYYESDA
DTATALTPAW MENPYIKVDT VAAEHLTRKR PGAEATGKVN VKTLRLGPLS KAGFYLAFQD
QGACMALLSL HLFYKKCAQL TVNLTRFPET VPRELVVPVA GSCVVDAVPA PGPSPSLYCR
EDGQWAEQPV TGCSCAPGFE AAEGNTKCRA CAQGTFKPLS GEGSCQPCPA NSHSNTIGSA
VCQCRVGYFR ARTDPRGAPC TTPPSAPRSV VSRLNGSSLH LEWSAPLESG GREDLTYALR
CRECRPGGSC APCGGDLTFD PGPRDLVEPW VVVRGLRPDF TYTFEVTALN GVSSLATGPV
PFEPVNVTTD REVPPAVSDI RVTRSSPSSL SLAWAVPRAP SGAVLDYEVK YHEKGAEGPS
SVRFLKTSEN RAELRGLKRG ASYLVQVRAR SEAGYGPFGQ EHHSQTQLDE SEGWREQLAL
IAGTAVVGVV LVLVVIVVAV LCLRKQSNGR EAEYSDKHGQ YLIGHGTKVY IDPFTYEDPN
EAVREFAKEI DVSYVKIEEV IGAGEFGEVC RGRLKAPGKK ESCVAIKTLK GGYTERQRRE
FLSEASIMGQ FEHPNIIRLE GVVTNSMPVM ILTEFMENGA LDSFLRLNDG QFTVIQLVGM
LRGIASGMRY LAEMSYVHRD LAARNILVNS NLVCKVSDFG LSRFLEENSS DPTYTSSLGG
KIPIRWTAPE AIAFRKFTSA SDAWSYGIVM WEVMSFGERP YWDMSNQDVI NAIEQDYRLP
PPPDCPTSLH QLMLDCWQKD RNARPRFPQV VSALDKMIRN PASLKIVARE NGGASHPLLD
QRQPHYSAFG SVGEWLRAIK MGRYEESFAA AGFGSFELVS QISAEDLLRI GVTLAGHQKK
ILASVQHMKS QAKPGTPGGT GGPAPQY
//
