EPHB4_MOUSE
ID EPHB4_MOUSE Reviewed; 987 AA.
AC P54761; Q60627; Q99MR2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Ephrin type-B receptor 4;
DE EC=2.7.10.1;
DE AltName: Full=Developmental kinase 2;
DE Short=mDK-2;
DE AltName: Full=Hepatoma transmembrane kinase;
DE AltName: Full=Tyrosine kinase MYK-1;
DE Flags: Precursor;
GN Name=Ephb4; Synonyms=Htk, Mdk2, Myk1;
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], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Kidney;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Lung;
RX PubMed=8152808;
RA Andres A.-C., Reid H.H., Zurcher G., Blaschke R.J., Albrecht D.,
RA Ziemiecki A.;
RT "Expression of two novel eph-related receptor protein tyrosine kinases in
RT mammary gland development and carcinogenesis.";
RL Oncogene 9:1461-1467(1994).
RN [3]
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., Miller W.,
RA 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION IN ANGIOGENESIS, AND DEVELOPMENTAL STAGE.
RX PubMed=10518221; DOI=10.1016/s1097-2765(00)80342-1;
RA Gerety S.S., Wang H.U., Chen Z.F., Anderson D.J.;
RT "Symmetrical mutant phenotypes of the receptor EphB4 and its specific
RT transmembrane ligand ephrin-B2 in cardiovascular development.";
RL Mol. Cell 4:403-414(1999).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-335.
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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-335.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, and Lung;
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 [9]
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 [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=27400125; DOI=10.1172/jci85794;
RA Martin-Almedina S., Martinez-Corral I., Holdhus R., Vicente A., Fotiou E.,
RA Lin S., Petersen K., Simpson M.A., Hoischen A., Gilissen C., Jeffery H.,
RA Atton G., Karapouliou C., Brice G., Gordon K., Wiseman J.W., Wedin M.,
RA Rockson S.G., Jeffery S., Mortimer P.S., Snyder M.P., Berland S.,
RA Mansour S., Makinen T., Ostergaard P.;
RT "EPHB4 kinase-inactivating mutations cause autosomal dominant lymphatic-
RT related hydrops fetalis.";
RL J. Clin. Invest. 126:3080-3088(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. Together with its
CC cognate ligand/functional ligand EFNB2 it is involved in the regulation
CC of cell adhesion and migration, and plays a central role in heart
CC morphogenesis, angiogenesis and blood vessel remodeling and
CC permeability. EPHB4-mediated forward signaling controls cellular
CC repulsion and segregation from EFNB2-expressing cells.
CC {ECO:0000269|PubMed:10518221}.
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 Interacts with RASA1; the interaction depends on EPHB4 tyrosine-
CC phosphorylation (By similarity). {ECO:0000250|UniProtKB:P54760}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54760};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P54760}.
CC -!- TISSUE SPECIFICITY: Expressed in various organ systems, including lung,
CC liver, kidney, intestine, muscle and heart (PubMed:7478528). Expressed
CC in myogenic progenitor cells (PubMed:27446912).
CC {ECO:0000269|PubMed:27446912, ECO:0000269|PubMed:7478528}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in the developing
CC cardiovascular system with higher expression in veins. First detected
CC in the developing anterior cardinal vein at 8.75 dpc. Abundant
CC expression at 16.5 dpc in various organ systems, including thymus,
CC heart, lung and kidney, where it is associated with cells of
CC endothelial origin. 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:10518221,
CC ECO:0000269|PubMed:27446912}.
CC -!- PTM: Phosphorylated; autophosphorylation is stimulated by EFNB2.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryo display cardiovascular defects and
CC lethality with very high penetrance. Growth retardation is observed at
CC 9.5 dpc with arrested heart development and lack of blood flow. By 10.5
CC dpc degeneration and necrosis are apparent throughout the embryo.
CC Conditional lymphovenous valves knockouts show a complete loss of
CC lymphatic valves (PubMed:27400125). {ECO:0000269|PubMed:10518221,
CC ECO:0000269|PubMed:27400125}.
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; Z49085; CAA88909.1; -; mRNA.
DR EMBL; U06834; AAA18591.1; -; mRNA.
DR EMBL; AF312033; AAK28823.1; -; Genomic_DNA.
DR EMBL; CH466529; EDL19273.1; -; Genomic_DNA.
DR EMBL; CH466529; EDL19275.1; -; Genomic_DNA.
DR CCDS; CCDS19767.1; -.
DR PIR; I48652; I48652.
DR PIR; I48953; I48953.
DR RefSeq; NP_034274.4; NM_010144.6.
DR AlphaFoldDB; P54761; -.
DR SMR; P54761; -.
DR BioGRID; 199478; 7.
DR STRING; 10090.ENSMUSP00000106684; -.
DR BindingDB; P54761; -.
DR ChEMBL; CHEMBL4739680; -.
DR GuidetoPHARMACOLOGY; 1833; -.
DR GlyGen; P54761; 3 sites.
DR iPTMnet; P54761; -.
DR PhosphoSitePlus; P54761; -.
DR SwissPalm; P54761; -.
DR MaxQB; P54761; -.
DR PaxDb; P54761; -.
DR PRIDE; P54761; -.
DR ProteomicsDB; 275531; -.
DR ABCD; P54761; 28 sequenced antibodies.
DR Antibodypedia; 4623; 701 antibodies from 41 providers.
DR DNASU; 13846; -.
DR Ensembl; ENSMUST00000061244; ENSMUSP00000051622; ENSMUSG00000029710.
DR Ensembl; ENSMUST00000144296; ENSMUSP00000115731; ENSMUSG00000029710.
DR Ensembl; ENSMUST00000166239; ENSMUSP00000130275; ENSMUSG00000029710.
DR GeneID; 13846; -.
DR KEGG; mmu:13846; -.
DR UCSC; uc009aci.2; mouse.
DR CTD; 2050; -.
DR MGI; MGI:104757; Ephb4.
DR VEuPathDB; HostDB:ENSMUSG00000029710; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000160057; -.
DR InParanoid; P54761; -.
DR OMA; TAHWLRT; -.
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; 13846; 1 hit in 78 CRISPR screens.
DR ChiTaRS; Ephb4; mouse.
DR PRO; PR:P54761; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P54761; protein.
DR Bgee; ENSMUSG00000029710; Expressed in embryonic post-anal tail and 207 other tissues.
DR ExpressionAtlas; P54761; baseline and differential.
DR Genevisible; P54761; MM.
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:0005003; F:ephrin receptor activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IGI:UniProtKB.
DR GO; GO:0003007; P:heart morphogenesis; IMP:UniProtKB.
DR GO; GO:1903849; P:positive regulation of aorta morphogenesis; IMP:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:2000525; P:positive regulation of T cell costimulation; IGI:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0048845; P:venous blood vessel morphogenesis; IMP:MGI.
DR CDD; cd10474; EphR_LBD_B4; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd09554; SAM_EPH-B4; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR037636; EPH-B4_SAM.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034290; EphB4_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; PS01186; EGF_2; 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; Developmental protein;
KW Disulfide bond; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..987
FT /note="Ephrin type-B receptor 4"
FT /id="PRO_0000016835"
FT TOPO_DOM 16..539
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..987
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 17..202
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 323..432
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 436..529
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 615..899
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 907..971
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 965..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 985..987
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 740
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 621..629
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54760"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54760"
FT MOD_RES 911
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54760"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54760"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..184
FT /evidence="ECO:0000250"
FT DISULFID 97..107
FT /evidence="ECO:0000250"
FT CONFLICT 120
FT /note="A -> R (in Ref. 1; CAA88909 and 2; AAA18591)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..353
FT /note="GRE -> RPR (in Ref. 2; AAA18591)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="P -> R (in Ref. 2; AAA18591)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="R -> A (in Ref. 2; AAA18591)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="P -> S (in Ref. 1; CAA88909)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="S -> R (in Ref. 2; AAA18591)"
FT /evidence="ECO:0000305"
FT CONFLICT 913
FT /note="G -> V (in Ref. 2; AAA18591)"
FT /evidence="ECO:0000305"
FT CONFLICT 938
FT /note="V -> M (in Ref. 2; AAA18591)"
FT /evidence="ECO:0000305"
FT CONFLICT 970..971
FT /note="SQ -> WE (in Ref. 2; AAA18591)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 987 AA; 108848 MW; E4FC5B2210723974 CRC64;
MELRALLCWA SLATALEETL LNTKLETADL KWVTYPQAEG QWEELSGLDE EQHSVRTYEV
CDMKRPGGQA HWLRTGWVPR RGAVHVYATI RFTMMECLSL PRASRSCKET FTVFYYESEA
DTATAHTPAW MENPYIKVDT VAAEHLTRKR PGAEATGKVN IKTLRLGPLS KAGFYLAFQD
QGACMALLSL HLFYKKCSWL ITNLTYFPET VPRELVVPVA GSCVANAVPT ANPSPSLYCR
EDGQWAEQQV TGCSCAPGYE AAESNKVCRA CGQGTFKPQI GDESCLPCPA NSHSNNIGSP
VCLCRIGYYR ARSDPRSSPC TTPPSAPRSV VHHLNGSTLR LEWSAPLESG GREDLTYAVR
CRECRPGGSC LPCGGDMTFD PGPRDLVEPW VAIRGLRPDV TYTFEVAALN GVSTLATGPP
PFEPVNVTTD REVPPAVSDI RVTRSSPSSL ILSWAIPRAP SGAVLDYEVK YHEKGAEGPS
SVRFLKTSEN RAELRGLKRG ASYLVQVRAR SEAGYGPFGQ EHHSQTQLDE SESWREQLAL
IAGTAVVGVV LVLVVVIIAV LCLRKQSNGR EVEYSDKHGQ YLIGHGTKVY IDPFTYEDPN
EAVREFAKEI DVSYVKIEEV IGAGEFGEVC RGRLKAPGKK ESCVAIKTLK GGYTERQRRE
FLSEASIMGQ FEHPNIIRLE GVVTNSVPVM ILTEFMENGA LDSFLRLNDG QFTVIQLVGM
LRGIASGMRY LAEMSYVHRD LAARNILVNS NLVCKVSDFG LSRFLEENSS DPTYTSSLGG
KIPIRWTAPE AIAFRKFTSA SDAWSYGIVM WEVMSFGERP YWDMSNQDVI NAIEQDYRLP
PPPDCPTSLH QLMLDCWQKD RNARPRFPQV VSALDKMIRN PASLKIVARE NGGASHPLLD
QRQPHYSAFG SVGEWLRAIK MGRYEESFAA AGFGSFEVVS QISAEDLLRI GVTLAGHQKK
ILASVQHMKS QAKPGAPGGT GGPAQQF
