MERTK_MOUSE
ID MERTK_MOUSE Reviewed; 994 AA.
AC Q60805; Q62194;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Tyrosine-protein kinase Mer;
DE EC=2.7.10.1;
DE AltName: Full=Proto-oncogene c-Mer;
DE AltName: Full=Receptor tyrosine kinase MerTK;
DE Flags: Precursor;
GN Name=Mertk; Synonyms=Mer;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=7784083;
RA Graham D.K., Bowman G.W., Dawson T.L., Stanford W.L., Earp H.S.,
RA Snodgrass H.R.;
RT "Cloning and developmental expression analysis of the murine c-mer tyrosine
RT kinase.";
RL Oncogene 10:2349-2359(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 472-994.
RC STRAIN=CD-1; TISSUE=Testis;
RA Dowds C.A., Burks D.J., Saling P.M.;
RT "A cDNA encoding part of a novel putative receptor tyrosine kinase.";
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=10227296; DOI=10.1038/19554;
RA Lu Q., Gore M., Zhang Q., Camenisch T., Boast S., Casagranda F., Lai C.,
RA Skinner M.K., Klein R., Matsushima G.K., Earp H.S., Goff S.P., Lemke G.;
RT "Tyro-3 family receptors are essential regulators of mammalian
RT spermatogenesis.";
RL Nature 398:723-728(1999).
RN [4]
RP INTERACTION WITH GRB2, AND MUTAGENESIS OF TYR-867.
RX PubMed=9891051; DOI=10.1128/mcb.19.2.1171;
RA Georgescu M.M., Kirsch K.H., Shishido T., Zong C., Hanafusa H.;
RT "Biological effects of c-Mer receptor tyrosine kinase in hematopoietic
RT cells depend on the Grb2 binding site in the receptor and activation of NF-
RT kappaB.";
RL Mol. Cell. Biol. 19:1171-1181(1999).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12884290; DOI=10.1002/eji.200324076;
RA Behrens E.M., Gadue P., Gong S.Y., Garrett S., Stein P.L., Cohen P.L.;
RT "The mer receptor tyrosine kinase: expression and function suggest a role
RT in innate immunity.";
RL Eur. J. Immunol. 33:2160-2167(2003).
RN [6]
RP INTERACTION WITH PLCG2.
RX PubMed=14704368; DOI=10.1189/jlb.0903439;
RA Todt J.C., Hu B., Curtis J.L.;
RT "The receptor tyrosine kinase MerTK activates phospholipase C gamma2 during
RT recognition of apoptotic thymocytes by murine macrophages.";
RL J. Leukoc. Biol. 75:705-713(2004).
RN [7]
RP INTERACTION WITH FAK/PTK2.
RX PubMed=15673687; DOI=10.1242/jcs.01632;
RA Wu Y., Singh S., Georgescu M.M., Birge R.B.;
RT "A role for Mer tyrosine kinase in alphavbeta5 integrin-mediated
RT phagocytosis of apoptotic cells.";
RL J. Cell Sci. 118:539-553(2005).
RN [8]
RP PHOSPHORYLATION AT TYR-867.
RX PubMed=18039660; DOI=10.1074/jbc.m706906200;
RA Tibrewal N., Wu Y., D'mello V., Akakura R., George T.C., Varnum B.,
RA Birge R.B.;
RT "Autophosphorylation docking site Tyr-867 in Mer receptor tyrosine kinase
RT allows for dissociation of multiple signaling pathways for phagocytosis of
RT apoptotic cells and down-modulation of lipopolysaccharide-inducible NF-
RT kappaB transcriptional activation.";
RL J. Biol. Chem. 283:3618-3627(2008).
RN [9]
RP FUNCTION.
RX PubMed=19117932; DOI=10.1167/iovs.08-3058;
RA Strick D.J., Feng W., Vollrath D.;
RT "Mertk drives myosin II redistribution during retinal pigment epithelial
RT phagocytosis.";
RL Invest. Ophthalmol. Vis. Sci. 50:2427-2435(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
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 [11]
RP INTERACTION WITH TUB AND TULP1.
RX PubMed=20978472; DOI=10.1038/emboj.2010.265;
RA Caberoy N.B., Zhou Y., Li W.;
RT "Tubby and tubby-like protein 1 are new MerTK ligands for phagocytosis.";
RL EMBO J. 29:3898-3910(2010).
RN [12]
RP FUNCTION IN IMMUNE RESPONSE INHIBITION.
RX PubMed=20363878; DOI=10.1210/en.2009-1498;
RA Sun B., Qi N., Shang T., Wu H., Deng T., Han D.;
RT "Sertoli cell-initiated testicular innate immune response through toll-like
RT receptor-3 activation is negatively regulated by Tyro3, Axl, and mer
RT receptors.";
RL Endocrinology 151:2886-2897(2010).
RN [13]
RP INTERACTION WITH LGALS3.
RX PubMed=21792939; DOI=10.1002/jcp.22955;
RA Caberoy N.B., Alvarado G., Bigcas J.L., Li W.;
RT "Galectin-3 is a new MerTK-specific eat-me signal.";
RL J. Cell. Physiol. 227:401-407(2012).
CC -!- FUNCTION: Receptor tyrosine kinase that transduces signals from the
CC extracellular matrix into the cytoplasm by binding to several ligands
CC including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological
CC processes including cell survival, migration, differentiation, and
CC phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the
CC cell surface induces autophosphorylation of MERTK on its intracellular
CC domain that provides docking sites for downstream signaling molecules.
CC Following activation by ligand, interacts with GRB2 or PLCG2 and
CC induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK
CC signaling plays a role in various processes such as macrophage
CC clearance of apoptotic cells, platelet aggregation, cytoskeleton
CC reorganization and engulfment. Functions in the retinal pigment
CC epithelium (RPE) as a regulator of rod outer segments fragments
CC phagocytosis. Also plays an important role in inhibition of Toll-like
CC receptors (TLRs)-mediated innate immune response by activating STAT1,
CC which selectively induces production of suppressors of cytokine
CC signaling SOCS1 and SOCS3. {ECO:0000269|PubMed:19117932,
CC ECO:0000269|PubMed:20363878}.
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: Interacts (upon activation) with TNK2; stimulates TNK2
CC autophosphorylation. Interacts (via N-terminus) with extracellular
CC ligands LGALS3, TUB, TULP1 and GAS6. Interacts with VAV1 in a
CC phosphotyrosine-independent manner. Interacts with TIMD4; this
CC interaction enhances TIMD4-mediated efferocytosis (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12866};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the hematopoietic
CC lineages: macrophages, NK cells, NKT cells, dendritic cells and
CC platelets. {ECO:0000269|PubMed:12884290}.
CC -!- DEVELOPMENTAL STAGE: Expressed during most, if not all, stages of
CC embryological development beginning in the morula and blastocyst and
CC progressing through the yolk sac and fetal liver stages.
CC -!- PTM: Autophosphorylated on Tyr-744, Tyr-748 and Tyr-749 in the
CC activation loop allowing full activity (By similarity).
CC Autophosphorylated on Tyr-867 leading to recruitment of downstream
CC partners of the signaling cascade such as PLCG2. {ECO:0000250,
CC ECO:0000269|PubMed:18039660}.
CC -!- DISRUPTION PHENOTYPE: knockout mice are fertile, but male animals that
CC lack all three receptors TYRO3, AXL and MERTK produce no mature sperm.
CC {ECO:0000269|PubMed:10227296}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. AXL/UFO subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; U21301; AAA80222.1; -; mRNA.
DR EMBL; L11625; AAA85355.1; -; mRNA.
DR CCDS; CCDS16716.1; -.
DR PIR; I49276; I49276.
DR RefSeq; NP_032613.1; NM_008587.2.
DR AlphaFoldDB; Q60805; -.
DR SMR; Q60805; -.
DR BioGRID; 201398; 19.
DR IntAct; Q60805; 1.
DR STRING; 10090.ENSMUSP00000014505; -.
DR GlyConnect; 2804; 6 N-Linked glycans (2 sites).
DR GlyGen; Q60805; 15 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; Q60805; -.
DR PhosphoSitePlus; Q60805; -.
DR CPTAC; non-CPTAC-3409; -.
DR MaxQB; Q60805; -.
DR PaxDb; Q60805; -.
DR PeptideAtlas; Q60805; -.
DR PRIDE; Q60805; -.
DR ProteomicsDB; 295928; -.
DR Antibodypedia; 33255; 870 antibodies from 43 providers.
DR DNASU; 17289; -.
DR Ensembl; ENSMUST00000014505; ENSMUSP00000014505; ENSMUSG00000014361.
DR GeneID; 17289; -.
DR KEGG; mmu:17289; -.
DR UCSC; uc008mgt.1; mouse.
DR CTD; 10461; -.
DR MGI; MGI:96965; Mertk.
DR VEuPathDB; HostDB:ENSMUSG00000014361; -.
DR eggNOG; ENOG502QQQ3; Eukaryota.
DR GeneTree; ENSGT00940000155669; -.
DR HOGENOM; CLU_015796_0_0_1; -.
DR InParanoid; Q60805; -.
DR OMA; LVIKWKP; -.
DR OrthoDB; 263089at2759; -.
DR PhylomeDB; Q60805; -.
DR TreeFam; TF317402; -.
DR BRENDA; 2.7.10.1; 3474.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR BioGRID-ORCS; 17289; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q60805; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q60805; protein.
DR Bgee; ENSMUSG00000014361; Expressed in stroma of bone marrow and 233 other tissues.
DR Genevisible; Q60805; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0043277; P:apoptotic cell clearance; IDA:MGI.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0046649; P:lymphocyte activation; IGI:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IGI:MGI.
DR GO; GO:0001818; P:negative regulation of cytokine production; IGI:MGI.
DR GO; GO:2000107; P:negative regulation of leukocyte apoptotic process; ISO:MGI.
DR GO; GO:0051250; P:negative regulation of lymphocyte activation; IGI:MGI.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0097350; P:neutrophil clearance; IGI:MGI.
DR GO; GO:0006909; P:phagocytosis; ISO:MGI.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IGI:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0032940; P:secretion by cell; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0060068; P:vagina development; IGI:MGI.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Proto-oncogene; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..994
FT /note="Tyrosine-protein kinase Mer"
FT /id="PRO_0000024444"
FT TOPO_DOM 19..497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..994
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 75..181
FT /note="Ig-like C2-type 1"
FT DOMAIN 192..268
FT /note="Ig-like C2-type 2"
FT DOMAIN 281..376
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 381..478
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 582..852
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 44..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 718
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 588..596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12866"
FT MOD_RES 744
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q12866"
FT MOD_RES 748
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q12866"
FT MOD_RES 749
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q12866"
FT MOD_RES 867
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18039660"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 213..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 867
FT /note="Y->F: Loss of GRB2 binding."
FT /evidence="ECO:0000269|PubMed:9891051"
FT CONFLICT 473..476
FT /note="IIIP -> SARA (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="I -> V (in Ref. 2; AAA85355)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 994 AA; 110157 MW; 603C09FA11F76FE0 CRC64;
MVLAPLLLGL LLLPALWSGG TAEKWEETEL DQLFSGPLPG RLPVNHRPFS APHSSRDQLP
PPQTGRSHPA HTAAPQVTST ASKLLPPVAF NHTIGHIVLS EHKNVKFNCS INIPNTYQET
AGISWWKDGK ELLGAHHSIT QFYPDEEGVS IIALFSIASV QRSDNGSYFC KMKVNNREIV
SDPIYVEVQG LPYFIKQPES VNVTRNTAFN LTCQAVGPPE PVNIFWVQNS SRVNEKPERS
PSVLTVPGLT ETAVFSCEAH NDKGLTVSKG VHINIKVIPS PPTEVHILNS TAHSILVSWV
PGFDGYSPLQ NCSIQVKEAD RLSNGSVMVF NTSASPHLYE IQQLQALANY SIAVSCRNEI
GWSAVSPWIL ASTTEGAPSV APLNITVFLN ESNNILDIRW TKPPIKRQDG ELVGYRISHV
WESAGTYKEL SEEVSQNGSW AQIPVQIHNA TCTVRIAAIT KGGIGPFSEP VNIIIPEHSK
VDYAPSSTPA PGNTDSMFII LGCFCGFILI GLILCISLAL RRRVQETKFG GAFSEEDSQL
VVNYRAKKSF CRRAIELTLQ SLGVSEELQN KLEDVVIDRN LLVLGKVLGE GEFGSVMEGN
LKQEDGTSQK VAVKTMKLDN FSQREIEEFL SEAACMKDFN HPNVIRLLGV CIELSSQGIP
KPMVILPFMK YGDLHTFLLY SRLNTGPKYI HLQTLLKFMM DIAQGMEYLS NRNFLHRDLA
ARNCMLRDDM TVCVADFGLS KKIYSGDYYR QGRIAKMPVK WIAIESLADR VYTSKSDVWA
FGVTMWEITT RGMTPYPGVQ NHEMYDYLLH GHRLKQPEDC LDELYDIMYS CWSADPLDRP
TFSVLRLQLE KLSESLPDAQ DKESIIYINT QLLESCEGIA NGPSLTGLDM NIDPDSIIAS
CTPGAAVSVV TAEVHENNLR EERYILNGGN EEWEDVSSTP FAAVTPEKDG VLPEDRLTKN
GVSWSHHSTL PLGSPSPDEL LFVDDSLEDS EVLM
