RON_MOUSE
ID RON_MOUSE Reviewed; 1378 AA.
AC Q62190; E9QMZ4; Q62555;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Macrophage-stimulating protein receptor;
DE Short=MSP receptor;
DE EC=2.7.10.1;
DE AltName: Full=Stem cell-derived tyrosine kinase;
DE AltName: Full=p185-Ron;
DE AltName: CD_antigen=CD136;
DE Contains:
DE RecName: Full=Macrophage-stimulating protein receptor alpha chain;
DE Contains:
DE RecName: Full=Macrophage-stimulating protein receptor beta chain;
DE Flags: Precursor;
GN Name=Mst1r; Synonyms=Ron, Stk;
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].
RX PubMed=8193352;
RA Iwama A., Okano A., Sudo T., Matsuda Y., Suda T.;
RT "Molecular cloning of a novel receptor tyrosine kinase gene, STK, derived
RT from enriched hematopoietic stem cells.";
RL Blood 83:3160-3169(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9467940; DOI=10.1038/sj.onc.1201508;
RA Waltz S.E., Toms C.L.V., McDowell S.A., Clay L.A., Muraoka R.S., Air E.L.,
RA Sun W.Y., Thomas M.B., Degen S.J.F.;
RT "Characterization of the mouse Ron/Stk receptor tyrosine kinase gene.";
RL Oncogene 16:27-42(1998).
RN [3]
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=8545120;
RA Gaudino G., Avantaggiato V., Follenzi A., Acampora D., Simeone A.,
RA Comoglio P.M.;
RT "The proto-oncogene RON is involved in development of epithelial, bone and
RT neuro-endocrine tissues.";
RL Oncogene 11:2627-2637(1995).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=9680329; DOI=10.1046/j.1365-4624.1997.00009.x;
RA Correll P.H., Iwama A., Tondat S., Mayrhofer G., Suda T., Bernstein A.;
RT "Deregulated inflammatory response in mice lacking the STK/RON receptor
RT tyrosine kinase.";
RL Genes Funct. 1:69-83(1997).
RN [6]
RP ALTERNATIVE SPLICING.
RX PubMed=10508511; DOI=10.1038/13787;
RA Persons D.A., Paulson R.F., Loyd M.R., Herley M.T., Bodner S.M.,
RA Bernstein A., Correll P.H., Ney P.A.;
RT "Fv2 encodes a truncated form of the Stk receptor tyrosine kinase.";
RL Nat. Genet. 23:159-165(1999).
RN [7]
RP INTERACTION OF ISOFORM SF-STK WITH FRIEND SPLEEN FOCUS-FORMING VIRUS GP55.
RX PubMed=11483734; DOI=10.1128/jvi.75.17.7893-7903.2001;
RA Nishigaki K., Thompson D., Hanson C., Yugawa T., Ruscetti S.;
RT "The envelope glycoprotein of friend spleen focus-forming virus covalently
RT interacts with and constitutively activates a truncated form of the
RT receptor tyrosine kinase Stk.";
RL J. Virol. 75:7893-7903(2001).
CC -!- FUNCTION: Receptor tyrosine kinase that transduces signals from the
CC extracellular matrix into the cytoplasm by binding to MST1 ligand.
CC Regulates many physiological processes including cell survival,
CC migration and differentiation. Ligand binding at the cell surface
CC induces autophosphorylation of RON on its intracellular domain that
CC provides docking sites for downstream signaling molecules. Following
CC activation by ligand, interacts with the PI3-kinase subunit PIK3R1,
CC PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by
CC RON leads to the activation of several signaling cascades including the
CC RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the
CC wound healing response by promoting epithelial cell migration,
CC proliferation as well as survival at the wound site. Also plays a role
CC in the innate immune response by regulating the migration and
CC phagocytic activity of macrophages. Alternatively, RON can also promote
CC signals such as cell migration and proliferation in response to growth
CC factors other than MST1 ligand.
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 -!- ACTIVITY REGULATION: In its inactive state, the C-terminal tail
CC interacts with the catalytic domain and inhibits the kinase activity.
CC Upon ligand binding, the C-terminal tail is displaced and becomes
CC phosphorylated, thus increasing the kinase activity.
CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain which are
CC disulfide linked. Binds PLXNB1. Associates with and is negatively
CC regulated by HYAL2. Interacts when phosphorylated with downstream
CC effectors including PIK3R1, PCLG1, GRB2 and GAB1. Interacts with
CC integrin beta1/ITGB1 in a ligand-independent fashion. Isoform sf-Stk
CC forms covalent heterodimers with friend spleen focus-forming virus
CC (FSFFV) gp55. {ECO:0000269|PubMed:11483734}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=RON;
CC IsoId=Q62190-1; Sequence=Displayed;
CC Name=sf-Stk;
CC IsoId=Q62190-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed in liver, skin, lung, brain, testis and
CC kidney. {ECO:0000269|PubMed:8545120}.
CC -!- PTM: Proteolytic processing yields the two subunits. {ECO:0000250}.
CC -!- PTM: Autophosphorylated in response to ligand binding on Tyr-1215 and
CC Tyr-1216 in the kinase domain leading to further phosphorylation of
CC Tyr-1330 and Tyr-1337 in the C-terminal multifunctional docking site.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor
CC stability and activity through proteasomal degradation (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show increased inflammation in an IFN-gamma-
CC mediated delayed-type hypersensitivity reaction and increased
CC susceptibility to lipopolysaccharide-induced endotoxic shock.
CC {ECO:0000269|PubMed:9680329}.
CC -!- MISCELLANEOUS: Interaction with FSFFV envelope-like membrane
CC glycoprotein gp55 results in constitutive tyrosine phosphorylation and
CC activation of isoform sf-Stk.
CC -!- MISCELLANEOUS: [Isoform sf-Stk]: Lacks part of the extracellular
CC domain, oligomerizes and is constitutively activated. This isoform
CC confers host susceptibility to Friend disease. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X74736; CAA52754.1; -; mRNA.
DR EMBL; U65949; AAC39953.1; -; Genomic_DNA.
DR EMBL; AL731808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS23509.1; -. [Q62190-1]
DR PIR; I48751; I48751.
DR RefSeq; NP_033100.2; NM_009074.2. [Q62190-1]
DR AlphaFoldDB; Q62190; -.
DR SMR; Q62190; -.
DR BioGRID; 202955; 11.
DR IntAct; Q62190; 2.
DR MINT; Q62190; -.
DR STRING; 10090.ENSMUSP00000035203; -.
DR BindingDB; Q62190; -.
DR ChEMBL; CHEMBL1795170; -.
DR DrugCentral; Q62190; -.
DR GlyGen; Q62190; 8 sites.
DR iPTMnet; Q62190; -.
DR PhosphoSitePlus; Q62190; -.
DR jPOST; Q62190; -.
DR MaxQB; Q62190; -.
DR PaxDb; Q62190; -.
DR PRIDE; Q62190; -.
DR ProteomicsDB; 260829; -. [Q62190-1]
DR Antibodypedia; 2092; 913 antibodies from 39 providers.
DR DNASU; 19882; -.
DR Ensembl; ENSMUST00000035203; ENSMUSP00000035203; ENSMUSG00000032584. [Q62190-1]
DR GeneID; 19882; -.
DR KEGG; mmu:19882; -.
DR UCSC; uc009rni.1; mouse. [Q62190-1]
DR CTD; 4486; -.
DR MGI; MGI:99614; Mst1r.
DR VEuPathDB; HostDB:ENSMUSG00000032584; -.
DR eggNOG; KOG1095; Eukaryota.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT00940000157842; -.
DR HOGENOM; CLU_005158_0_0_1; -.
DR InParanoid; Q62190; -.
DR OMA; TCWRCLR; -.
DR OrthoDB; 408584at2759; -.
DR PhylomeDB; Q62190; -.
DR TreeFam; TF317402; -.
DR BRENDA; 2.7.10.1; 3474.
DR Reactome; R-MMU-8852405; Signaling by MST1.
DR BioGRID-ORCS; 19882; 3 hits in 75 CRISPR screens.
DR PRO; PR:Q62190; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q62190; protein.
DR Bgee; ENSMUSG00000032584; Expressed in lip and 121 other tissues.
DR ExpressionAtlas; Q62190; baseline and differential.
DR Genevisible; Q62190; MM.
DR GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0005773; C:vacuole; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0009615; P:response to virus; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd11279; Sema_RON; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR039413; RON_Sema.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016244; Tyr_kinase_HGF/MSP_rcpt.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 3.
DR PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00429; IPT; 4.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00630; Sema; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF81296; SSF81296; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Host-virus interaction; Immunity;
KW Innate immunity; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1378
FT /note="Macrophage-stimulating protein receptor"
FT /id="PRO_0000024455"
FT CHAIN 25..305
FT /note="Macrophage-stimulating protein receptor alpha chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024456"
FT CHAIN 311..1378
FT /note="Macrophage-stimulating protein receptor beta chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024457"
FT TOPO_DOM 25..960
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 961..981
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 982..1378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..524
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 571..673
FT /note="IPT/TIG 1"
FT DOMAIN 686..769
FT /note="IPT/TIG 2"
FT DOMAIN 772..864
FT /note="IPT/TIG 3"
FT DOMAIN 1059..1322
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1002..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1185
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 1065..1073
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1091
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1138..1141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1215
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q04912"
FT MOD_RES 1216
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q04912"
FT MOD_RES 1330
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q04912"
FT MOD_RES 1337
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q04912"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 901
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 102..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 108..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 136..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 175..178
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 301..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 386..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 387..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 529..547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 535..569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 538..554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 550..560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT CONFLICT 713..714
FT /note="VG -> IA (in Ref. 1; CAA52754)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="V -> A (in Ref. 1; CAA52754)"
FT /evidence="ECO:0000305"
FT CONFLICT 1148
FT /note="H -> R (in Ref. 1; CAA52754 and 2; AAC39953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1378 AA; 150519 MW; 5899D3A17F95F76D CRC64;
MGLPLPLLQS SLLLMLLLRL SAASTNLNWQ CPRIPYAASR DFSVKYVVPS FSAGGRVQAT
AAYEDSTNSA VFVATRNHLH VLGPDLQFIE NLTTGPIGNP GCQTCASCGP GPHGPPKDTD
TLVLVMEPGL PALVSCGSTL QGRCFLHELE PRGKALHLAA PACLFSANNN KPEACTDCVA
SPLGTRVTVV EQGHASYFYV ASSLDPELAA SFSPRSVSIR RLKSDTSGFQ PGFPSLSVLP
KYLASYLIKY VYSFHSGDFV YFLTVQPISV TSPPSALHTR LVRLNAVEPE IGDYRELVLD
CHFAPKRRRR GAPEGTQPYP VLQAAHSAPV DAKLAVELSI SEGQEVLFGV FVTVKDGGSG
MGPNSVVCAF PIYHLNILIE EGVEYCCHSS NSSSLLSRGL DFFQTPSFCP NPPGGEASGP
SSRCHYFPLM VHASFTRVDL FNGLLGSVKV TALHVTRLGN VTVAHMGTVD GRVLQVEIAR
SLNYLLYVSN FSLGSSGQPV HRDVSRLGND LLFASGDQVF KVPIQGPGCR HFLTCWRCLR
AQRFMGCGWC GDRCDRQKEC PGSWQQDHCP PEISEFYPHS GPLRGTTRLT LCGSNFYLRP
DDVVPEGTHQ ITVGQSPCRL LPKDSSSPRP GSLKEFIQEL ECELEPLVTQ AVGTTNISLV
ITNMPAGKHF RVEGISVQEG FSFVEPVLTS IKPDFGPRAG GTYLTLEGQS LSVGTSRAVL
VNGTQCRLEQ VNEEQILCVT PPGAGTARVP LHLQIGGAEV PGSWTFHYKE DPIVLDISPK
CGYSGSHIMI HGQHLTSAWH FTLSFHDGQS TVESRCAGQF VEQQQRRCRL PEYVVRNPQG
WATGNLSVWG DGAAGFTLPG FRFLPPPSPL RAGLVELKPE EHSVKVEYVG LGAVADCVTV
NMTVGGEVCQ HELRGDVVIC PLPPSLQLGK DGVPLQVCVD GGCHILSQVV RSSPGRASQR
ILLIALLVLI LLVAVLAVAL IFNSRRRKKQ LGAHSLSPTT LSDINDTASG APNHEESSES
RDGTSVPLLR TESIRLQDLD RMLLAEVKDV LIPHEQVVIH TDQVIGKGHF GVVYHGEYTD
GAQNQTHCAI KSLSRITEVQ EVEAFLREGL LMRGLHHPNI LALIGIMLPP EGLPRVLLPY
MRHGDLLHFI RSPQRNPTVK DLVSFGLQVA CGMEYLAEQK FVHRDLAARN CMLDESFTVK
VADFGLARGV LDKEYYSVRQ HRHARLPVKW MALESLQTYR FTTKSDVWSF GVLLWELLTR
GAPPYPHIDP FDLSHFLAQG RRLPQPEYCP DSLYHVMLRC WEADPAARPT FRALVLEVKQ
VVASLLGDHY VQLTAAYVNV GPRAVDDGSV PPEQVQPSPQ HCRSTSKPRP LSEPPLPT
