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Macrophage-stimulating protein receptor (MSP receptor) (EC 2.7.10.1) (Stem cell-derived tyrosine kinase) (p185-Ron) (CD antigen CD136) [Cleaved into: Macrophage-stimulating protein receptor alpha chain; Macrophage-stimulating protein receptor beta chain]

 RON_MOUSE               Reviewed;        1378 AA.
Q62190; E9QMZ4; Q62555;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
07-NOV-2018, entry version 180.
RecName: Full=Macrophage-stimulating protein receptor;
Short=MSP receptor;
EC=2.7.10.1;
AltName: Full=Stem cell-derived tyrosine kinase;
AltName: Full=p185-Ron;
AltName: CD_antigen=CD136;
Contains:
RecName: Full=Macrophage-stimulating protein receptor alpha chain;
Contains:
RecName: Full=Macrophage-stimulating protein receptor beta chain;
Flags: Precursor;
Name=Mst1r; Synonyms=Ron, Stk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8193352;
Iwama A., Okano A., Sudo T., Matsuda Y., Suda T.;
"Molecular cloning of a novel receptor tyrosine kinase gene, STK,
derived from enriched hematopoietic stem cells.";
Blood 83:3160-3169(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=9467940; DOI=10.1038/sj.onc.1201508;
Waltz S.E., Toms C.L.V., McDowell S.A., Clay L.A., Muraoka R.S.,
Air E.L., Sun W.Y., Thomas M.B., Degen S.J.F.;
"Characterization of the mouse Ron/Stk receptor tyrosine kinase
gene.";
Oncogene 16:27-42(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
TISSUE SPECIFICITY.
PubMed=8545120;
Gaudino G., Avantaggiato V., Follenzi A., Acampora D., Simeone A.,
Comoglio P.M.;
"The proto-oncogene RON is involved in development of epithelial, bone
and neuro-endocrine tissues.";
Oncogene 11:2627-2637(1995).
[5]
DISRUPTION PHENOTYPE.
PubMed=9680329;
Correll P.H., Iwama A., Tondat S., Mayrhofer G., Suda T.,
Bernstein A.;
"Deregulated inflammatory response in mice lacking the STK/RON
receptor tyrosine kinase.";
Genes Funct. 1:69-83(1997).
[6]
ALTERNATIVE SPLICING.
PubMed=10508511; DOI=10.1038/13787;
Persons D.A., Paulson R.F., Loyd M.R., Herley M.T., Bodner S.M.,
Bernstein A., Correll P.H., Ney P.A.;
"Fv2 encodes a truncated form of the Stk receptor tyrosine kinase.";
Nat. Genet. 23:159-165(1999).
[7]
INTERACTION OF ISOFORM SF-STK WITH FRIEND SPLEEN FOCUS-FORMING VIRUS
GP55.
PubMed=11483734; DOI=10.1128/JVI.75.17.7893-7903.2001;
Nishigaki K., Thompson D., Hanson C., Yugawa T., Ruscetti S.;
"The envelope glycoprotein of friend spleen focus-forming virus
covalently interacts with and constitutively activates a truncated
form of the receptor tyrosine kinase Stk.";
J. Virol. 75:7893-7903(2001).
-!- FUNCTION: Receptor tyrosine kinase that transduces signals from
the extracellular matrix into the cytoplasm by binding to MST1
ligand. Regulates many physiological processes including cell
survival, migration and differentiation. Ligand binding at the
cell surface induces autophosphorylation of RON on its
intracellular domain that provides docking sites for downstream
signaling molecules. Following activation by ligand, interacts
with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1.
Recruitment of these downstream effectors by RON leads to the
activation of several signaling cascades including the RAS-ERK,
PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound
healing response by promoting epithelial cell migration,
proliferation as well as survival at the wound site. Plays also a
role in the innate immune response by regulating the migration and
phagocytic activity of macrophages. Alternatively, RON can also
promote signals such as cell migration and proliferation in
response to growth factors other than MST1 ligand.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ACTIVITY REGULATION: In its inactive state, the C-terminal tail
interacts with the catalytic domain and inhibits the kinase
activity. Upon ligand binding, the C-terminal tail is displaced
and becomes phosphorylated, thus increasing the kinase activity.
-!- SUBUNIT: Heterodimer of an alpha chain and a beta chain which are
disulfide linked. Binds PLXNB1. Associates with and is negatively
regulated by HYAL2. Interacts when phosphorylated with downstream
effectors including PIK3R1, PCLG1, GRB2 and GAB1. Interacts with
integrin beta1/ITGB1 in a ligand-independent fashion. Isoform sf-
Stk forms covalent heterodimers with friend spleen focus-forming
virus (FSFFV) gp55. {ECO:0000269|PubMed:11483734}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=RON;
IsoId=Q62190-1; Sequence=Displayed;
Name=sf-Stk;
IsoId=Q62190-2; Sequence=Not described;
Note=Lacks part of the extracellular domain, oligomerizes and is
constitutively activated. This isoform confers host
susceptibility to Friend disease.;
-!- TISSUE SPECIFICITY: Expressed in liver, skin, lung, brain, testis
and kidney. {ECO:0000269|PubMed:8545120}.
-!- PTM: Proteolytic processing yields the two subunits.
{ECO:0000250}.
-!- PTM: Autophosphorylated in response to ligand binding on Tyr-1215
and Tyr-1216 in the kinase domain leading to further
phosphorylation of Tyr-1330 and Tyr-1337 in the C-terminal
multifunctional docking site. {ECO:0000250}.
-!- PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor
stability and activity through proteasomal degradation (By
similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show increased inflammation in an IFN-
gamma-mediated delayed-type hypersensitivity reaction and
increased susceptibility to lipopolysaccharide-induced endotoxic
shock. {ECO:0000269|PubMed:9680329}.
-!- MISCELLANEOUS: Interaction with FSFFV envelope-like membrane
glycoprotein gp55 results in constitutive tyrosine phosphorylation
and activation of isoform sf-Stk.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; X74736; CAA52754.1; -; mRNA.
EMBL; U65949; AAC39953.1; -; Genomic_DNA.
EMBL; AL731808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS23509.1; -. [Q62190-1]
PIR; I48751; I48751.
RefSeq; NP_033100.2; NM_009074.2. [Q62190-1]
UniGene; Mm.3901; -.
ProteinModelPortal; Q62190; -.
SMR; Q62190; -.
IntAct; Q62190; 1.
STRING; 10090.ENSMUSP00000035203; -.
BindingDB; Q62190; -.
ChEMBL; CHEMBL1795170; -.
iPTMnet; Q62190; -.
PhosphoSitePlus; Q62190; -.
PaxDb; Q62190; -.
PRIDE; Q62190; -.
Ensembl; ENSMUST00000035203; ENSMUSP00000035203; ENSMUSG00000032584. [Q62190-1]
GeneID; 19882; -.
KEGG; mmu:19882; -.
UCSC; uc009rni.1; mouse. [Q62190-1]
CTD; 4486; -.
MGI; MGI:99614; Mst1r.
eggNOG; KOG1095; Eukaryota.
eggNOG; KOG3610; Eukaryota.
eggNOG; ENOG410XRIK; LUCA.
GeneTree; ENSGT00810000125384; -.
HOGENOM; HOG000220900; -.
HOVERGEN; HBG006348; -.
InParanoid; Q62190; -.
KO; K05100; -.
OMA; QHELRGD; -.
OrthoDB; EOG091G0751; -.
TreeFam; TF317402; -.
BRENDA; 2.7.10.1; 3474.
PRO; PR:Q62190; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032584; Expressed in 116 organ(s), highest expression level in stomach.
ExpressionAtlas; Q62190; baseline and differential.
Genevisible; Q62190; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0001725; C:stress fiber; IDA:MGI.
GO; GO:0005773; C:vacuole; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
GO; GO:0009968; P:negative regulation of signal transduction; IBA:GO_Central.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:0009615; P:response to virus; IMP:MGI.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; IBA:GO_Central.
CDD; cd11279; Sema_RON; 1.
Gene3D; 2.130.10.10; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR016201; PSI.
InterPro; IPR039413; RON_Sema.
InterPro; IPR001627; Semap_dom.
InterPro; IPR036352; Semap_dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016244; Tyr_kinase_HGF/MSP_rcpt.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01403; Sema; 1.
Pfam; PF01833; TIG; 3.
PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00429; IPT; 4.
SMART; SM00423; PSI; 1.
SMART; SM00630; Sema; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF101912; SSF101912; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF81296; SSF81296; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS51004; SEMA; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; Glycoprotein;
Host-virus interaction; Immunity; Innate immunity; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 1378 Macrophage-stimulating protein receptor.
/FTId=PRO_0000024455.
CHAIN 25 305 Macrophage-stimulating protein receptor
alpha chain. {ECO:0000255}.
/FTId=PRO_0000024456.
CHAIN 311 1378 Macrophage-stimulating protein receptor
beta chain. {ECO:0000255}.
/FTId=PRO_0000024457.
TOPO_DOM 25 960 Extracellular. {ECO:0000255}.
TRANSMEM 961 981 Helical. {ECO:0000255}.
TOPO_DOM 982 1378 Cytoplasmic. {ECO:0000255}.
DOMAIN 33 524 Sema. {ECO:0000255|PROSITE-
ProRule:PRU00352}.
DOMAIN 571 673 IPT/TIG 1.
DOMAIN 686 769 IPT/TIG 2.
DOMAIN 772 864 IPT/TIG 3.
DOMAIN 1059 1322 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1065 1073 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1138 1141 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 307 310 Poly-Arg.
ACT_SITE 1185 1185 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 1091 1091 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 1189 1189 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 1215 1215 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q04912}.
MOD_RES 1216 1216 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q04912}.
MOD_RES 1330 1330 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q04912}.
MOD_RES 1337 1337 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:Q04912}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 391 391 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 460 460 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 490 490 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 656 656 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 722 722 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 845 845 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 901 901 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 102 105 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 108 163 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 136 144 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 175 178 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 301 368 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 386 409 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 387 424 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 529 547 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 535 569 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 538 554 {ECO:0000255|PROSITE-ProRule:PRU00352}.
DISULFID 550 560 {ECO:0000255|PROSITE-ProRule:PRU00352}.
CONFLICT 713 714 VG -> IA (in Ref. 1; CAA52754).
{ECO:0000305}.
CONFLICT 719 719 V -> A (in Ref. 1; CAA52754).
{ECO:0000305}.
CONFLICT 1148 1148 H -> R (in Ref. 1; CAA52754 and 2;
AAC39953). {ECO:0000305}.
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


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