(data stored in ACNUC1130 zone)

HOVERGEN: RON_MOUSE

ID   RON_MOUSE               Reviewed;        1378 AA.
AC   Q62190; Q62555;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   13-OCT-2009, entry version 99.
DE   RecName: Full=Macrophage-stimulating protein receptor;
DE            Short=MSP receptor;
DE            EC=2.7.10.1;
DE   AltName: Full=p185-Ron;
DE   AltName: Full=Stem cell-derived tyrosine kinase;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94250897; PubMed=8193352;
RA   Iwama A., Okano A., Sudo T., Matsuda Y., Suda T.;
RT   "Molecular cloning of a novel receptor tyrosine kinase gene, STK,
RT   derived from enriched hematopoietic stem cells.";
RL   Blood 83:3160-3169(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=98127434; 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.,
RA   Air E.L., Sun W.Y., Thomas M.B., Degen S.J.F.;
RT   "Characterization of the mouse Ron/Stk receptor tyrosine kinase
RT   gene.";
RL   Oncogene 16:27-42(1998).
RN   [3]
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   [4]
RP   INTERACTION OF ISOFORM SF-STK WITH FRIEND SPLEEN FOCUS-FORMING VIRUS
RP   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
RT   covalently interacts with and constitutively activates a truncated
RT   form of the receptor tyrosine kinase Stk.";
RL   J. Virol. 75:7893-7903(2001).
CC   -!- FUNCTION: Receptor for macrophage stimulating protein (MSP). Has a
CC       tyrosine-protein kinase activity.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Heterodimer formed of an alpha chain and a beta chain
CC       which are disulfide linked. Binds PLXNB1 (By similarity).
CC       Associates with and is negatively regulated by HYAL2 (By
CC       similarity). Isoform sf-Stk forms covalent heterodimers with
CC       friend spleen focus-forming virus (FSFFV) gp55.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       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         Note=Lacks part of the extracellular domain, oligomerizes and is
CC         constitutively activated. This isoform confers host
CC         susceptibility to Friend disease;
CC   -!- PTM: Proteolytically cleaved to yield the alpha and the beta
CC       chains.
CC   -!- PTM: Phosphorylated in response to ligand binding (By similarity).
CC   -!- MISCELLANEOUS: Interaction with FSFFV envelope-like membrane
CC       glycoprotein gp55 results in constitutive tyrosine phosphorylation
CC       and activation of isoform sf-Stk.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family.
CC   -!- SIMILARITY: Contains 3 IPT/TIG domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 Sema domain.
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CC   -!- GENE_FAMILY: HBG006348 [ FAMILY / ALN / TREE ]
DR   EMBL; X74736; CAA52754.1; -; mRNA.
DR   EMBL; U65949; AAC39953.1; -; Genomic_DNA.
DR   IPI; IPI00311127; -.
DR   PIR; I48751; I48751.
DR   UniGene; Mm.3901; -.
DR   HSSP; P11362; 1FGK.
DR   STRING; Q62190; -.
DR   PhosphoSite; Q62190; -.
DR   PRIDE; Q62190; -.
DR   Ensembl; ENSMUST00000035203; ENSMUSP00000035203; ENSMUSG00000032584; Mus musculus.
DR   KEGG; mmu:19882; -.
DR   UCSC; uc009rni.1; mouse.
DR   CTD; 19882; -.
DR   MGI; MGI:99614; Mst1r.
DR   HOGENOM; Q62190; -.
DR   HOVERGEN; Q62190; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 297384; -.
DR   ArrayExpress; Q62190; -.
DR   Bgee; Q62190; -.
DR   Genevestigator; Q62190; -.
DR   GermOnline; ENSMUSG00000032584; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0001725; C:stress fiber; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kin...; IEA:EC.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:InterPro.
DR   GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR000719; Prot_kinase_core.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR001245; Tyr_pkinase.
DR   InterPro; IPR008266; Tyr_pkinase_AS.
DR   InterPro; IPR016244; TyrPK_HGF-R.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   Pfam; PF01833; TIG; 3.
DR   PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   ProDom; PD000001; Prot_kinase; 1.
DR   SMART; SM00429; IPT; 4.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SMART; SM00219; TyrKc; 1.
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;
DR   PRODOM; Q62190.
DR   SWISS-2DPAGE; Q62190.
KW   Alternative splicing; ATP-binding; Cleavage on pair of basic residues;
KW   Disulfide bond; Glycoprotein; Host-virus interaction; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Repeat;
KW   Signal; Transferase; Transmembrane; Tyrosine-protein kinase.
FT   DOMAIN       28     70       PRODOM:2005.1:PD025042  2
FT   DOMAIN       71    150       PRODOM:2005.1:PD003973  45
FT   DOMAIN      152    229       PRODOM:2005.1:PD962738  14
FT   DOMAIN      248    395       PRODOM:2005.1:PD331587  41
FT   DOMAIN      398    476       PRODOM:2005.1:PD314756  3
FT   DOMAIN      488    533       PRODOM:2005.1:PDA1E5D5  5
FT   DOMAIN      534    603       PRODOM:2005.1:PD001668  42
FT   DOMAIN      604    685       PRODOM:2005.1:PD721145  1
FT   DOMAIN      686    741       PRODOM:2005.1:PD003981  45
FT   DOMAIN      758    959       PRODOM:2005.1:PD591320  41
FT   DOMAIN     1018   1063       PRODOM:2005.1:PD702648  2
FT   DOMAIN     1317   1378       PRODOM:2005.1:PD019143  1
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24   1378       Macrophage-stimulating protein receptor.
FT                                /FTId=PRO_0000024455.
FT   CHAIN        25    305       Macrophage-stimulating protein receptor
FT                                alpha chain (Potential).
FT                                /FTId=PRO_0000024456.
FT   CHAIN       311   1378       Macrophage-stimulating protein receptor
FT                                beta chain (Potential).
FT                                /FTId=PRO_0000024457.
FT   TOPO_DOM     25    960       Extracellular (Potential).
FT   TRANSMEM    961    981       Potential.
FT   TOPO_DOM    982   1378       Cytoplasmic (Potential).
FT   DOMAIN       33    524       Sema.
FT   DOMAIN      571    673       IPT/TIG 1.
FT   DOMAIN      686    769       IPT/TIG 2.
FT   DOMAIN      772    864       IPT/TIG 3.
FT   DOMAIN     1059   1322       Protein kinase.
FT   NP_BIND    1065   1073       ATP (By similarity).
FT   COMPBIAS    307    310       Poly-Arg.
FT   ACT_SITE   1185   1185       Proton acceptor (By similarity).
FT   BINDING    1091   1091       ATP (By similarity).
FT   MOD_RES    1330   1330       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1337   1337       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   CARBOHYD     91     91       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    391    391       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    460    460       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    490    490       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    656    656       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    722    722       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    845    845       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    901    901       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    713    714       VG -> IA (in Ref. 1; CAA52754).
FT   CONFLICT    719    719       V -> A (in Ref. 1; CAA52754).
SQ   SEQUENCE   1378 AA;  150538 MW;  FC5F932377B57009 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
     MRHGDLLRFI 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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