RON_HUMAN
ID RON_HUMAN Reviewed; 1400 AA.
AC Q04912; A0A087WZG2; B5A944; B5A945; B5A946; B5A947;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Macrophage-stimulating protein receptor;
DE Short=MSP receptor;
DE EC=2.7.10.1;
DE AltName: Full=CDw136;
DE AltName: Full=Protein-tyrosine kinase 8;
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=PTK8, RON;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RON), AND VARIANTS GLN-322 AND ARG-523.
RC TISSUE=Keratinocyte;
RX PubMed=8386824;
RA Ronsin C., Muscatelli F., Mattei M.-G., Breathnach R.;
RT "A novel putative receptor protein tyrosine kinase of the met family.";
RL Oncogene 8:1195-1202(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=8816464; DOI=10.1128/mcb.16.10.5518;
RA Collesi C., Santoro M.M., Gaudino G., Comoglio P.M.;
RT "A splicing variant of the RON transcript induces constitutive tyrosine
RT kinase activity and an invasive phenotype.";
RL Mol. Cell. Biol. 16:5518-5526(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RON-1; RON-2; RON-3 AND RON-4).
RX PubMed=18593464; DOI=10.1186/ar2447;
RA Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
RA Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
RT "Novel splice variants derived from the receptor tyrosine kinase
RT superfamily are potential therapeutics for rheumatoid arthritis.";
RL Arthritis Res. Ther. 10:R73-R73(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP INTERACTION WITH PIK3R1.
RX PubMed=7687741; DOI=10.1128/mcb.13.8.4600-4608.1993;
RA Ponzetto C., Bardelli A., Maina F., Longati P., Panayotou G., Dhand R.,
RA Waterfield M.D., Comoglio P.M.;
RT "A novel recognition motif for phosphatidylinositol 3-kinase binding
RT mediates its association with the hepatocyte growth factor/scatter factor
RT receptor.";
RL Mol. Cell. Biol. 13:4600-4608(1993).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=8062829; DOI=10.1002/j.1460-2075.1994.tb06659.x;
RA Gaudino G., Follenzi A., Naldini L., Collesi C., Santoro M., Gallo K.A.,
RA Godowski P.J., Comoglio P.M.;
RT "RON is a heterodimeric tyrosine kinase receptor activated by the HGF
RT homologue MSP.";
RL EMBO J. 13:3524-3532(1994).
RN [7]
RP FUNCTION.
RX PubMed=7939629; DOI=10.1126/science.7939629;
RA Wang M.-H., Ronsin C., Gesnel M.-C., Coupey L., Skeel A., Leonard E.J.,
RA Breatnach R.;
RT "Identification of the ron gene product as the receptor for the human
RT macrophage stimulating protein.";
RL Science 266:117-119(1994).
RN [8]
RP FUNCTION IN WOUND HEALING RESPONSE.
RX PubMed=9764835; DOI=10.1046/j.1523-1747.1998.00332.x;
RA Nanney L.B., Skeel A., Luan J., Polis S., Richmond A., Wang M.H.,
RA Leonard E.J.;
RT "Proteolytic cleavage and activation of pro-macrophage-stimulating protein
RT and upregulation of its receptor in tissue injury.";
RL J. Invest. Dermatol. 111:573-581(1998).
RN [9]
RP INTERACTION WITH ITGB1.
RX PubMed=10222149; DOI=10.1006/excr.1999.4429;
RA Danilkovitch A., Skeel A., Leonard E.J.;
RT "Macrophage stimulating protein-induced epithelial cell adhesion is
RT mediated by a PI3-K-dependent, but FAK-independent mechanism.";
RL Exp. Cell Res. 248:575-582(1999).
RN [10]
RP INTERACTION WITH MST1.
RX PubMed=10514476; DOI=10.1074/jbc.274.42.29937;
RA Danilkovitch A., Miller M., Leonard E.J.;
RT "Interaction of macrophage-stimulating protein with its receptor. Residues
RT critical for beta chain binding and evidence for independent alpha chain
RT binding.";
RL J. Biol. Chem. 274:29937-29943(1999).
RN [11]
RP REVIEW ON FUNCTION.
RX PubMed=12472665; DOI=10.1046/j.1365-3083.2002.01177.x;
RA Wang M.H., Zhou Y.Q., Chen Y.Q.;
RT "Macrophage-stimulating protein and RON receptor tyrosine kinase: potential
RT regulators of macrophage inflammatory activities.";
RL Scand. J. Immunol. 56:545-553(2002).
RN [12]
RP UBIQUITINATION.
RX PubMed=12802274; DOI=10.1038/sj.onc.1206585;
RA Penengo L., Rubin C., Yarden Y., Gaudino G.;
RT "c-Cbl is a critical modulator of the Ron tyrosine kinase receptor.";
RL Oncogene 22:3669-3679(2003).
RN [13]
RP INTERACTION WITH HYAL2.
RX PubMed=12676986; DOI=10.1073/pnas.0837136100;
RA Danilkovitch-Miagkova A., Duh F.-M., Kuzmin I., Angeloni D., Liu S.-L.,
RA Miller A.D., Lerman M.I.;
RT "Hyaluronidase 2 negatively regulates RON receptor tyrosine kinase and
RT mediates transformation of epithelial cells by jaagsiekte sheep
RT retrovirus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4580-4585(2003).
RN [14]
RP INTERACTION WITH PLXNB1.
RX PubMed=15184888; DOI=10.1038/sj.onc.1207650;
RA Conrotto P., Corso S., Gamberini S., Comoglio P.M., Giordano S.;
RT "Interplay between scatter factor receptors and B plexins controls invasive
RT growth.";
RL Oncogene 23:5131-5137(2004).
RN [15]
RP PHOSPHORYLATION AT TYR-1238; TYR-1239; TYR-1353 AND TYR-1360, AND ACTIVITY
RP REGULATION.
RX PubMed=15632155; DOI=10.1074/jbc.m412623200;
RA Yokoyama N., Ischenko I., Hayman M.J., Miller W.T.;
RT "The C terminus of RON tyrosine kinase plays an autoinhibitory role.";
RL J. Biol. Chem. 280:8893-8900(2005).
RN [16]
RP FUNCTION.
RX PubMed=18836480; DOI=10.1038/onc.2008.383;
RA Feres K.J., Ischenko I., Hayman M.J.;
RT "The RON receptor tyrosine kinase promotes MSP-independent cell spreading
RT and survival in breast epithelial cells.";
RL Oncogene 28:279-288(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP INTERACTION WITH GAB1 AND GRB2.
RX PubMed=21784853; DOI=10.1074/jbc.m111.239384;
RA Chaudhuri A., Xie M.H., Yang B., Mahapatra K., Liu J., Marsters S.,
RA Bodepudi S., Ashkenazi A.;
RT "Distinct involvement of the Gab1 and Grb2 adaptor proteins in signal
RT transduction by the related receptor tyrosine kinases RON and MET.";
RL J. Biol. Chem. 286:32762-32774(2011).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1060-1357 IN COMPLEX WITH AMP-PNP
RP AND MAGNESIUM, ACTIVE SITE, AND PHOSPHORYLATION AT TYR-1238.
RX PubMed=20726546; DOI=10.1021/bi100409w;
RA Wang J., Steinbacher S., Augustin M., Schreiner P., Epstein D.,
RA Mulvihill M.J., Crew A.P.;
RT "The crystal structure of a constitutively active mutant RON kinase
RT suggests an intramolecular autophosphorylation hypothesis.";
RL Biochemistry 49:7972-7974(2010).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 42-568, GLYCOSYLATION AT ASN-488,
RP AND DISULFIDE BONDS.
RX PubMed=22848655; DOI=10.1371/journal.pone.0041912;
RA Chao K.L., Tsai I.W., Chen C., Herzberg O.;
RT "Crystal structure of the Sema-PSI extracellular domain of human RON
RT receptor tyrosine kinase.";
RL PLoS ONE 7:E41912-E41912(2012).
RN [21]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-75; THR-95; CYS-185; GLN-322; ASP-356;
RP LEU-434; ASP-465; CYS-504; ARG-523; PRO-613; MET-900; GLY-1304; GLY-1335
RP AND CYS-1360.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [22]
RP VARIANTS NPCA3 HIS-306; THR-327; GLY-670 AND THR-973, AND INVOLVEMENT IN
RP NPCA3.
RX PubMed=26951679; DOI=10.1073/pnas.1523436113;
RA Dai W., Zheng H., Cheung A.K., Tang C.S., Ko J.M., Wong B.W., Leong M.M.,
RA Sham P.C., Cheung F., Kwong D.L., Ngan R.K., Ng W.T., Yau C.C., Pan J.,
RA Peng X., Tung S., Zhang Z., Ji M., Chiang A.K., Lee A.W., Lee V.H.,
RA Lam K.O., Au K.H., Cheng H.C., Yiu H.H., Lung M.L.;
RT "Whole-exome sequencing identifies MST1R as a genetic susceptibility gene
RT in nasopharyngeal carcinoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:3317-3322(2016).
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. {ECO:0000269|PubMed:18836480,
CC ECO:0000269|PubMed:7939629, ECO:0000269|PubMed:9764835}.
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 {ECO:0000269|PubMed:15632155}.
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.
CC {ECO:0000269|PubMed:10222149, ECO:0000269|PubMed:10514476,
CC ECO:0000269|PubMed:12676986, ECO:0000269|PubMed:15184888,
CC ECO:0000269|PubMed:20726546, ECO:0000269|PubMed:21784853,
CC ECO:0000269|PubMed:7687741}.
CC -!- INTERACTION:
CC Q04912; P26927: MST1; NbExp=5; IntAct=EBI-2637518, EBI-6929133;
CC Q04912; O43157: PLXNB1; NbExp=3; IntAct=EBI-2637518, EBI-1111488;
CC Q04912; O15031: PLXNB2; NbExp=2; IntAct=EBI-2637518, EBI-722004;
CC Q04912; Q9ULL4: PLXNB3; NbExp=2; IntAct=EBI-2637518, EBI-311073;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=RON;
CC IsoId=Q04912-1; Sequence=Displayed;
CC Name=Delta-RON; Synonyms=sf-RON;
CC IsoId=Q04912-2; Sequence=VSP_005007;
CC Name=RON-1;
CC IsoId=Q04912-3; Sequence=VSP_038920, VSP_038921;
CC Name=RON-2;
CC IsoId=Q04912-4; Sequence=VSP_038919, VSP_038922, VSP_038923;
CC Name=RON-3;
CC IsoId=Q04912-5; Sequence=VSP_038924, VSP_038925;
CC Name=RON-4;
CC IsoId=Q04912-6; Sequence=VSP_038922, VSP_038923;
CC Name=RON-5;
CC IsoId=Q04912-7; Sequence=VSP_038919;
CC -!- TISSUE SPECIFICITY: Expressed in colon, skin, lung and bone marrow.
CC {ECO:0000269|PubMed:8062829}.
CC -!- PTM: Proteolytic processing yields the two subunits.
CC -!- PTM: Autophosphorylated in response to ligand binding on Tyr-1238 and
CC Tyr-1239 in the kinase domain leading to further phosphorylation of
CC Tyr-1353 and Tyr-1360 in the C-terminal multifunctional docking site.
CC {ECO:0000269|PubMed:15632155, ECO:0000269|PubMed:20726546}.
CC -!- PTM: Ubiquitinated. Ubiquitination by CBL regulates the receptor
CC stability and activity through proteasomal degradation.
CC {ECO:0000269|PubMed:12802274}.
CC -!- DISEASE: Nasopharyngeal carcinoma, 3 (NPCA3) [MIM:617075]: A form of
CC nasopharyngeal carcinoma, a malignant neoplasm that originates in the
CC nasopharyngeal epithelium and includes 4 subtypes: keratinizing
CC squamous cell, non-keratinizing, basaloid squamous cell, and papillary
CC adenocarcinoma. {ECO:0000269|PubMed:26951679}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- MISCELLANEOUS: [Isoform Delta-RON]: Lacks part of the extracellular
CC domain, oligomerizes and is constitutively activated. Expressed at
CC higher level in cancer cells. {ECO:0000303|PubMed:26951679}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RONID287.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X70040; CAA49634.1; -; mRNA.
DR EMBL; EU826582; ACF47618.1; -; mRNA.
DR EMBL; EU826583; ACF47619.1; -; mRNA.
DR EMBL; EU826584; ACF47620.1; -; mRNA.
DR EMBL; EU826585; ACF47621.1; -; mRNA.
DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC876868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS2807.1; -. [Q04912-1]
DR CCDS; CCDS58833.1; -. [Q04912-2]
DR CCDS; CCDS82777.1; -. [Q04912-7]
DR PIR; I38185; I38185.
DR RefSeq; NP_001231866.1; NM_001244937.2. [Q04912-2]
DR RefSeq; NP_002438.2; NM_002447.3. [Q04912-1]
DR PDB; 3PLS; X-ray; 2.24 A; A=1060-1357.
DR PDB; 4FWW; X-ray; 1.85 A; A=42-568.
DR PDB; 4QT8; X-ray; 3.00 A; A/B=25-683.
DR PDBsum; 3PLS; -.
DR PDBsum; 4FWW; -.
DR PDBsum; 4QT8; -.
DR AlphaFoldDB; Q04912; -.
DR SMR; Q04912; -.
DR BioGRID; 110592; 99.
DR DIP; DIP-6029N; -.
DR IntAct; Q04912; 15.
DR MINT; Q04912; -.
DR STRING; 9606.ENSP00000296474; -.
DR BindingDB; Q04912; -.
DR ChEMBL; CHEMBL2689; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q04912; -.
DR GuidetoPHARMACOLOGY; 1816; -.
DR GlyGen; Q04912; 8 sites.
DR iPTMnet; Q04912; -.
DR PhosphoSitePlus; Q04912; -.
DR BioMuta; MST1R; -.
DR DMDM; 294862462; -.
DR EPD; Q04912; -.
DR jPOST; Q04912; -.
DR MassIVE; Q04912; -.
DR MaxQB; Q04912; -.
DR PaxDb; Q04912; -.
DR PeptideAtlas; Q04912; -.
DR PRIDE; Q04912; -.
DR ProteomicsDB; 58294; -. [Q04912-1]
DR ProteomicsDB; 58295; -. [Q04912-2]
DR ProteomicsDB; 58296; -. [Q04912-3]
DR ProteomicsDB; 58297; -. [Q04912-4]
DR ProteomicsDB; 58298; -. [Q04912-5]
DR ProteomicsDB; 58299; -. [Q04912-6]
DR ABCD; Q04912; 13 sequenced antibodies.
DR Antibodypedia; 2092; 913 antibodies from 39 providers.
DR DNASU; 4486; -.
DR Ensembl; ENST00000296474.8; ENSP00000296474.3; ENSG00000164078.14. [Q04912-1]
DR Ensembl; ENST00000344206.8; ENSP00000341325.4; ENSG00000164078.14. [Q04912-2]
DR Ensembl; ENST00000621387.4; ENSP00000482642.1; ENSG00000164078.14. [Q04912-7]
DR GeneID; 4486; -.
DR KEGG; hsa:4486; -.
DR MANE-Select; ENST00000296474.8; ENSP00000296474.3; NM_002447.4; NP_002438.2.
DR UCSC; uc003cxy.5; human. [Q04912-1]
DR CTD; 4486; -.
DR DisGeNET; 4486; -.
DR GeneCards; MST1R; -.
DR HGNC; HGNC:7381; MST1R.
DR HPA; ENSG00000164078; Tissue enhanced (skin, stomach).
DR MalaCards; MST1R; -.
DR MIM; 600168; gene.
DR MIM; 617075; phenotype.
DR neXtProt; NX_Q04912; -.
DR OpenTargets; ENSG00000164078; -.
DR PharmGKB; PA31186; -.
DR VEuPathDB; HostDB:ENSG00000164078; -.
DR eggNOG; KOG1095; Eukaryota.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT00940000157842; -.
DR HOGENOM; CLU_005158_0_0_1; -.
DR InParanoid; Q04912; -.
DR OrthoDB; 408584at2759; -.
DR PhylomeDB; Q04912; -.
DR TreeFam; TF317402; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; Q04912; -.
DR Reactome; R-HSA-8852405; Signaling by MST1.
DR SignaLink; Q04912; -.
DR SIGNOR; Q04912; -.
DR BioGRID-ORCS; 4486; 6 hits in 1106 CRISPR screens.
DR ChiTaRS; MST1R; human.
DR GeneWiki; MST1R; -.
DR GenomeRNAi; 4486; -.
DR Pharos; Q04912; Tchem.
DR PRO; PR:Q04912; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q04912; protein.
DR Bgee; ENSG00000164078; Expressed in mucosa of transverse colon and 114 other tissues.
DR ExpressionAtlas; Q04912; baseline and differential.
DR Genevisible; Q04912; HS.
DR GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0005773; C:vacuole; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0005011; F:macrophage colony-stimulating factor receptor activity; TAS:ProtInc.
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:0006952; P:defense response; TAS:ProtInc.
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:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007338; P:single fertilization; TAS:ProtInc.
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; 2.
DR PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00429; IPT; 3.
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 3D-structure; Alternative splicing; ATP-binding;
KW Cleavage on pair of basic residues; Disease variant; Disulfide bond;
KW Glycoprotein; Immunity; Innate immunity; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1400
FT /note="Macrophage-stimulating protein receptor"
FT /id="PRO_0000024452"
FT CHAIN 25..304
FT /note="Macrophage-stimulating protein receptor alpha chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024453"
FT CHAIN 310..1400
FT /note="Macrophage-stimulating protein receptor beta chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024454"
FT TOPO_DOM 25..957
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 958..978
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 979..1400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..522
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 569..671
FT /note="IPT/TIG 1"
FT DOMAIN 684..767
FT /note="IPT/TIG 2"
FT DOMAIN 770..860
FT /note="IPT/TIG 3"
FT DOMAIN 1082..1345
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1367..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1208
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:20726546"
FT BINDING 1088..1096
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 1114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 1161..1164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 1212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 1238
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:15632155,
FT ECO:0000305|PubMed:20726546"
FT MOD_RES 1239
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000305|PubMed:15632155"
FT MOD_RES 1353
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15632155"
FT MOD_RES 1360
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15632155"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22848655"
FT CARBOHYD 654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 101..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:22848655"
FT DISULFID 107..162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:22848655"
FT DISULFID 135..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:22848655"
FT DISULFID 174..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:22848655"
FT DISULFID 300..367
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:22848655"
FT DISULFID 385..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:22848655"
FT DISULFID 386..422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:22848655"
FT DISULFID 527..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:22848655"
FT DISULFID 533..567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:22848655"
FT DISULFID 536..552
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:22848655"
FT DISULFID 548..558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352,
FT ECO:0000269|PubMed:22848655"
FT VAR_SEQ 411..516
FT /note="Missing (in isoform RON-2 and isoform RON-5)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_038919"
FT VAR_SEQ 475..495
FT /note="ELVRSLNYLLYVSNFSLGDSG -> GPHPHSPLALGPCLHPHFAHI (in
FT isoform RON-1)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_038920"
FT VAR_SEQ 496..1400
FT /note="Missing (in isoform RON-1)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_038921"
FT VAR_SEQ 628..647
FT /note="PVPRKDFVEEFECELEPLGT -> YNLVPPLPFPEGGNQAAPSP (in
FT isoform RON-2 and isoform RON-4)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_038922"
FT VAR_SEQ 648..1400
FT /note="Missing (in isoform RON-2 and isoform RON-4)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_038923"
FT VAR_SEQ 884..932
FT /note="Missing (in isoform Delta-RON)"
FT /evidence="ECO:0000305"
FT /id="VSP_005007"
FT VAR_SEQ 884..907
FT /note="YIGLGAVADCVGINVTVGGESCQH -> VSVRDRGRDSWGSESRGQPTGWSS
FT (in isoform RON-3)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_038924"
FT VAR_SEQ 908..1400
FT /note="Missing (in isoform RON-3)"
FT /evidence="ECO:0000303|PubMed:18593464"
FT /id="VSP_038925"
FT VARIANT 75
FT /note="R -> S (in dbSNP:rs35887539)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041768"
FT VARIANT 95
FT /note="P -> T (in dbSNP:rs55908300)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041769"
FT VARIANT 185
FT /note="R -> C (in dbSNP:rs55633379)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041770"
FT VARIANT 306
FT /note="R -> H (in NPCA3; dbSNP:rs200046052)"
FT /evidence="ECO:0000269|PubMed:26951679"
FT /id="VAR_076928"
FT VARIANT 322
FT /note="R -> Q (in dbSNP:rs2230593)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:8386824"
FT /id="VAR_006350"
FT VARIANT 327
FT /note="A -> T (in NPCA3; unknown pathological significance;
FT dbSNP:rs200757776)"
FT /evidence="ECO:0000269|PubMed:26951679"
FT /id="VAR_076929"
FT VARIANT 356
FT /note="G -> D (in dbSNP:rs35924402)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041771"
FT VARIANT 434
FT /note="S -> L (in dbSNP:rs2230591)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_029238"
FT VARIANT 440
FT /note="N -> S (in dbSNP:rs2230592)"
FT /id="VAR_029239"
FT VARIANT 465
FT /note="G -> D (in dbSNP:rs34564898)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041772"
FT VARIANT 504
FT /note="R -> C (in dbSNP:rs34350470)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041773"
FT VARIANT 523
FT /note="Q -> R (in dbSNP:rs2230590)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:8386824"
FT /id="VAR_041774"
FT VARIANT 613
FT /note="Q -> P (in dbSNP:rs35986685)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041775"
FT VARIANT 670
FT /note="V -> G (in NPCA3; unknown pathological significance;
FT dbSNP:rs201024956)"
FT /evidence="ECO:0000269|PubMed:26951679"
FT /id="VAR_076930"
FT VARIANT 900
FT /note="V -> M (in dbSNP:rs56091918)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041776"
FT VARIANT 973
FT /note="A -> T (in NPCA3; unknown pathological significance;
FT dbSNP:rs773053723)"
FT /evidence="ECO:0000269|PubMed:26951679"
FT /id="VAR_076931"
FT VARIANT 1195
FT /note="G -> S (in dbSNP:rs7433231)"
FT /id="VAR_061749"
FT VARIANT 1304
FT /note="R -> G (in dbSNP:rs528985327)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041777"
FT VARIANT 1335
FT /note="R -> G (in dbSNP:rs1062633)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_024577"
FT VARIANT 1360
FT /note="Y -> C (in dbSNP:rs56330223)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041778"
FT CONFLICT 209
FT /note="A -> G (in Ref. 1; CAA49634)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="R -> RQ (in Ref. 3; ACF47620)"
FT /evidence="ECO:0000305"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4QT8"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:4FWW"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:4FWW"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4QT8"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:4FWW"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4FWW"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 275..288
FT /evidence="ECO:0007829|PDB:4FWW"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 294..302
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 320..328
FT /evidence="ECO:0007829|PDB:4FWW"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 344..351
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:4FWW"
FT HELIX 371..386
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:4FWW"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:4QT8"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:4FWW"
FT TURN 438..445
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 485..491
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:4FWW"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:4FWW"
FT HELIX 533..538
FT /evidence="ECO:0007829|PDB:4FWW"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 549..553
FT /evidence="ECO:0007829|PDB:4FWW"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:4FWW"
FT TURN 559..561
FT /evidence="ECO:0007829|PDB:4FWW"
FT STRAND 563..567
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 570..575
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 589..593
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 609..615
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 653..659
FT /evidence="ECO:0007829|PDB:4QT8"
FT STRAND 672..682
FT /evidence="ECO:0007829|PDB:4QT8"
FT HELIX 1064..1069
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1071..1073
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1077..1079
FT /evidence="ECO:0007829|PDB:3PLS"
FT STRAND 1080..1091
FT /evidence="ECO:0007829|PDB:3PLS"
FT STRAND 1094..1102
FT /evidence="ECO:0007829|PDB:3PLS"
FT STRAND 1104..1106
FT /evidence="ECO:0007829|PDB:3PLS"
FT STRAND 1108..1116
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1122..1136
FT /evidence="ECO:0007829|PDB:3PLS"
FT STRAND 1148..1150
FT /evidence="ECO:0007829|PDB:3PLS"
FT STRAND 1153..1155
FT /evidence="ECO:0007829|PDB:3PLS"
FT STRAND 1158..1161
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1169..1174
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1182..1201
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1211..1213
FT /evidence="ECO:0007829|PDB:3PLS"
FT STRAND 1214..1216
FT /evidence="ECO:0007829|PDB:3PLS"
FT STRAND 1222..1224
FT /evidence="ECO:0007829|PDB:3PLS"
FT TURN 1232..1235
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1236..1239
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1250..1253
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1256..1259
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1266..1282
FT /evidence="ECO:0007829|PDB:3PLS"
FT TURN 1287..1290
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1293..1295
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1296..1301
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1314..1323
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1328..1330
FT /evidence="ECO:0007829|PDB:3PLS"
FT HELIX 1334..1347
FT /evidence="ECO:0007829|PDB:3PLS"
SQ SEQUENCE 1400 AA; 152241 MW; 358672D466B8E70D CRC64;
MELLPPLPQS FLLLLLLPAK PAAGEDWQCP RTPYAASRDF DVKYVVPSFS AGGLVQAMVT
YEGDRNESAV FVAIRNRLHV LGPDLKSVQS LATGPAGDPG CQTCAACGPG PHGPPGDTDT
KVLVLDPALP ALVSCGSSLQ GRCFLHDLEP QGTAVHLAAP ACLFSAHHNR PDDCPDCVAS
PLGTRVTVVE QGQASYFYVA SSLDAAVAAS FSPRSVSIRR LKADASGFAP GFVALSVLPK
HLVSYSIEYV HSFHTGAFVY FLTVQPASVT DDPSALHTRL ARLSATEPEL GDYRELVLDC
RFAPKRRRRG APEGGQPYPV LRVAHSAPVG AQLATELSIA EGQEVLFGVF VTGKDGGPGV
GPNSVVCAFP IDLLDTLIDE GVERCCESPV HPGLRRGLDF FQSPSFCPNP PGLEALSPNT
SCRHFPLLVS SSFSRVDLFN GLLGPVQVTA LYVTRLDNVT VAHMGTMDGR ILQVELVRSL
NYLLYVSNFS LGDSGQPVQR DVSRLGDHLL FASGDQVFQV PIQGPGCRHF LTCGRCLRAW
HFMGCGWCGN MCGQQKECPG SWQQDHCPPK LTEFHPHSGP LRGSTRLTLC GSNFYLHPSG
LVPEGTHQVT VGQSPCRPLP KDSSKLRPVP RKDFVEEFEC ELEPLGTQAV GPTNVSLTVT
NMPPGKHFRV DGTSVLRGFS FMEPVLIAVQ PLFGPRAGGT CLTLEGQSLS VGTSRAVLVN
GTECLLARVS EGQLLCATPP GATVASVPLS LQVGGAQVPG SWTFQYREDP VVLSISPNCG
YINSHITICG QHLTSAWHLV LSFHDGLRAV ESRCERQLPE QQLCRLPEYV VRDPQGWVAG
NLSARGDGAA GFTLPGFRFL PPPHPPSANL VPLKPEEHAI KFEYIGLGAV ADCVGINVTV
GGESCQHEFR GDMVVCPLPP SLQLGQDGAP LQVCVDGECH ILGRVVRPGP DGVPQSTLLG
ILLPLLLLVA ALATALVFSY WWRRKQLVLP PNLNDLASLD QTAGATPLPI LYSGSDYRSG
LALPAIDGLD STTCVHGASF SDSEDESCVP LLRKESIQLR DLDSALLAEV KDVLIPHERV
VTHSDRVIGK GHFGVVYHGE YIDQAQNRIQ CAIKSLSRIT EMQQVEAFLR EGLLMRGLNH
PNVLALIGIM LPPEGLPHVL LPYMCHGDLL QFIRSPQRNP TVKDLISFGL QVARGMEYLA
EQKFVHRDLA ARNCMLDESF TVKVADFGLA RDILDREYYS VQQHRHARLP VKWMALESLQ
TYRFTTKSDV WSFGVLLWEL LTRGAPPYRH IDPFDLTHFL AQGRRLPQPE YCPDSLYQVM
QQCWEADPAV RPTFRVLVGE VEQIVSALLG DHYVQLPATY MNLGPSTSHE MNVRPEQPQF
SPMPGNVRRP RPLSEPPRPT
