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 27-MAR-2024, entry version 228. 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 GLYCOSYLATION BY TMEM260. RX PubMed=37186866; DOI=10.1073/pnas.2302584120; RA Larsen I.S.B., Povolo L., Zhou L., Tian W., Mygind K.J., Hintze J., RA Jiang C., Hartill V., Prescott K., Johnson C.A., Mullegama S.V., RA McConkie-Rosell A., McDonald M., Hansen L., Vakhrushev S.Y., RA Schjoldager K.T., Clausen H., Worzfeld T., Joshi H.J., Halim A.; RT "The SHDRA syndrome-associated geDne TMEM260 encodes a protein-specific O- RT mannosyltransferase."; RL Proc. Natl. Acad. Sci. U.S.A. 120:e2302584120-e2302584120(2023). RN [20] 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 [21] 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 [22] 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 [23] 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 -!- PTM: O-mannosylation of IPT/TIG domains on Thr or Ser residues by CC TMEM260 is required for protein maturation (PubMed:37186866). O- CC mannosylated residues are composed of single mannose glycans that are CC not elongated or modified (PubMed:37186866). CC {ECO:0000269|PubMed:37186866}. 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="https://atlasgeneticsoncology.org/gene/287/RON"; 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; 233. DR DIP; DIP-6029N; -. DR IntAct; Q04912; 144. DR MINT; Q04912; -. DR STRING; 9606.ENSP00000296474; -. DR BindingDB; Q04912; -. DR ChEMBL; CHEMBL2689; -. DR DrugBank; DB08865; Crizotinib. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q04912; -. DR GuidetoPHARMACOLOGY; 1816; -. DR GlyCosmos; Q04912; 8 sites, No reported glycans. DR GlyGen; Q04912; 8 sites. DR iPTMnet; Q04912; -. DR PhosphoSitePlus; Q04912; -. DR SwissPalm; Q04912; -. DR BioMuta; MST1R; -. DR DMDM; 294862462; -. DR CPTAC; CPTAC-2850; -. DR CPTAC; CPTAC-2851; -. DR EPD; Q04912; -. DR jPOST; Q04912; -. DR MassIVE; Q04912; -. DR MaxQB; Q04912; -. DR PaxDb; 9606-ENSP00000296474; -. DR PeptideAtlas; 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; 1151 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 AGR; HGNC:7381; -. DR CTD; 4486; -. DR DisGeNET; 4486; -. DR GeneCards; MST1R; -. DR HGNC; HGNC:7381; MST1R. DR HPA; ENSG00000164078; Tissue enhanced (intestine, 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; 1614410at2759; -. 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; 8 hits in 1184 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 116 other cell types or tissues. DR ExpressionAtlas; Q04912; baseline and differential. DR GO; GO:0009986; C:cell surface; HDA:UniProtKB. 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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; cd00102; IPT; 1. DR CDD; cd01180; IPT_plexin_repeat1; 1. DR CDD; cd01179; IPT_plexin_repeat2; 1. DR CDD; cd05058; PTKc_Met_Ron; 1. DR CDD; cd11279; Sema_RON; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. 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; IPR002165; Plexin_repeat. 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 PANTHER; PTHR24416:SF113; MACROPHAGE-STIMULATING PROTEIN RECEPTOR; 1. DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 SMART; SM00429; IPT; 3. DR SMART; SM00423; PSI; 1. DR SMART; SM00630; Sema; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF81296; E set domains; 3. DR SUPFAM; SSF103575; Plexin repeat; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF101912; Sema domain; 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. DR Genevisible; Q04912; HS. 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; uncertain 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; uncertain 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; uncertain 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 //