##gff-version 3
Q10656	UniProtKB	Signal peptide	1	19	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Chain	20	1040	.	.	.	ID=PRO_0000016796;Note=Myoblast growth factor receptor egl-15	
Q10656	UniProtKB	Topological domain	20	525	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Transmembrane	526	549	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Topological domain	550	1040	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Domain	33	125	.	.	.	Note=Ig-like C2-type 1	
Q10656	UniProtKB	Domain	287	383	.	.	.	Note=Ig-like C2-type 2	
Q10656	UniProtKB	Domain	391	501	.	.	.	Note=Ig-like C2-type 3	
Q10656	UniProtKB	Domain	640	931	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q10656	UniProtKB	Region	234	267	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q10656	UniProtKB	Region	952	984	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q10656	UniProtKB	Region	1021	1040	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q10656	UniProtKB	Compositional bias	234	253	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q10656	UniProtKB	Active site	797	797	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10028	
Q10656	UniProtKB	Binding site	646	654	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q10656	UniProtKB	Binding site	672	672	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q10656	UniProtKB	Modified residue	828	828	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q10656	UniProtKB	Glycosylation	121	121	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Glycosylation	280	280	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Glycosylation	299	299	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Glycosylation	401	401	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Glycosylation	407	407	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Glycosylation	433	433	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Glycosylation	440	440	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Glycosylation	449	449	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Glycosylation	474	474	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Glycosylation	497	497	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q10656	UniProtKB	Disulfide bond	55	109	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q10656	UniProtKB	Disulfide bond	314	367	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q10656	UniProtKB	Disulfide bond	414	485	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00114	
Q10656	UniProtKB	Alternative sequence	129	245	.	.	.	ID=VSP_019861;Note=In isoform b. FCDYFLFPDIHHLNIPMECVCLWKYNKEAKRSDVNYAAVTGEVCSKYASRMINRARKPLPMIPCFGDHCKEFDTTPVSDFGLPGKPEDDPLVKRVVLKKDDVIVPVHDSEESPSESR->PLKLFDWLTEHRVFDISHLLPKLLPPAEMRRVKSQLGGWEKMNNEQKIVRARHILRLRQINHALG;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12835392;Dbxref=PMID:12835392	
Q10656	UniProtKB	Alternative sequence	829	829	.	.	.	ID=VSP_002991;Note=In isoform c%2C isoform d and isoform e. R->RL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12835392;Dbxref=PMID:12835392	
Q10656	UniProtKB	Alternative sequence	984	984	.	.	.	ID=VSP_002992;Note=In isoform c%2C isoform d and isoform e. E->EVDQN;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12835392;Dbxref=PMID:12835392	
Q10656	UniProtKB	Alternative sequence	1027	1040	.	.	.	ID=VSP_002994;Note=In isoform c. RIPSNNNSMSKPEF->LYIHKVLNEPIGNGYVRQDKLARAVSGVANQSLDSALGSPAWPSYDRPSNKASCLDQTHQYYNTTSKIQYLHFTFDDPDCMTRSRDSAIFEESYHPNYIQSHPLYSKIIIKKNMTPRNPLPTKETIV;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12835392;Dbxref=PMID:12835392	
Q10656	UniProtKB	Alternative sequence	1027	1040	.	.	.	ID=VSP_019862;Note=In isoform d. RIPSNNNSMSKPEF->LYIHKVLNEPIGNGYVRQDKLARAVSGVANQSLDSALGSPAWPSYDRPSNKASCLDDEKHHYYYS;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12835392;Dbxref=PMID:12835392	
Q10656	UniProtKB	Alternative sequence	1027	1040	.	.	.	ID=VSP_019863;Note=In isoform e. RIPSNNNSMSKPEF->LYIHKVLNEPIGNGSNSPVL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12835392;Dbxref=PMID:12835392	
Q10656	UniProtKB	Mutagenesis	680	680	.	.	.	Note=In n1775%3B loss of activity. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7585964;Dbxref=PMID:7585964	
Q10656	UniProtKB	Mutagenesis	714	714	.	.	.	Note=In n1783%3B loss of activity. Ectopic membrane extension in body wall muscles. P->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16495308,ECO:0000269|PubMed:7585964;Dbxref=PMID:16495308,PMID:7585964	
Q10656	UniProtKB	Sequence conflict	551	551	.	.	.	Note=Q->G;Ontology_term=ECO:0000305;evidence=ECO:0000305