##gff-version 3
Q9JM58	UniProtKB	Signal peptide	1	33	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JM58	UniProtKB	Chain	34	425	.	.	.	ID=PRO_0000011040;Note=Cytokine receptor-like factor 1	
Q9JM58	UniProtKB	Domain	35	134	.	.	.	Note=Ig-like C2-type	
Q9JM58	UniProtKB	Domain	140	235	.	.	.	Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316	
Q9JM58	UniProtKB	Domain	240	344	.	.	.	Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316	
Q9JM58	UniProtKB	Region	335	366	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9JM58	UniProtKB	Region	402	425	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9JM58	UniProtKB	Motif	330	334	.	.	.	Note=WSXWS motif	
Q9JM58	UniProtKB	Modified residue	222	222	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15378723;Dbxref=PMID:15378723	
Q9JM58	UniProtKB	Glycosylation	95	95	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JM58	UniProtKB	Glycosylation	107	107	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JM58	UniProtKB	Glycosylation	143	143	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JM58	UniProtKB	Glycosylation	171	171	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JM58	UniProtKB	Glycosylation	295	295	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JM58	UniProtKB	Glycosylation	385	385	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9JM58	UniProtKB	Disulfide bond	146	156	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9JM58	UniProtKB	Disulfide bond	187	198	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250