##gff-version 3
Q9NTN9	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NTN9	UniProtKB	Chain	18	838	.	.	.	ID=PRO_0000032333;Note=Semaphorin-4G	
Q9NTN9	UniProtKB	Topological domain	18	675	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NTN9	UniProtKB	Transmembrane	676	696	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NTN9	UniProtKB	Topological domain	697	838	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NTN9	UniProtKB	Domain	35	505	.	.	.	Note=Sema;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00352	
Q9NTN9	UniProtKB	Domain	507	558	.	.	.	Note=PSI	
Q9NTN9	UniProtKB	Domain	567	649	.	.	.	Note=Ig-like C2-type	
Q9NTN9	UniProtKB	Region	723	777	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9NTN9	UniProtKB	Compositional bias	760	777	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9NTN9	UniProtKB	Modified residue	795	795	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q9NTN9	UniProtKB	Modified residue	837	837	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WUH7	
Q9NTN9	UniProtKB	Glycosylation	55	55	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NTN9	UniProtKB	Glycosylation	111	111	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NTN9	UniProtKB	Glycosylation	126	126	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NTN9	UniProtKB	Glycosylation	388	388	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NTN9	UniProtKB	Glycosylation	542	542	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NTN9	UniProtKB	Glycosylation	598	598	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9NTN9	UniProtKB	Disulfide bond	104	115	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9NTN9	UniProtKB	Disulfide bond	133	142	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9NTN9	UniProtKB	Disulfide bond	270	377	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9NTN9	UniProtKB	Disulfide bond	294	337	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9NTN9	UniProtKB	Disulfide bond	508	525	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9NTN9	UniProtKB	Disulfide bond	517	534	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9NTN9	UniProtKB	Disulfide bond	584	632	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9NTN9	UniProtKB	Alternative sequence	543	543	.	.	.	ID=VSP_035067;Note=In isoform 2 and isoform 3. R->RSQGSR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334	
Q9NTN9	UniProtKB	Alternative sequence	565	838	.	.	.	ID=VSP_043883;Note=In isoform 3. PPPPLKTRSVLRGDDVLLPCDQPSNLARALWLLNGSMGLSDGQGGYRVGVDGLLVTDAQPEHSGNYGCYAEENGLRTLLASYSLTVRPATPAPAPKAPATPGAQLAPDVRLLYVLAIAALGGLCLILASSLLYVACLREGRRGRRRKYSLGRASRAGGSAVQLQTVSGQCPGEEDEGDDEGAGGLEGSCLQIIPGEGAPAPPPPPPPPPPAELTNGLVALPSRLRRMNGNSYVLLRQSNNGVPAGPCSFAEELSRILEKRKHTQLVEQLDESSV->RALQVHMGSMSPPSAWPCVLDGPETRQDLCQPPKPCVHSHAHMEECLSAGLQCPHPHLLLVHSCFIPASGLGVPSQLPHPIWSSSPAPCGDLFVKSLGTGQPGEVRLHHSPPLPSCVALVNQPPHSPWSFSRV;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334