##gff-version 3
P30680	UniProtKB	Chain	1	369	.	.	.	ID=PRO_0000070123;Note=Somatostatin receptor type 2	
P30680	UniProtKB	Topological domain	1	43	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Transmembrane	44	67	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Topological domain	68	78	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Transmembrane	79	103	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Topological domain	104	118	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Transmembrane	119	138	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Topological domain	139	161	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Transmembrane	162	181	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Topological domain	182	207	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Transmembrane	208	229	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Topological domain	230	253	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Transmembrane	254	278	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Topological domain	279	288	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Transmembrane	289	303	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Topological domain	304	369	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Modified residue	341	341	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19389921;Dbxref=PMID:19389921	
P30680	UniProtKB	Modified residue	343	343	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19389921;Dbxref=PMID:19389921	
P30680	UniProtKB	Modified residue	348	348	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19389921;Dbxref=PMID:19389921	
P30680	UniProtKB	Modified residue	353	353	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19389921;Dbxref=PMID:19389921	
P30680	UniProtKB	Modified residue	354	354	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19389921;Dbxref=PMID:19389921	
P30680	UniProtKB	Lipidation	328	328	.	.	.	Note=S-palmitoyl cysteine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Glycosylation	9	9	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Glycosylation	22	22	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Glycosylation	29	29	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Glycosylation	32	32	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P30680	UniProtKB	Disulfide bond	115	193	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00521	
P30680	UniProtKB	Alternative sequence	332	369	.	.	.	ID=VSP_001924;Note=In isoform B. VSGAEDGERSDSKQDKSRLNETTETQRTLLNGDLQTSI->ADNSKTGEEDTMAWV;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P30680	UniProtKB	Beta strand	365	368	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6EXJ