##gff-version 3
O43556	UniProtKB	Chain	1	437	.	.	.	ID=PRO_0000031677;Note=Epsilon-sarcoglycan	
O43556	UniProtKB	Topological domain	1	317	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O43556	UniProtKB	Transmembrane	318	338	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O43556	UniProtKB	Topological domain	339	437	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O43556	UniProtKB	Glycosylation	200	200	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19159218;Dbxref=PMID:19159218	
O43556	UniProtKB	Alternative sequence	347	355	.	.	.	ID=VSP_045092;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15193417;Dbxref=PMID:15193417	
O43556	UniProtKB	Alternative sequence	418	418	.	.	.	ID=VSP_054079;Note=In isoform 3. Q->QWSFAPVAQAGVQWSDLGSLQPPPPR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O43556	UniProtKB	Alternative sequence	434	437	.	.	.	ID=VSP_045093;Note=In isoform 2. KWYP->DFRLTTFQRFEVNGIPEERKLTEAMNL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15193417;Dbxref=PMID:15193417	
O43556	UniProtKB	Natural variant	36	36	.	.	.	ID=VAR_066732;Note=In DYT11. T->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18175340;Dbxref=PMID:18175340	
O43556	UniProtKB	Natural variant	49	49	.	.	.	ID=VAR_058088;Note=N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs11548284,PMID:15489334	
O43556	UniProtKB	Natural variant	60	60	.	.	.	ID=VAR_066733;Note=In DYT11%3B affects protein stability%3B the mutant undergoes endoplasmic reticulum-associated degradation. H->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15079037,ECO:0000269|PubMed:21796726;Dbxref=PMID:15079037,PMID:21796726	
O43556	UniProtKB	Natural variant	60	60	.	.	.	ID=VAR_066734;Note=In DYT11%3B affects protein stability%3B the mutant undergoes endoplasmic reticulum-associated degradation. H->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15258227,ECO:0000269|PubMed:21796726;Dbxref=PMID:15258227,PMID:21796726	
O43556	UniProtKB	Natural variant	92	92	.	.	.	ID=VAR_066735;Note=In DYT11%3B results in gain-of-glycosylation%3B the mutant is targeted to the plasma membrane at reduced levels compared to wild-type. M->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16227522,ECO:0000269|PubMed:21796726;Dbxref=PMID:16227522,PMID:21796726	
O43556	UniProtKB	Natural variant	100	100	.	.	.	ID=VAR_066736;Note=In DYT11. W->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18362280;Dbxref=PMID:18362280	
O43556	UniProtKB	Natural variant	112	112	.	.	.	ID=VAR_066737;Note=In DYT11. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17853490;Dbxref=PMID:17853490	
O43556	UniProtKB	Natural variant	115	115	.	.	.	ID=VAR_066738;Note=In DYT11%3B affects protein stability%3B the mutant undergoes endoplasmic reticulum-associated degradation. Y->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16227522,ECO:0000269|PubMed:18362280,ECO:0000269|PubMed:21796726;Dbxref=PMID:16227522,PMID:18362280,PMID:21796726	
O43556	UniProtKB	Natural variant	175	175	.	.	.	ID=VAR_066739;Note=In DYT11. L->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19066193;Dbxref=PMID:19066193	
O43556	UniProtKB	Natural variant	177	177	.	.	.	ID=VAR_066740;Note=In DYT11. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19066193;Dbxref=PMID:19066193	
O43556	UniProtKB	Natural variant	184	184	.	.	.	ID=VAR_066741;Note=In DYT11%3B affects protein stability%3B the mutant undergoes endoplasmic reticulum-associated degradation. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18175340;Dbxref=dbSNP:rs1064794321,PMID:18175340	
O43556	UniProtKB	Natural variant	196	196	.	.	.	ID=VAR_026750;Note=In DYT11. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12402271;Dbxref=dbSNP:rs121908491,PMID:12402271	
O43556	UniProtKB	Natural variant	270	270	.	.	.	ID=VAR_066742;Note=In DYT11%3B affects protein stability%3B the mutant undergoes endoplasmic reticulum-associated degradation. W->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19066193,ECO:0000269|PubMed:21796726;Dbxref=PMID:19066193,PMID:21796726	
O43556	UniProtKB	Natural variant	271	271	.	.	.	ID=VAR_066743;Note=In DYT11%3B affects protein stability%3B the mutant undergoes endoplasmic reticulum-associated degradation. C->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16227522,ECO:0000269|PubMed:21796726;Dbxref=dbSNP:rs372686312,PMID:16227522,PMID:21796726	
O43556	UniProtKB	Natural variant	399	399	.	.	.	ID=VAR_058089;Note=P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs17851923,PMID:15489334	
O43556	UniProtKB	Sequence conflict	78	78	.	.	.	Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305