##gff-version 3
P27798	UniProtKB	Signal peptide	1	15	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P27798	UniProtKB	Chain	16	395	.	.	.	ID=PRO_0000004180;Note=Calreticulin	
P27798	UniProtKB	Repeat	186	197	.	.	.	Note=1-1	
P27798	UniProtKB	Repeat	205	216	.	.	.	Note=1-2	
P27798	UniProtKB	Repeat	222	233	.	.	.	Note=1-3	
P27798	UniProtKB	Repeat	239	250	.	.	.	Note=1-4	
P27798	UniProtKB	Repeat	254	264	.	.	.	Note=2-1	
P27798	UniProtKB	Repeat	268	278	.	.	.	Note=2-2	
P27798	UniProtKB	Repeat	282	292	.	.	.	Note=2-3	
P27798	UniProtKB	Region	186	250	.	.	.	Note=4 X approximate repeats	
P27798	UniProtKB	Region	193	301	.	.	.	Note=P-domain	
P27798	UniProtKB	Region	202	255	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P27798	UniProtKB	Region	254	292	.	.	.	Note=3 X approximate repeats	
P27798	UniProtKB	Region	302	395	.	.	.	Note=C-domain	
P27798	UniProtKB	Region	340	395	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P27798	UniProtKB	Motif	392	395	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138	
P27798	UniProtKB	Compositional bias	202	216	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P27798	UniProtKB	Compositional bias	224	249	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P27798	UniProtKB	Compositional bias	340	377	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P27798	UniProtKB	Compositional bias	378	395	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P27798	UniProtKB	Binding site	105	105	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14211	
P27798	UniProtKB	Binding site	107	107	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14211	
P27798	UniProtKB	Binding site	124	124	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14211	
P27798	UniProtKB	Binding site	131	131	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14211	
P27798	UniProtKB	Binding site	312	312	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14211	
P27798	UniProtKB	Disulfide bond	101	133	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P27798	UniProtKB	Mutagenesis	28	395	.	.	.	Note=In bz29%3B extended lifespan. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32905769;Dbxref=PMID:32905769	
P27798	UniProtKB	Mutagenesis	182	182	.	.	.	Note=Partial reduction in ced-3-mediated cleavage%3B when associated with E-225 and E-253. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17371877;Dbxref=PMID:17371877	
P27798	UniProtKB	Mutagenesis	225	225	.	.	.	Note=Partial reduction in ced-3-mediated cleavage%3B when associated with E-182 and E-253. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17371877;Dbxref=PMID:17371877	
P27798	UniProtKB	Mutagenesis	253	253	.	.	.	Note=Partial reduction in ced-3-mediated cleavage%3B when associated with E-182 and E-225. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17371877;Dbxref=PMID:17371877