##gff-version 3
P97708	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P97708	UniProtKB	Chain	23	351	.	.	.	ID=PRO_0000041721;Note=Zona pellucida sperm-binding protein 3	
P97708	UniProtKB	Propeptide	352	424	.	.	.	ID=PRO_0000041722;Note=Removed in mature form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16342937;Dbxref=PMID:16342937	
P97708	UniProtKB	Topological domain	23	387	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P97708	UniProtKB	Transmembrane	388	408	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P97708	UniProtKB	Topological domain	409	424	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P97708	UniProtKB	Domain	45	308	.	.	.	Note=ZP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00375	
P97708	UniProtKB	Modified residue	23	23	.	.	.	Note=Pyrrolidone carboxylic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16342937;Dbxref=PMID:16342937	
P97708	UniProtKB	Glycosylation	32	32	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P97708	UniProtKB	Glycosylation	34	34	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P97708	UniProtKB	Glycosylation	39	39	.	.	.	Note=O-linked (GalNAc...) serine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P97708	UniProtKB	Glycosylation	146	146	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16342937;Dbxref=PMID:16342937	
P97708	UniProtKB	Glycosylation	155	155	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P97708	UniProtKB	Glycosylation	162	162	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P97708	UniProtKB	Glycosylation	273	273	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16342937;Dbxref=PMID:16342937	
P97708	UniProtKB	Glycosylation	304	304	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16342937;Dbxref=PMID:16342937	
P97708	UniProtKB	Glycosylation	327	327	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P97708	UniProtKB	Glycosylation	330	330	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16342937;Dbxref=PMID:16342937	
P97708	UniProtKB	Disulfide bond	46	139	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P97708	UniProtKB	Disulfide bond	78	98	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16342937;Dbxref=PMID:16342937	
P97708	UniProtKB	Disulfide bond	216	283	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16342937;Dbxref=PMID:16342937	
P97708	UniProtKB	Disulfide bond	240	301	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16342937;Dbxref=PMID:16342937	
P97708	UniProtKB	Sequence conflict	55	55	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P97708	UniProtKB	Sequence conflict	112	112	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P97708	UniProtKB	Sequence conflict	412	412	.	.	.	Note=K->M;Ontology_term=ECO:0000305;evidence=ECO:0000305