##gff-version 3
P10761	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12799386;Dbxref=PMID:12799386	
P10761	UniProtKB	Chain	23	351	.	.	.	ID=PRO_0000041715;Note=Zona pellucida sperm-binding protein 3	
P10761	UniProtKB	Propeptide	352	424	.	.	.	ID=PRO_0000041716;Note=Removed in mature form;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12799386;Dbxref=PMID:12799386	
P10761	UniProtKB	Topological domain	23	387	.	.	.	Note=Extracellular	
P10761	UniProtKB	Transmembrane	388	408	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P10761	UniProtKB	Topological domain	409	424	.	.	.	Note=Cytoplasmic	
P10761	UniProtKB	Domain	45	308	.	.	.	Note=ZP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00375	
P10761	UniProtKB	Modified residue	23	23	.	.	.	Note=Pyrrolidone carboxylic acid;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12799386;Dbxref=PMID:12799386	
P10761	UniProtKB	Glycosylation	32	32	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P10761	UniProtKB	Glycosylation	34	34	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P10761	UniProtKB	Glycosylation	39	39	.	.	.	Note=O-linked (GalNAc...) serine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P10761	UniProtKB	Glycosylation	146	146	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12799386;Dbxref=PMID:12799386	
P10761	UniProtKB	Glycosylation	155	155	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P10761	UniProtKB	Glycosylation	162	162	.	.	.	Note=O-linked (GalNAc...) threonine;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P10761	UniProtKB	Glycosylation	273	273	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12799386;Dbxref=PMID:12799386	
P10761	UniProtKB	Glycosylation	304	304	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12799386;Dbxref=PMID:12799386	
P10761	UniProtKB	Glycosylation	327	327	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12799386;Dbxref=PMID:12799386	
P10761	UniProtKB	Glycosylation	330	330	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12799386;Dbxref=PMID:12799386	
P10761	UniProtKB	Disulfide bond	46	139	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19052627;Dbxref=PMID:19052627	
P10761	UniProtKB	Disulfide bond	78	98	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12799386;Dbxref=PMID:12799386	
P10761	UniProtKB	Disulfide bond	216	283	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12799386;Dbxref=PMID:12799386	
P10761	UniProtKB	Disulfide bond	240	301	.	.	.	Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12799386;Dbxref=PMID:12799386	
P10761	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Reduces protein solubility and causes formation of an abnormal disulfide bond between C-111 and C-139 in approximately half of the molecules. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19052627;Dbxref=PMID:19052627	
P10761	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Causes a mild reduction of protein solubility. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19052627;Dbxref=PMID:19052627	
P10761	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Strongly reduces protein solubility. Y->L%2CV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19052627;Dbxref=PMID:19052627	
P10761	UniProtKB	Mutagenesis	111	111	.	.	.	Note=Reduces protein solubility. Y->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19052627;Dbxref=PMID:19052627	
P10761	UniProtKB	Beta strand	42	46	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5OSQ	
P10761	UniProtKB	Beta strand	48	58	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5OSQ	
P10761	UniProtKB	Beta strand	60	63	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5OSQ	
P10761	UniProtKB	Helix	68	70	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5OSQ	
P10761	UniProtKB	Beta strand	71	75	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5OSQ	
P10761	UniProtKB	Beta strand	81	84	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5OSQ	
P10761	UniProtKB	Beta strand	86	94	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5OSQ	
P10761	UniProtKB	Helix	95	98	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5OSQ	
P10761	UniProtKB	Beta strand	100	104	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5OSQ	
P10761	UniProtKB	Beta strand	106	117	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5OSQ	
P10761	UniProtKB	Beta strand	133	142	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5OSQ