##gff-version 3
O95925	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
O95925	UniProtKB	Chain	22	133	.	.	.	ID=PRO_0000041378;Note=Eppin	
O95925	UniProtKB	Domain	26	73	.	.	.	Note=WAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00722	
O95925	UniProtKB	Domain	77	127	.	.	.	Note=BPTI/Kunitz inhibitor;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00031	
O95925	UniProtKB	Region	102	133	.	.	.	Note=Interaction with SEMG1	
O95925	UniProtKB	Region	117	133	.	.	.	Note=Interaction with LTF;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22699487;Dbxref=PMID:22699487	
O95925	UniProtKB	Disulfide bond	33	61	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
O95925	UniProtKB	Disulfide bond	40	65	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
O95925	UniProtKB	Disulfide bond	48	60	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
O95925	UniProtKB	Disulfide bond	54	69	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
O95925	UniProtKB	Disulfide bond	77	127	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
O95925	UniProtKB	Disulfide bond	86	110	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
O95925	UniProtKB	Disulfide bond	102	123	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
O95925	UniProtKB	Alternative sequence	1	31	.	.	.	ID=VSP_006755;Note=In isoform 2. MGSSGLLSLLVLFVLLANVQGPGLTDWLFPR->MLSKAHGCKTALSLG;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:11404006;Dbxref=PMID:11404006	
O95925	UniProtKB	Alternative sequence	131	133	.	.	.	ID=VSP_043679;Note=In isoform 3. RFP->QPCPKIKVECEVEEIDQCTKPRDCPENMKCCPFSRGKKCLDFRKASLST;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
O95925	UniProtKB	Natural variant	92	92	.	.	.	ID=VAR_024696;Note=H->R;Dbxref=dbSNP:rs2231838	
O95925	UniProtKB	Natural variant	128	128	.	.	.	ID=VAR_052950;Note=K->T;Dbxref=dbSNP:rs2231839	
O95925	UniProtKB	Mutagenesis	87	87	.	.	.	Note=Loss of effect on KLK3 activity. L->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17644992;Dbxref=PMID:17644992	
O95925	UniProtKB	Mutagenesis	102	102	.	.	.	Note=Reduces the binding to SEMG1 by 45%25. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22699487;Dbxref=PMID:22699487	
O95925	UniProtKB	Mutagenesis	107	107	.	.	.	Note=Reduces the binding to SEMG1 by 68%25. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22699487;Dbxref=PMID:22699487	
O95925	UniProtKB	Mutagenesis	110	110	.	.	.	Note=Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1%3B when associated with A-123 and A-127. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22699487;Dbxref=PMID:22699487	
O95925	UniProtKB	Mutagenesis	117	117	.	.	.	Note=Reduces the binding to SEMG1 by 68%25 and to LTF by 73%25. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22699487;Dbxref=PMID:22699487	
O95925	UniProtKB	Mutagenesis	123	123	.	.	.	Note=Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1%3B when associated with A-110 and A-127. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22699487;Dbxref=PMID:22699487	
O95925	UniProtKB	Mutagenesis	127	127	.	.	.	Note=Does not affect the binding of SEMG1 or LTF. Does not affect the binding of SEMG1%3B when associated with A-110 and A-123. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22699487;Dbxref=PMID:22699487