##gff-version 3
Q9R0S2	UniProtKB	Signal peptide	1	41	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0S2	UniProtKB	Propeptide	42	128	.	.	.	ID=PRO_0000028848;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0S2	UniProtKB	Chain	129	618	.	.	.	ID=PRO_0000028849;Note=Matrix metalloproteinase-24	
Q9R0S2	UniProtKB	Chain	129	554	.	.	.	ID=PRO_0000302759;Note=Processed matrix metalloproteinase-24;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R0S2	UniProtKB	Topological domain	42	575	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0S2	UniProtKB	Transmembrane	576	596	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0S2	UniProtKB	Topological domain	597	618	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9R0S2	UniProtKB	Repeat	350	398	.	.	.	Note=Hemopexin 1	
Q9R0S2	UniProtKB	Repeat	399	444	.	.	.	Note=Hemopexin 2	
Q9R0S2	UniProtKB	Repeat	446	494	.	.	.	Note=Hemopexin 3	
Q9R0S2	UniProtKB	Repeat	495	542	.	.	.	Note=Hemopexin 4	
Q9R0S2	UniProtKB	Region	296	352	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9R0S2	UniProtKB	Motif	110	117	.	.	.	Note=Cysteine switch;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0S2	UniProtKB	Motif	616	618	.	.	.	Note=PDZ-binding	
Q9R0S2	UniProtKB	Compositional bias	320	337	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9R0S2	UniProtKB	Active site	256	256	.	.	.	Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10095,ECO:0000269|PubMed:10085137;Dbxref=PMID:10085137	
Q9R0S2	UniProtKB	Binding site	112	112	.	.	.	Note=In inhibited form;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0S2	UniProtKB	Binding site	255	255	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
Q9R0S2	UniProtKB	Binding site	259	259	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
Q9R0S2	UniProtKB	Binding site	265	265	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10095	
Q9R0S2	UniProtKB	Site	554	555	.	.	.	Note=Cleavage%3B by furin	
Q9R0S2	UniProtKB	Disulfide bond	353	542	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9R0S2	UniProtKB	Mutagenesis	256	256	.	.	.	Note=Loss of function. Does not prevent proteolytic processing. E->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10085137,ECO:0000269|PubMed:11470782;Dbxref=PMID:10085137,PMID:11470782	
Q9R0S2	UniProtKB	Mutagenesis	549	554	.	.	.	Note=Abolishes proteolytic processing. Gain of function mutant. Missing	
Q9R0S2	UniProtKB	Mutagenesis	616	618	.	.	.	Note=Impaired recycling affecting its internalization%2C leading to decreased activity on the plasma surface. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14990567;Dbxref=PMID:14990567	
Q9R0S2	UniProtKB	Sequence conflict	7	28	.	.	.	Note=GRAAPGQASRWSGWRAPGRLLP->AALRRARPRAGALAGPGAAA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R0S2	UniProtKB	Sequence conflict	44	50	.	.	.	Note=KPAGADA->SRPGR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R0S2	UniProtKB	Sequence conflict	46	46	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R0S2	UniProtKB	Sequence conflict	306	308	.	.	.	Note=LEP->SGA;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R0S2	UniProtKB	Sequence conflict	326	326	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R0S2	UniProtKB	Sequence conflict	337	341	.	.	.	Note=PPLGD->RPWG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R0S2	UniProtKB	Sequence conflict	449	449	.	.	.	Note=I->KP;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R0S2	UniProtKB	Sequence conflict	502	502	.	.	.	Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9R0S2	UniProtKB	Sequence conflict	589	589	.	.	.	Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305