##gff-version 3
Q7TPR4	UniProtKB	Chain	1	892	.	.	.	ID=PRO_0000073432;Note=Alpha-actinin-1	
Q7TPR4	UniProtKB	Domain	31	135	.	.	.	Note=Calponin-homology (CH) 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044	
Q7TPR4	UniProtKB	Domain	144	250	.	.	.	Note=Calponin-homology (CH) 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044	
Q7TPR4	UniProtKB	Repeat	274	384	.	.	.	Note=Spectrin 1	
Q7TPR4	UniProtKB	Repeat	394	499	.	.	.	Note=Spectrin 2	
Q7TPR4	UniProtKB	Repeat	509	620	.	.	.	Note=Spectrin 3	
Q7TPR4	UniProtKB	Repeat	630	733	.	.	.	Note=Spectrin 4	
Q7TPR4	UniProtKB	Domain	746	781	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
Q7TPR4	UniProtKB	Domain	787	822	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
Q7TPR4	UniProtKB	Region	1	247	.	.	.	Note=Actin-binding	
Q7TPR4	UniProtKB	Region	274	733	.	.	.	Note=Interaction with DDN;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q7TPR4	UniProtKB	Binding site	759	759	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
Q7TPR4	UniProtKB	Binding site	761	761	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
Q7TPR4	UniProtKB	Binding site	763	763	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
Q7TPR4	UniProtKB	Binding site	765	765	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
Q7TPR4	UniProtKB	Binding site	770	770	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
Q7TPR4	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12814	
Q7TPR4	UniProtKB	Modified residue	6	6	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12814	
Q7TPR4	UniProtKB	Modified residue	12	12	.	.	.	Note=Phosphotyrosine%3B by FAK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12814	
Q7TPR4	UniProtKB	Modified residue	95	95	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12814	
Q7TPR4	UniProtKB	Modified residue	195	195	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12814	
Q7TPR4	UniProtKB	Modified residue	471	471	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12814	
Q7TPR4	UniProtKB	Modified residue	676	676	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12814	
Q7TPR4	UniProtKB	Modified residue	677	677	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P12814	
Q7TPR4	UniProtKB	Modified residue	890	890	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z1P2	
Q7TPR4	UniProtKB	Mutagenesis	32	32	.	.	.	Note=Shows less organization of the circumferential actin-filament network compared to controls. Q->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23434115;Dbxref=PMID:23434115	
Q7TPR4	UniProtKB	Mutagenesis	105	105	.	.	.	Note=Shows less organization of the circumferential actin-filament network compared to controls. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23434115;Dbxref=PMID:23434115	
Q7TPR4	UniProtKB	Helix	826	837	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C0A	
Q7TPR4	UniProtKB	Beta strand	841	844	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C0A	
Q7TPR4	UniProtKB	Helix	845	851	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C0A	
Q7TPR4	UniProtKB	Helix	854	863	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C0A	
Q7TPR4	UniProtKB	Beta strand	869	871	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C0A	
Q7TPR4	UniProtKB	Beta strand	876	879	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C0A	
Q7TPR4	UniProtKB	Helix	880	887	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6C0A