7SXA
T-Plastin-F-actin complex, pre-bundling intermediate state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003779 | molecular_function | actin binding |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005884 | cellular_component | actin filament |
A | 0005886 | cellular_component | plasma membrane |
A | 0032432 | cellular_component | actin filament bundle |
A | 0046872 | molecular_function | metal ion binding |
A | 0051015 | molecular_function | actin filament binding |
A | 0051017 | biological_process | actin filament bundle assembly |
A | 0051639 | biological_process | actin filament network formation |
A | 0060348 | biological_process | bone development |
B | 0001725 | cellular_component | stress fiber |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005856 | cellular_component | cytoskeleton |
B | 0005865 | cellular_component | striated muscle thin filament |
B | 0005884 | cellular_component | actin filament |
B | 0016787 | molecular_function | hydrolase activity |
B | 0030240 | biological_process | skeletal muscle thin filament assembly |
B | 0048741 | biological_process | skeletal muscle fiber development |
C | 0001725 | cellular_component | stress fiber |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005856 | cellular_component | cytoskeleton |
C | 0005865 | cellular_component | striated muscle thin filament |
C | 0005884 | cellular_component | actin filament |
C | 0016787 | molecular_function | hydrolase activity |
C | 0030240 | biological_process | skeletal muscle thin filament assembly |
C | 0048741 | biological_process | skeletal muscle fiber development |
D | 0001725 | cellular_component | stress fiber |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005856 | cellular_component | cytoskeleton |
D | 0005865 | cellular_component | striated muscle thin filament |
D | 0005884 | cellular_component | actin filament |
D | 0016787 | molecular_function | hydrolase activity |
D | 0030240 | biological_process | skeletal muscle thin filament assembly |
D | 0048741 | biological_process | skeletal muscle fiber development |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DLNSNGFICdyEL |
Chain | Residue | Details |
A | ASP25-LEU37 | |
A | ASP65-PHE77 |
site_id | PS00019 |
Number of Residues | 10 |
Details | ACTININ_1 Actinin-type actin-binding domain signature 1. EKyAFVNWIN |
Chain | Residue | Details |
A | GLU125-ASN134 | |
A | GLU399-ASN408 |
site_id | PS00020 |
Number of Residues | 25 |
Details | ACTININ_2 Actinin-type actin-binding domain signature 2. VvNIGAeDLrAgkphLvLGLLWqII |
Chain | Residue | Details |
A | VAL211-ILE235 | |
A | LEU478-MET502 |
site_id | PS00406 |
Number of Residues | 11 |
Details | ACTINS_1 Actins signature 1. YVGDEAQs.KRG |
Chain | Residue | Details |
C | TYR53-GLY63 |
site_id | PS00432 |
Number of Residues | 9 |
Details | ACTINS_2 Actins signature 2. WITKqEYDE |
Chain | Residue | Details |
C | TRP356-GLU364 |
site_id | PS01132 |
Number of Residues | 13 |
Details | ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR |
Chain | Residue | Details |
C | LEU104-ARG116 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | MOD_RES: N-acetylcysteine; in intermediate form => ECO:0000250|UniProtKB:P62737 |
Chain | Residue | Details |
C | CYS0 | |
B | CYS0 | |
D | CYS0 | |
A | GLU36 | |
A | ASP65 | |
A | ASN67 | |
A | ASP69 | |
A | LYS71 | |
A | GLU76 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269|PubMed:456601 |
Chain | Residue | Details |
C | ASP1 | |
B | ASP1 | |
D | ASP1 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: Methionine (R)-sulfoxide => ECO:0000250|UniProtKB:P68134 |
Chain | Residue | Details |
C | MET44 | |
C | MET47 | |
B | MET44 | |
B | MET47 | |
D | MET44 | |
D | MET47 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: Tele-methylhistidine => ECO:0000269|PubMed:12356759, ECO:0007744|PDB:1MDU |
Chain | Residue | Details |
C | HIC73 | |
B | HIC73 | |
D | HIC73 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | MOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68133 |
Chain | Residue | Details |
C | LYS84 | |
B | LYS84 | |
D | LYS84 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | THR391 |