7SX9

T-Plastin-F-actin complex, anti-parallel bundled state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001725	cellular_component	stress fiber
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0005865	cellular_component	striated muscle thin filament
A	0005884	cellular_component	actin filament
A	0016787	molecular_function	hydrolase activity
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0048741	biological_process	skeletal muscle fiber 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	0003779	molecular_function	actin binding
D	0005509	molecular_function	calcium ion binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005884	cellular_component	actin filament
D	0005886	cellular_component	plasma membrane
D	0032432	cellular_component	actin filament bundle
D	0046872	molecular_function	metal ion binding
D	0051015	molecular_function	actin filament binding
D	0051017	biological_process	actin filament bundle assembly
D	0051639	biological_process	actin filament network formation
D	0060348	biological_process	bone development
E	0001725	cellular_component	stress fiber
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005737	cellular_component	cytoplasm
E	0005856	cellular_component	cytoskeleton
E	0005865	cellular_component	striated muscle thin filament
E	0005884	cellular_component	actin filament
E	0016787	molecular_function	hydrolase activity
E	0030240	biological_process	skeletal muscle thin filament assembly
E	0048741	biological_process	skeletal muscle fiber development
G	0001725	cellular_component	stress fiber
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005856	cellular_component	cytoskeleton
G	0005865	cellular_component	striated muscle thin filament
G	0005884	cellular_component	actin filament
G	0016787	molecular_function	hydrolase activity
G	0030240	biological_process	skeletal muscle thin filament assembly
G	0048741	biological_process	skeletal muscle fiber development
H	0001725	cellular_component	stress fiber
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0005856	cellular_component	cytoskeleton
H	0005865	cellular_component	striated muscle thin filament
H	0005884	cellular_component	actin filament
H	0016787	molecular_function	hydrolase activity
H	0030240	biological_process	skeletal muscle thin filament assembly
H	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
D	ASP25-LEU37
D	ASP65-PHE77

---

site_id	PS00019
Number of Residues	10
Details	ACTININ_1 Actinin-type actin-binding domain signature 1. EKyAFVNWIN

Chain	Residue	Details
D	GLU125-ASN134
D	GLU399-ASN408

---

site_id	PS00020
Number of Residues	25
Details	ACTININ_2 Actinin-type actin-binding domain signature 2. VvNIGAeDLrAgkphLvLGLLWqII

Chain	Residue	Details
D	VAL211-ILE235
D	LEU478-MET502

---

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
B	TYR53-GLY63

---

site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WITKqEYDE

Chain	Residue	Details
B	TRP356-GLU364

---

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR

Chain	Residue	Details
B	LEU104-ARG116

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448

Chain	Residue	Details
D	ASP25
D	ASN27
D	ASN29
D	GLU36
D	ASP65
D	ASN67
D	ASP69
D	LYS71
D	GLU76

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99K51

Chain	Residue	Details
D	SER268
A	ASP1
C	ASP1
G	ASP1
E	ASP1
H	ASP1

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
D	SER293
E	MET47
H	MET44
H	MET47
B	MET47
A	MET44
A	MET47
C	MET44
C	MET47
G	MET44
G	MET47
E	MET44

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
D	SER326
A	HIC73
C	HIC73
G	HIC73
E	HIC73
H	HIC73

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
D	SER339
A	LYS84
C	LYS84
G	LYS84
E	LYS84
H	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
D	THR391

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