Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6UPW

Metavinculin ABD-F-actin complex

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	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
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
L	0002009	biological_process	morphogenesis of an epithelium
L	0002102	cellular_component	podosome
L	0002162	molecular_function	dystroglycan binding
L	0003779	molecular_function	actin binding
L	0005198	molecular_function	structural molecule activity
L	0005515	molecular_function	protein binding
L	0005576	cellular_component	extracellular region
L	0005737	cellular_component	cytoplasm
L	0005829	cellular_component	cytosol
L	0005856	cellular_component	cytoskeleton
L	0005886	cellular_component	plasma membrane
L	0005911	cellular_component	cell-cell junction
L	0005912	cellular_component	adherens junction
L	0005916	cellular_component	fascia adherens
L	0005925	cellular_component	focal adhesion
L	0007155	biological_process	cell adhesion
L	0007160	biological_process	cell-matrix adhesion
L	0008013	molecular_function	beta-catenin binding
L	0015629	cellular_component	actin cytoskeleton
L	0016020	cellular_component	membrane
L	0030032	biological_process	lamellipodium assembly
L	0030055	cellular_component	cell-substrate junction
L	0030334	biological_process	regulation of cell migration
L	0030336	biological_process	negative regulation of cell migration
L	0031625	molecular_function	ubiquitin protein ligase binding
L	0032991	cellular_component	protein-containing complex
L	0034333	biological_process	adherens junction assembly
L	0034394	biological_process	protein localization to cell surface
L	0034774	cellular_component	secretory granule lumen
L	0035580	cellular_component	specific granule lumen
L	0035633	biological_process	maintenance of blood-brain barrier
L	0042383	cellular_component	sarcolemma
L	0042995	cellular_component	cell projection
L	0043034	cellular_component	costamere
L	0043297	biological_process	apical junction assembly
L	0044291	cellular_component	cell-cell contact zone
L	0045294	molecular_function	alpha-catenin binding
L	0045296	molecular_function	cadherin binding
L	0048675	biological_process	axon extension
L	0051015	molecular_function	actin filament binding
L	0051893	biological_process	regulation of focal adhesion assembly
L	0061826	cellular_component	podosome ring
L	0070062	cellular_component	extracellular exosome
L	0070161	cellular_component	anchoring junction
L	0070527	biological_process	platelet aggregation
L	0090136	biological_process	epithelial cell-cell adhesion
L	1903140	biological_process	regulation of establishment of endothelial barrier
L	1903561	cellular_component	extracellular vesicle
L	1904702	biological_process	regulation of protein localization to adherens junction
L	1904813	cellular_component	ficolin-1-rich granule lumen
M	0002009	biological_process	morphogenesis of an epithelium
M	0002102	cellular_component	podosome
M	0002162	molecular_function	dystroglycan binding
M	0003779	molecular_function	actin binding
M	0005198	molecular_function	structural molecule activity
M	0005515	molecular_function	protein binding
M	0005576	cellular_component	extracellular region
M	0005737	cellular_component	cytoplasm
M	0005829	cellular_component	cytosol
M	0005856	cellular_component	cytoskeleton
M	0005886	cellular_component	plasma membrane
M	0005911	cellular_component	cell-cell junction
M	0005912	cellular_component	adherens junction
M	0005916	cellular_component	fascia adherens
M	0005925	cellular_component	focal adhesion
M	0007155	biological_process	cell adhesion
M	0007160	biological_process	cell-matrix adhesion
M	0008013	molecular_function	beta-catenin binding
M	0015629	cellular_component	actin cytoskeleton
M	0016020	cellular_component	membrane
M	0030032	biological_process	lamellipodium assembly
M	0030055	cellular_component	cell-substrate junction
M	0030334	biological_process	regulation of cell migration
M	0030336	biological_process	negative regulation of cell migration
M	0031625	molecular_function	ubiquitin protein ligase binding
M	0032991	cellular_component	protein-containing complex
M	0034333	biological_process	adherens junction assembly
M	0034394	biological_process	protein localization to cell surface
M	0034774	cellular_component	secretory granule lumen
M	0035580	cellular_component	specific granule lumen
M	0035633	biological_process	maintenance of blood-brain barrier
M	0042383	cellular_component	sarcolemma
M	0042995	cellular_component	cell projection
M	0043034	cellular_component	costamere
M	0043297	biological_process	apical junction assembly
M	0044291	cellular_component	cell-cell contact zone
M	0045294	molecular_function	alpha-catenin binding
M	0045296	molecular_function	cadherin binding
M	0048675	biological_process	axon extension
M	0051015	molecular_function	actin filament binding
M	0051893	biological_process	regulation of focal adhesion assembly
M	0061826	cellular_component	podosome ring
M	0070062	cellular_component	extracellular exosome
M	0070161	cellular_component	anchoring junction
M	0070527	biological_process	platelet aggregation
M	0090136	biological_process	epithelial cell-cell adhesion
M	1903140	biological_process	regulation of establishment of endothelial barrier
M	1903561	cellular_component	extracellular vesicle
M	1904702	biological_process	regulation of protein localization to adherens junction
M	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue ADP C 401

Chain	Residue
C	GLY13
C	LYS213
C	GLU214
C	GLY302
C	TYR306
C	MG402
C	SER14
C	GLY15
C	LEU16
C	LYS18
C	GLY156
C	ASP157
C	GLY182
C	ARG210

site_id	AC2
Number of Residues	1
Details	binding site for residue MG C 402

Chain	Residue
C	ADP401

site_id	AC3
Number of Residues	13
Details	binding site for residue ADP B 401

Chain	Residue
B	GLY13
B	SER14
B	GLY15
B	LEU16
B	LYS18
B	GLY156
B	ASP157
B	LYS213
B	GLU214
B	GLY302
B	TYR306
B	LYS336
B	MG402

site_id	AC4
Number of Residues	1
Details	binding site for residue MG B 402

Chain	Residue
B	ADP401

site_id	AC5
Number of Residues	15
Details	binding site for residue ADP A 401

Chain	Residue
A	GLY13
A	SER14
A	GLY15
A	LEU16
A	LYS18
A	GLY156
A	ASP157
A	GLY182
A	ARG210
A	LYS213
A	GLU214
A	GLY302
A	MET305
A	TYR306
A	MG402

site_id	AC6
Number of Residues	2
Details	binding site for residue MG A 402

Chain	Residue
A	GLN137
A	ADP401

site_id	AC7
Number of Residues	15
Details	binding site for residue ADP D 401

Chain	Residue
D	GLY13
D	SER14
D	GLY15
D	LEU16
D	LYS18
D	GLY156
D	ASP157
D	GLY182
D	ARG210
D	LYS213
D	GLU214
D	GLY302
D	TYR306
D	LYS336
D	MG402

site_id	AC8
Number of Residues	1
Details	binding site for residue MG D 402

Chain	Residue
D	ADP401

site_id	AC9
Number of Residues	15
Details	binding site for residue ADP E 401

Chain	Residue
E	GLY13
E	SER14
E	GLY15
E	LEU16
E	LYS18
E	GLY156
E	ASP157
E	GLY182
E	ARG210
E	LYS213
E	GLU214
E	GLY302
E	TYR306
E	LYS336
E	MG402

site_id	AD1
Number of Residues	2
Details	binding site for residue MG E 402

Chain	Residue
E	GLN137
E	ADP401

Functional Information from PROSITE/UniProt

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	PS00663
Number of Residues	21
Details	VINCULIN_1 Vinculin family talin-binding region signature. KnLgpgMtkMakmideRQQEL

Chain	Residue	Details
L	LYS162-LEU182

site_id	PS00664
Number of Residues	11
Details	VINCULIN_2 Vinculin repeated domain signature. LnQAkgWLrDP

Chain	Residue	Details
L	LEU277-PRO287
L	ILE388-PRO398
L	ILE497-PRO507

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	5
Details	MOD_RES: N-acetylaspartate; in Actin, alpha skeletal muscle => ECO:0000269\|PubMed:456601

Chain	Residue	Details
C	ASP1
B	ASP1
A	ASP1
D	ASP1
E	ASP1
M	SER574

site_id	SWS_FT_FI2
Number of Residues	10
Details	MOD_RES: Methionine (R)-sulfoxide => ECO:0000250\|UniProtKB:P68134

Chain	Residue	Details
C	MET44
E	MET47
C	MET47
B	MET44
B	MET47
A	MET44
A	MET47
D	MET44
D	MET47
E	MET44

site_id	SWS_FT_FI3
Number of Residues	5
Details	MOD_RES: Tele-methylhistidine => ECO:0000269\|PubMed:12356759, ECO:0007744\|PDB:1MDU

Chain	Residue	Details
C	HIC73
M	SER600
M	SER795
M	SER809
B	HIC73
A	HIC73
D	HIC73
E	HIC73
L	SER809
M	SER260
M	SER275
M	SER579

site_id	SWS_FT_FI4
Number of Residues	5
Details	MOD_RES: N6-methyllysine => ECO:0000250\|UniProtKB:P68133

Chain	Residue	Details
C	LYS84
B	LYS84
A	LYS84
D	LYS84
E	LYS84

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
L	SER290
M	SER290

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
L	SER346
M	SER346

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:21406692

Chain	Residue	Details
L	SER434
M	SER434

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000305

Chain	Residue	Details
L	TYR537
M	TYR537

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
L	THR604
M	THR604

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
L	THR672
M	THR672

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17081983, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
L	SER721
M	SER721

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
L	TYR822
M	TYR822

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphotyrosine; by SRC-type Tyr-kinases => ECO:0000269\|PubMed:15229287

Chain	Residue	Details
L	TYR1133
M	TYR1133

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)