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Vinculin (Metavinculin)

 VINC_CHICK              Reviewed;        1135 AA.
P12003; Q91024;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
22-NOV-2017, entry version 168.
RecName: Full=Vinculin;
AltName: Full=Metavinculin;
Name=VCL; Synonyms=VINC1;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Embryo;
PubMed=3141928; DOI=10.1073/pnas.85.22.8535;
Coutu M.D., Craig S.W.;
"cDNA-derived sequence of chicken embryo vinculin.";
Proc. Natl. Acad. Sci. U.S.A. 85:8535-8539(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Embryo;
PubMed=2497736; DOI=10.1042/bj2590453;
Price G.J., Jones P., Davison M.D., Patel B., Bendori R., Geiger B.,
Critchley D.R.;
"Primary sequence and domain structure of chicken vinculin.";
Biochem. J. 259:453-461(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
2).
PubMed=1618784;
Byrne B.J., Kaczorowski Y.J., Coutu M.D., Craig S.W.;
"Chicken vinculin and meta-vinculin are derived from a single gene by
alternative splicing of a 207-base pair exon unique to meta-
vinculin.";
J. Biol. Chem. 267:12845-12850(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-881.
TISSUE=Embryo;
PubMed=3117046; DOI=10.1042/bj2450595;
Price G.J., Jones P., Davison M.D., Patel B., Eperon I.C.,
Critchley D.R.;
"Isolation and characterization of a vinculin cDNA from chick-embryo
fibroblasts.";
Biochem. J. 245:595-603(1987).
[5]
ACETYLATION.
PubMed=3030822; DOI=10.1016/0014-5793(87)81536-3;
Kellie S., Wigglesworth N.M.;
"The cytoskeletal protein vinculin is acylated by myristic acid.";
FEBS Lett. 213:428-432(1987).
[6]
TALIN INTERACTION DOMAIN.
PubMed=2512301; DOI=10.1083/jcb.109.6.2917;
Jones P., Jackson P., Price G.J., Patel B., Ohanion V., Lear A.L.,
Critchley D.R.;
"Identification of a talin binding site in the cytoskeletal protein
vinculin.";
J. Cell Biol. 109:2917-2927(1989).
[7]
INTERACTION WITH NRAP.
PubMed=10320340; DOI=10.1021/bi982395t;
Luo G., Herrera A.H., Horowits R.;
"Molecular interactions of N-RAP, a nebulin-related protein of
striated muscle myotendon junctions and intercalated disks.";
Biochemistry 38:6135-6143(1999).
[8]
PHOSPHORYLATION AT TYR-100 AND TYR-1134, FUNCTION, AND MUTAGENESIS OF
TYR-100; TYR-160; TYR-537; TYR-692; TYR-822 AND TYR-1134.
PubMed=15229287; DOI=10.1091/mbc.E04-03-0264;
Zhang Z., Izaguirre G., Lin S.-Y., Lee H.Y., Schaefer E.,
Haimovich B.;
"The phosphorylation of vinculin on tyrosine residues 100 and 1065,
mediated by SRC kinases, affects cell spreading.";
Mol. Biol. Cell 15:4234-4247(2004).
[9]
INTERACTION WITH TLN1.
PubMed=20610383; DOI=10.1074/JBC.M109.095455;
Gingras A.R., Bate N., Goult B.T., Patel B., Kopp P.M., Emsley J.,
Barsukov I.L., Roberts G.C., Critchley D.R.;
"Central region of talin has a unique fold that binds vinculin and
actin.";
J. Biol. Chem. 285:29577-29587(2010).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20584916; DOI=10.1083/jcb.201001149;
le Duc Q., Shi Q., Blonk I., Sonnenberg A., Wang N., Leckband D.,
de Rooij J.;
"Vinculin potentiates E-cadherin mechanosensing and is recruited to
actin-anchored sites within adherens junctions in a myosin II-
dependent manner.";
J. Cell Biol. 189:1107-1115(2010).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CTNNB1.
PubMed=20086044; DOI=10.1242/jcs.056432;
Peng X., Cuff L.E., Lawton C.D., DeMali K.A.;
"Vinculin regulates cell-surface E-cadherin expression by binding to
beta-catenin.";
J. Cell Sci. 123:567-577(2010).
[12]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 881-1135 OF ISOFORM 1.
PubMed=10612396; DOI=10.1016/S0092-8674(00)81549-4;
Bakolitsa C., de Pereda J.M., Bagshaw C.R., Critchley D.R.,
Liddington R.C.;
"Crystal structure of the vinculin tail suggests a pathway for
activation.";
Cell 99:603-613(1999).
[13]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-259 IN COMPLEX WITH
APBB1IP, AND INTERACTION WITH TLN1 AND APBB1IP.
PubMed=23389036; DOI=10.1074/jbc.M112.438119;
Goult B.T., Zacharchenko T., Bate N., Tsang R., Hey F., Gingras A.R.,
Elliott P.R., Roberts G.C., Ballestrem C., Critchley D.R.,
Barsukov I.L.;
"RIAM and vinculin binding to talin are mutually exclusive and
regulate adhesion assembly and turnover.";
J. Biol. Chem. 288:8238-8249(2013).
-!- FUNCTION: Actin filament (F-actin)-binding protein involved in
cell-matrix adhesion and cell-cell adhesion. Regulates cell-
surface E-cadherin expression and potentiates mechanosensing by
the E-cadherin complex. May also play important roles in cell
morphology and locomotion. {ECO:0000269|PubMed:15229287,
ECO:0000269|PubMed:20086044, ECO:0000269|PubMed:20584916}.
-!- SUBUNIT: Exhibits self-association properties. Interacts with
APBB1IP, NRAP and TLN1. Interacts with CTNNB1 and this interaction
is necessary for its localization to the cell-cell junctions and
for its function in regulating cell surface expression of E-
cadherin. {ECO:0000269|PubMed:10320340,
ECO:0000269|PubMed:20086044, ECO:0000269|PubMed:20610383,
ECO:0000269|PubMed:23389036}.
-!- INTERACTION:
P68135:ACTA1 (xeno); NbExp=2; IntAct=EBI-6138078, EBI-367540;
P05094-2:ACTN1; NbExp=5; IntAct=EBI-1039563, EBI-6049246;
P49024:PXN; NbExp=5; IntAct=EBI-1039563, EBI-2896280;
P26039:Tln1 (xeno); NbExp=5; IntAct=EBI-1039563, EBI-1039593;
P50552:VASP (xeno); NbExp=2; IntAct=EBI-1039563, EBI-748201;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20584916};
Peripheral membrane protein {ECO:0000305|PubMed:20584916};
Cytoplasmic side {ECO:0000305|PubMed:20584916}. Cell junction,
adherens junction {ECO:0000269|PubMed:20086044,
ECO:0000269|PubMed:20584916}. Cell junction, focal adhesion
{ECO:0000269|PubMed:20086044}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P85972}. Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:Q64727}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q64727}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q64727}. Note=Recruitment to cell-cell
junctions occurs in a myosin II-dependent manner
(PubMed:20584916). Interaction with CTNNB1 is necessary for its
localization to the cell-cell junctions (PubMed:20086044).
{ECO:0000269|PubMed:20086044, ECO:0000269|PubMed:20584916}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=Metavinculin;
IsoId=P12003-2; Sequence=Displayed;
Name=1; Synonyms=Vinculin;
IsoId=P12003-1; Sequence=VSP_010772;
-!- TISSUE SPECIFICITY: Isoform Metavinculin is muscle-specific.
-!- DOMAIN: Exists in at least two conformations. When in the closed,
'inactive' conformation, extensive interactions between the head
and tail domains prevent detectable binding to most of its
ligands. It takes on an 'active' conformation after cooperative
and simultaneous binding of two different ligands. This activation
involves displacement of the head-tail interactions and leads to a
significant accumulation of ternary complexes. The active form
then binds a number of proteins that have both signaling and
structural roles that are essential for cell adhesion.
{ECO:0000250|UniProtKB:P18206}.
-!- DOMAIN: The N-terminal globular head (Vh) comprises of subdomains
D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links
actin filaments into bundles. An intramolecular interaction
between Vh and Vt masks the F-actin-binding domain located in Vt.
The binding of talin and alpha-actinin to the D1 subdomain of
vinculin induces a helical bundle conversion of this subdomain,
leading to the disruption of the intramolecular interaction and
the exposure of the cryptic F-actin-binding domain of Vt. Vt
inhibits actin filament barbed end elongation without affecting
the critical concentration of actin assembly.
{ECO:0000250|UniProtKB:P18206}.
-!- PTM: Phosphorylated; on serines, threonines and tyrosines.
Phosphorylation on Tyr-1134 in activated platelets affects head-
tail interactions and cell spreading but has no effect on actin
binding nor on localization to focal adhesion plaques.
{ECO:0000269|PubMed:15229287}.
-!- PTM: Acetylated; mainly by myristic acid but also by a small
amount of palmitic acid. {ECO:0000269|PubMed:3030822}.
-!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
{ECO:0000305}.
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EMBL; J04126; AAA49136.1; -; mRNA.
EMBL; M87837; AAA49135.1; -; Genomic_DNA.
EMBL; Y00312; CAA68412.1; -; mRNA.
PIR; A31346; A29997.
RefSeq; NP_990772.1; NM_205441.1. [P12003-1]
RefSeq; XP_015143689.1; XM_015288203.1. [P12003-2]
UniGene; Gga.15976; -.
UniGene; Gga.698; -.
PDB; 1QKR; X-ray; 1.80 A; A/B=879-1135.
PDB; 1ST6; X-ray; 3.10 A; A=1-1135.
PDB; 1T01; X-ray; 2.06 A; A=1-254.
PDB; 1U6H; X-ray; 2.38 A; A=1-259.
PDB; 1XWJ; X-ray; 2.60 A; A=2-259.
PDB; 1ZVZ; X-ray; 1.80 A; A=2-259.
PDB; 1ZW2; X-ray; 2.10 A; A=2-259.
PDB; 1ZW3; X-ray; 3.30 A; A=2-259.
PDB; 2GDC; X-ray; 2.74 A; A=1-266.
PDB; 3JBI; EM; 8.50 A; V=879-1130.
PDB; 3ZDL; X-ray; 2.30 A; A=1-259.
PDB; 4E17; X-ray; 2.30 A; A=1-259.
PDB; 4E18; X-ray; 2.40 A; A=1-259.
PDBsum; 1QKR; -.
PDBsum; 1ST6; -.
PDBsum; 1T01; -.
PDBsum; 1U6H; -.
PDBsum; 1XWJ; -.
PDBsum; 1ZVZ; -.
PDBsum; 1ZW2; -.
PDBsum; 1ZW3; -.
PDBsum; 2GDC; -.
PDBsum; 3JBI; -.
PDBsum; 3ZDL; -.
PDBsum; 4E17; -.
PDBsum; 4E18; -.
ProteinModelPortal; P12003; -.
SMR; P12003; -.
BioGrid; 676671; 2.
DIP; DIP-35191N; -.
ELM; P12003; -.
IntAct; P12003; 15.
STRING; 9031.ENSGALP00000008131; -.
iPTMnet; P12003; -.
PaxDb; P12003; -.
PRIDE; P12003; -.
Ensembl; ENSGALT00000008145; ENSGALP00000008131; ENSGALG00000005079. [P12003-2]
Ensembl; ENSGALT00000061988; ENSGALP00000048583; ENSGALG00000005079. [P12003-1]
GeneID; 396422; -.
KEGG; gga:396422; -.
CTD; 7414; -.
eggNOG; KOG3681; Eukaryota.
eggNOG; ENOG410XSRU; LUCA.
GeneTree; ENSGT00550000074411; -.
HOGENOM; HOG000007828; -.
HOVERGEN; HBG079758; -.
InParanoid; P12003; -.
KO; K05700; -.
OrthoDB; EOG091G038S; -.
PhylomeDB; P12003; -.
Reactome; R-GGA-114608; Platelet degranulation.
Reactome; R-GGA-445355; Smooth Muscle Contraction.
Reactome; R-GGA-6798695; Neutrophil degranulation.
SABIO-RK; P12003; -.
EvolutionaryTrace; P12003; -.
PRO; PR:P12003; -.
Proteomes; UP000000539; Chromosome 6.
Bgee; ENSGALG00000005079; -.
ExpressionAtlas; P12003; baseline and differential.
GO; GO:0015629; C:actin cytoskeleton; IDA:AgBase.
GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
GO; GO:0005903; C:brush border; IDA:AgBase.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0043034; C:costamere; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; IDA:AgBase.
GO; GO:0090637; C:inner dense plaque of desmosome; IDA:AgBase.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005927; C:muscle tendon junction; IDA:AgBase.
GO; GO:0031594; C:neuromuscular junction; IDA:AgBase.
GO; GO:0090636; C:outer dense plaque of desmosome; IDA:AgBase.
GO; GO:0005886; C:plasma membrane; IDA:AgBase.
GO; GO:0002102; C:podosome; IEA:Ensembl.
GO; GO:0042383; C:sarcolemma; IDA:AgBase.
GO; GO:0098723; C:skeletal muscle myofibril; IDA:AgBase.
GO; GO:0001725; C:stress fiber; IDA:AgBase.
GO; GO:1990357; C:terminal web; IDA:AgBase.
GO; GO:0030018; C:Z disc; IDA:AgBase.
GO; GO:0005915; C:zonula adherens; IDA:AgBase.
GO; GO:0051015; F:actin filament binding; IEA:InterPro.
GO; GO:0051393; F:alpha-actinin binding; IDA:AgBase.
GO; GO:0045294; F:alpha-catenin binding; IDA:BHF-UCL.
GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
GO; GO:0045296; F:cadherin binding; IPI:BHF-UCL.
GO; GO:0002162; F:dystroglycan binding; IEA:Ensembl.
GO; GO:0051371; F:muscle alpha-actinin binding; IMP:AgBase.
GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
GO; GO:0097110; F:scaffold protein binding; IPI:AgBase.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0017166; F:vinculin binding; IDA:AgBase.
GO; GO:0034333; P:adherens junction assembly; IDA:BHF-UCL.
GO; GO:0043297; P:apical junction assembly; IEA:Ensembl.
GO; GO:0048675; P:axon extension; IEA:Ensembl.
GO; GO:0090136; P:epithelial cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
GO; GO:0002009; P:morphogenesis of an epithelium; IDA:BHF-UCL.
GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
InterPro; IPR017997; Vinculin.
InterPro; IPR006077; Vinculin/catenin.
InterPro; IPR000633; Vinculin_CS.
PANTHER; PTHR18914; PTHR18914; 3.
PANTHER; PTHR18914:SF1; PTHR18914:SF1; 3.
Pfam; PF01044; Vinculin; 3.
SUPFAM; SSF47220; SSF47220; 8.
PROSITE; PS00663; VINCULIN_1; 1.
PROSITE; PS00664; VINCULIN_2; 3.
1: Evidence at protein level;
3D-structure; Actin-binding; Alternative splicing; Cell adhesion;
Cell junction; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Lipoprotein; Membrane; Myristate; Palmitate;
Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P26234}.
CHAIN 2 1135 Vinculin.
/FTId=PRO_0000064255.
REPEAT 259 369 1. {ECO:0000255}.
REPEAT 370 479 2. {ECO:0000255}.
REPEAT 480 589 3. {ECO:0000255}.
REGION 2 835 N-terminal globular head.
{ECO:0000250|UniProtKB:P18206}.
REGION 168 208 Talin-interaction.
{ECO:0000269|PubMed:2512301}.
REGION 259 589 3 X 112 AA tandem repeats. {ECO:0000255}.
REGION 836 878 Linker (Pro-rich).
{ECO:0000250|UniProtKB:P18206}.
REGION 879 1135 C-terminal tail.
{ECO:0000250|UniProtKB:P18206}.
REGION 1004 1047 Facilitates phospholipid membrane
insertion.
{ECO:0000250|UniProtKB:Q64727}.
REGION 1121 1135 Facilitates phospholipid membrane
insertion.
{ECO:0000250|UniProtKB:Q64727}.
COMPBIAS 837 878 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
MOD_RES 100 100 Phosphotyrosine.
{ECO:0000269|PubMed:15229287}.
MOD_RES 537 537 Phosphotyrosine. {ECO:0000305}.
MOD_RES 822 822 Phosphotyrosine.
{ECO:0000250|UniProtKB:P18206}.
MOD_RES 1134 1134 Phosphotyrosine; by SRC-type Tyr-kinases.
{ECO:0000269|PubMed:15229287}.
VAR_SEQ 916 984 Missing (in isoform 1).
{ECO:0000303|PubMed:2497736,
ECO:0000303|PubMed:3141928}.
/FTId=VSP_010772.
MUTAGEN 100 100 Y->F: Some reduction of phosphorylation
levels in platelets. Little change in
cell spreading. Complete loss of
phosphorylation. No change in subcellular
location nor on in vitro actin binding.
40% decrease in cell spreading; when
associated with F-1134.
{ECO:0000269|PubMed:15229287}.
MUTAGEN 160 160 Y->F: No change of phosphorylation levels
in platelets.
{ECO:0000269|PubMed:15229287}.
MUTAGEN 537 537 Y->F: No change of phosphorylation levels
in platelets.
{ECO:0000269|PubMed:15229287}.
MUTAGEN 692 692 Y->F: No change of phosphorylation levels
in platelets.
{ECO:0000269|PubMed:15229287}.
MUTAGEN 822 822 Y->F: No change of phosphorylation levels
in platelets.
{ECO:0000269|PubMed:15229287}.
MUTAGEN 1134 1134 Y->F: Greatly reduced phosphorylation
levels in platelets. Little change in
cell spreading. Complete loss of
phosphorylation. No change in subcellular
location nor on in vitro actin binding.
40% decrease in cell spreading; when
associated with F-100.
{ECO:0000269|PubMed:15229287}.
CONFLICT 442 447 TAKLSD -> QLSCQI (in Ref. 2 and 4;
CAA68412). {ECO:0000305}.
CONFLICT 701 701 Q -> H (in Ref. 2 and 4; CAA68412).
{ECO:0000305}.
CONFLICT 880 880 E -> K (in Ref. 4; CAA68412).
{ECO:0000305}.
HELIX 7 28 {ECO:0000244|PDB:1ZVZ}.
TURN 29 32 {ECO:0000244|PDB:1ZVZ}.
STRAND 33 35 {ECO:0000244|PDB:1ZVZ}.
HELIX 41 63 {ECO:0000244|PDB:1ZVZ}.
HELIX 68 73 {ECO:0000244|PDB:1ZVZ}.
HELIX 75 97 {ECO:0000244|PDB:1ZVZ}.
HELIX 102 146 {ECO:0000244|PDB:1ZVZ}.
HELIX 148 150 {ECO:0000244|PDB:3ZDL}.
HELIX 154 181 {ECO:0000244|PDB:1ZVZ}.
HELIX 185 215 {ECO:0000244|PDB:1ZVZ}.
STRAND 218 221 {ECO:0000244|PDB:1T01}.
HELIX 222 249 {ECO:0000244|PDB:1ZVZ}.
HELIX 253 255 {ECO:0000244|PDB:3ZDL}.
HELIX 256 275 {ECO:0000244|PDB:1ST6}.
HELIX 277 285 {ECO:0000244|PDB:1ST6}.
TURN 292 295 {ECO:0000244|PDB:1ST6}.
HELIX 296 311 {ECO:0000244|PDB:1ST6}.
HELIX 318 338 {ECO:0000244|PDB:1ST6}.
TURN 339 342 {ECO:0000244|PDB:1ST6}.
HELIX 347 395 {ECO:0000244|PDB:1ST6}.
HELIX 405 421 {ECO:0000244|PDB:1ST6}.
HELIX 428 451 {ECO:0000244|PDB:1ST6}.
HELIX 457 482 {ECO:0000244|PDB:1ST6}.
HELIX 493 505 {ECO:0000244|PDB:1ST6}.
HELIX 516 531 {ECO:0000244|PDB:1ST6}.
HELIX 535 556 {ECO:0000244|PDB:1ST6}.
HELIX 567 598 {ECO:0000244|PDB:1ST6}.
HELIX 604 614 {ECO:0000244|PDB:1ST6}.
HELIX 622 650 {ECO:0000244|PDB:1ST6}.
HELIX 654 681 {ECO:0000244|PDB:1ST6}.
TURN 682 684 {ECO:0000244|PDB:1ST6}.
HELIX 689 714 {ECO:0000244|PDB:1ST6}.
HELIX 719 739 {ECO:0000244|PDB:1ST6}.
STRAND 742 744 {ECO:0000244|PDB:1ST6}.
TURN 746 748 {ECO:0000244|PDB:1ST6}.
HELIX 752 772 {ECO:0000244|PDB:1ST6}.
HELIX 777 802 {ECO:0000244|PDB:1ST6}.
STRAND 803 806 {ECO:0000244|PDB:1ST6}.
TURN 809 813 {ECO:0000244|PDB:1ST6}.
HELIX 814 817 {ECO:0000244|PDB:1ST6}.
TURN 818 823 {ECO:0000244|PDB:1ST6}.
HELIX 824 835 {ECO:0000244|PDB:1ST6}.
STRAND 887 890 {ECO:0000244|PDB:1ST6}.
STRAND 892 894 {ECO:0000244|PDB:1ST6}.
HELIX 897 909 {ECO:0000244|PDB:1ST6}.
HELIX 961 964 {ECO:0000244|PDB:1QKR}.
HELIX 966 978 {ECO:0000244|PDB:1QKR}.
HELIX 987 1005 {ECO:0000244|PDB:1QKR}.
HELIX 1010 1012 {ECO:0000244|PDB:1QKR}.
HELIX 1013 1040 {ECO:0000244|PDB:1QKR}.
HELIX 1044 1054 {ECO:0000244|PDB:1QKR}.
HELIX 1057 1074 {ECO:0000244|PDB:1QKR}.
STRAND 1075 1077 {ECO:0000244|PDB:1ST6}.
HELIX 1082 1113 {ECO:0000244|PDB:1QKR}.
HELIX 1121 1123 {ECO:0000244|PDB:1QKR}.
SEQUENCE 1135 AA; 124560 MW; 28CC2699C9511058 CRC64;
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVSAVQAA VSNLVRVGKE
TVQTTEDQIL KRDMPPAFIK VENACTKLVR AAQMLQADPY SVPARDYLID GSRGILSGTS
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ
ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNTKS QGIEEALKNR NFTVEKMSAE
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ALIDSKMNQA KGWLRDPNAP PGDAGEQAIR
QILDEAGKAG ELCAGKERRE ILGTCKTLGQ MTDQLADLRA RGQGATPMAM QKAQQVSQGL
DLLTAKVENA ARKLEAMTNS KQAIAKKIDA AQNWLADPNG GSEGEEHIRG IMSEARKVAE
LCEEPKERDD ILRSLGEISA LTAKLSDLRR HGKGDSPEAR ALAKQIATSL QNLQSKTNRA
VANTRPVKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGRRLA NVMMGPYRQD
LLAKCDRVDQ LAAQLADLAA RGEGESPQAR AIAAQLQDSL KDLKARMQEA MTQEVSDVFS
DTTTPIKLLA VAATAPSDTP NREEVFEERA ANFENHAARL GATAEKAAAV GTANKTTVEG
IQATVKSARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK
SLLDASEEAI KKDLDKCKVA MANMQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR
EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP
DFPPPPPDLE HLHLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEAINQPMMM
AARQLHDEAR KWSSKPVTVI NEAAEAGVDI DEEDDADVEF SLPSDIEDDY EPELLLMPTN
QPVNQPILAA AQSLHREATK WSSKGNDIIA AAKRMALLMA EMSRLVRGGS GNKRALIQCA
KDIAKASDEV TRLAKEVAKQ CTDKRIRTNL LQVCERIPTI STQLKILSTV KATMLGRTNI
SDEESEQATE MLVHNAQNLM QSVKETVREA EAASIKIRTD AGFTLRWVRK TPWYQ


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