P12003 (VINC_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vinculin

Alternative name(s):
Metavinculin

Gene names

Name:	VCL
Synonyms:	VINC1

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	1135 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.8 Ref.9 Ref.10
Subunit structure	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. Ref.6 Ref.7 Ref.10 Ref.12
Subcellular location	Cytoplasm › cytoskeleton. Cell junction › adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Cytoplasmic face of adhesion plaques. Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions. Ref.9 Ref.10
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 By similarity. Ref.6 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 By similarity. Ref.6
Post-translational modification	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. Ref.8 Acetylated; mainly by myristic acid but also by a small amount of palmitic acid.
Sequence similarities	Belongs to the vinculin/alpha-catenin family.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Actin-binding
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adherens junction assembly Inferred from direct assay Ref.10. Source: BHF-UCL epithelial cell-cell adhesion Inferred from direct assay Ref.10. Source: BHF-UCL lamellipodium assembly Inferred from sequence or structural similarity. Source: UniProtKB morphogenesis of an epithelium Inferred from direct assay Ref.10. Source: BHF-UCL regulation of cell migration Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	actin cytoskeleton Inferred from electronic annotation. Source: InterPro cell-cell junction Inferred from direct assay Ref.9. Source: UniProtKB costamere Inferred from sequence or structural similarity. Source: UniProtKB focal adhesion Inferred from sequence or structural similarity. Source: UniProtKB mitochondrial inner membrane Inferred from direct assay PubMed 12615910. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alpha-catenin binding Inferred from direct assay Ref.10. Source: BHF-UCL beta-catenin binding Inferred from direct assay Ref.10. Source: BHF-UCL structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTN1	P05094-2	5	EBI-1039563,EBI-6049246
PXN	P49024	5	EBI-1039563,EBI-2896280
VASP	P50552	2	EBI-1039563,EBI-748201	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: P12003-2)

Also known as: Metavinculin;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: P12003-1)

Also known as: Vinculin;

The sequence of this isoform differs from the canonical sequence as follows:
     916-984: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 1135

1134

Vinculin

PRO_0000064255

Regions

Repeat

259 – 369

111

1

Repeat

370 – 479

110

2

Repeat

480 – 589

110

3

Region

2 – 835

834

N-terminal globular head By similarity

Region

168 – 208

41

Talin-interaction

Region

259 – 589

331

3 X 112 AA tandem repeats

Region

836 – 878

43

Linker (Pro-rich) By similarity

Region

879 – 1135

257

C-terminal tail By similarity

Region

1004 – 1047

44

Facilitates phospholipid membrane insertion By similarity

Region

1121 – 1135

15

Facilitates phospholipid membrane insertion By similarity

Compositional bias

837 – 878

42

Pro-rich

Amino acid modifications

Modified residue

100

1

Phosphotyrosine Ref.8

Modified residue

537

1

Phosphotyrosine Potential

Modified residue

822

1

Phosphotyrosine Potential

Modified residue

1134

1

Phosphotyrosine; by SRC-type Tyr-kinases Ref.8

Natural variations

Alternative sequence

916 – 984

69

Missing in isoform 1.

VSP_010772

Experimental info

Mutagenesis

100

1

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. Ref.8

Mutagenesis

160

1

Y → F: No change of phosphorylation levels in platelets. Ref.8

Mutagenesis

537

1

Y → F: No change of phosphorylation levels in platelets. Ref.8

Mutagenesis

692

1

Y → F: No change of phosphorylation levels in platelets. Ref.8

Mutagenesis

822

1

Y → F: No change of phosphorylation levels in platelets. Ref.8

Mutagenesis

1134

1

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. Ref.8

Sequence conflict

442 – 447

6

TAKLSD → QLSCQI Ref.2

Sequence conflict

442 – 447

6

TAKLSD → QLSCQI in CAA68412. Ref.4

Sequence conflict

701

1

Q → H Ref.2

Sequence conflict

701

1

Q → H in CAA68412. Ref.4

Sequence conflict

880

1

E → K in CAA68412. Ref.4

Secondary structure

1

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1135

Helix Strand Turn

Details...

Helix

7 – 28

22

Turn

29 – 32

4

Beta strand

33 – 35

3

Helix

41 – 63

23

Helix

68 – 73

6

Helix

75 – 97

23

Helix

102 – 146

45

Helix

148 – 150

3

Helix

154 – 181

28

Helix

185 – 215

31

Beta strand

218 – 221

4

Helix

222 – 249

28

Helix

253 – 255

3

Helix

256 – 275

20

Helix

277 – 285

9

Turn

292 – 295

4

Helix

296 – 311

16

Helix

318 – 338

21

Turn

339 – 342

4

Helix

347 – 395

49

Helix

405 – 421

17

Helix

428 – 451

24

Helix

457 – 482

26

Helix

493 – 505

13

Helix

516 – 531

16

Helix

535 – 556

22

Helix

567 – 598

32

Helix

604 – 614

11

Helix

622 – 650

29

Helix

654 – 681

28

Turn

682 – 684

3

Helix

689 – 714

26

Helix

719 – 739

21

Beta strand

742 – 744

3

Turn

746 – 748

3

Helix

752 – 772

21

Helix

777 – 802

26

Beta strand

803 – 806

4

Turn

809 – 813

5

Helix

814 – 817

4

Turn

818 – 823

6

Helix

824 – 835

12

Beta strand

887 – 890

4

Helix

892 – 895

4

Helix

897 – 904

8

Helix

974 – 978

5

Helix

987 – 1005

19

Helix

1010 – 1012

3

Helix

1013 – 1040

28

Helix

1044 – 1054

11

Helix

1057 – 1074

18

Beta strand

1075 – 1077

3

Helix

1082 – 1113

32

Helix

1121 – 1123

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 (Metavinculin) [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 28CC2699C9511058	FASTA	1,135	124,560
	10 20 30 40 50 60 MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVSAVQAA VSNLVRVGKE 70 80 90 100 110 120 TVQTTEDQIL KRDMPPAFIK VENACTKLVR AAQMLQADPY SVPARDYLID GSRGILSGTS 130 140 150 160 170 180 DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ 190 200 210 220 230 240 ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNTKS QGIEEALKNR NFTVEKMSAE 250 260 270 280 290 300 INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ALIDSKMNQA KGWLRDPNAP PGDAGEQAIR 310 320 330 340 350 360 QILDEAGKAG ELCAGKERRE ILGTCKTLGQ MTDQLADLRA RGQGATPMAM QKAQQVSQGL 370 380 390 400 410 420 DLLTAKVENA ARKLEAMTNS KQAIAKKIDA AQNWLADPNG GSEGEEHIRG IMSEARKVAE 430 440 450 460 470 480 LCEEPKERDD ILRSLGEISA LTAKLSDLRR HGKGDSPEAR ALAKQIATSL QNLQSKTNRA 490 500 510 520 530 540 VANTRPVKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGRRLA NVMMGPYRQD 550 560 570 580 590 600 LLAKCDRVDQ LAAQLADLAA RGEGESPQAR AIAAQLQDSL KDLKARMQEA MTQEVSDVFS 610 620 630 640 650 660 DTTTPIKLLA VAATAPSDTP NREEVFEERA ANFENHAARL GATAEKAAAV GTANKTTVEG 670 680 690 700 710 720 IQATVKSARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK 730 740 750 760 770 780 SLLDASEEAI KKDLDKCKVA MANMQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR 790 800 810 820 830 840 EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP 850 860 870 880 890 900 DFPPPPPDLE HLHLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEAINQPMMM 910 920 930 940 950 960 AARQLHDEAR KWSSKPVTVI NEAAEAGVDI DEEDDADVEF SLPSDIEDDY EPELLLMPTN 970 980 990 1000 1010 1020 QPVNQPILAA AQSLHREATK WSSKGNDIIA AAKRMALLMA EMSRLVRGGS GNKRALIQCA 1030 1040 1050 1060 1070 1080 KDIAKASDEV TRLAKEVAKQ CTDKRIRTNL LQVCERIPTI STQLKILSTV KATMLGRTNI 1090 1100 1110 1120 1130 SDEESEQATE MLVHNAQNLM QSVKETVREA EAASIKIRTD AGFTLRWVRK TPWYQ
	Isoform 1 (Vinculin) [UniParc]. Checksum: 6F585201260BA47F	FASTA	1,066	116,999
	10 20 30 40 50 60 MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVSAVQAA VSNLVRVGKE 70 80 90 100 110 120 TVQTTEDQIL KRDMPPAFIK VENACTKLVR AAQMLQADPY SVPARDYLID GSRGILSGTS 130 140 150 160 170 180 DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ 190 200 210 220 230 240 ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNTKS QGIEEALKNR NFTVEKMSAE 250 260 270 280 290 300 INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ALIDSKMNQA KGWLRDPNAP PGDAGEQAIR 310 320 330 340 350 360 QILDEAGKAG ELCAGKERRE ILGTCKTLGQ MTDQLADLRA RGQGATPMAM QKAQQVSQGL 370 380 390 400 410 420 DLLTAKVENA ARKLEAMTNS KQAIAKKIDA AQNWLADPNG GSEGEEHIRG IMSEARKVAE 430 440 450 460 470 480 LCEEPKERDD ILRSLGEISA LTAKLSDLRR HGKGDSPEAR ALAKQIATSL QNLQSKTNRA 490 500 510 520 530 540 VANTRPVKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGRRLA NVMMGPYRQD 550 560 570 580 590 600 LLAKCDRVDQ LAAQLADLAA RGEGESPQAR AIAAQLQDSL KDLKARMQEA MTQEVSDVFS 610 620 630 640 650 660 DTTTPIKLLA VAATAPSDTP NREEVFEERA ANFENHAARL GATAEKAAAV GTANKTTVEG 670 680 690 700 710 720 IQATVKSARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK 730 740 750 760 770 780 SLLDASEEAI KKDLDKCKVA MANMQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR 790 800 810 820 830 840 EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP 850 860 870 880 890 900 DFPPPPPDLE HLHLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEAINQPMMM 910 920 930 940 950 960 AARQLHDEAR KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGNKRALIQC AKDIAKASDE 970 980 990 1000 1010 1020 VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISDEESEQAT 1030 1040 1050 1060 EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLRWVR KTPWYQ

References

[1]	"cDNA-derived sequence of chicken embryo vinculin." Coutu M.D., Craig S.W. Proc. Natl. Acad. Sci. U.S.A. 85:8535-8539(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Embryo.
[2]	"Primary sequence and domain structure of chicken vinculin." Price G.J., Jones P., Davison M.D., Patel B., Bendori R., Geiger B., Critchley D.R. Biochem. J. 259:453-461(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Embryo.
[3]	"Chicken vinculin and meta-vinculin are derived from a single gene by alternative splicing of a 207-base pair exon unique to meta-vinculin." Byrne B.J., Kaczorowski Y.J., Coutu M.D., Craig S.W. J. Biol. Chem. 267:12845-12850(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
[4]	"Isolation and characterization of a vinculin cDNA from chick-embryo fibroblasts." Price G.J., Jones P., Davison M.D., Patel B., Eperon I.C., Critchley D.R. Biochem. J. 245:595-603(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-881. Tissue: Embryo.
[5]	"The cytoskeletal protein vinculin is acylated by myristic acid." Kellie S., Wigglesworth N.M. FEBS Lett. 213:428-432(1987) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION.
[6]	"Identification of a talin binding site in the cytoskeletal protein vinculin." Jones P., Jackson P., Price G.J., Patel B., Ohanion V., Lear A.L., Critchley D.R. J. Cell Biol. 109:2917-2927(1989) [PubMed] [Europe PMC] [Abstract] Cited for: TALIN INTERACTION DOMAIN.
[7]	"Molecular interactions of N-RAP, a nebulin-related protein of striated muscle myotendon junctions and intercalated disks." Luo G., Herrera A.H., Horowits R. Biochemistry 38:6135-6143(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NRAP.
[8]	"The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading." Zhang Z., Izaguirre G., Lin S.-Y., Lee H.Y., Schaefer E., Haimovich B. Mol. Biol. Cell 15:4234-4247(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-100 AND TYR-1134, FUNCTION, MUTAGENESIS OF TYR-100; TYR-160; TYR-537; TYR-692; TYR-822 AND TYR-1134.
[9]	"Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner." le Duc Q., Shi Q., Blonk I., Sonnenberg A., Wang N., Leckband D., de Rooij J. J. Cell Biol. 189:1107-1115(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	"Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin." Peng X., Cuff L.E., Lawton C.D., DeMali K.A. J. Cell Sci. 123:567-577(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1.
[11]	"Crystal structure of the vinculin tail suggests a pathway for activation." Bakolitsa C., de Pereda J.M., Bagshaw C.R., Critchley D.R., Liddington R.C. Cell 99:603-613(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 881-1135 OF ISOFORM 1.
[12]	"RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover." 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. J. Biol. Chem. 0:0-0(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-259 IN COMPLEX WITH APBB1IP, INTERACTION WITH TLN1 AND APBB1IP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04126 mRNA. Translation: AAA49136.1.
M87837 Genomic DNA. Translation: AAA49135.1.
Y00312 mRNA. Translation: CAA68412.1.

IPI

IPI00589062.
IPI00602492.

PIR

A29997. A31346.

RefSeq

NP_990772.1. NM_205441.1.

UniGene

Gga.698.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QKR	X-ray	1.80	A/B	879-1135	[»]
1ST6	X-ray	3.10	A	1-1135	[»]
1T01	X-ray	2.06	A	1-254	[»]
1U6H	X-ray	2.38	A	1-259	[»]
1XWJ	X-ray	2.60	A	1-259	[»]
1ZVZ	X-ray	1.80	A	2-258	[»]
1ZW2	X-ray	2.10	A	1-259	[»]
1ZW3	X-ray	3.30	A	2-258	[»]
2GDC	X-ray	2.74	A	1-265	[»]
3ZDL	X-ray	2.30	A	1-259	[»]
4E17	X-ray	2.30	A	1-259	[»]
4E18	X-ray	2.40	A	1-259	[»]

ProteinModelPortal

P12003.

SMR

P12003. Positions 1-254.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35191N.

IntAct

P12003. 6 interactions.

STRING

9031.ENSGALP00000008131.

Proteomic databases

PaxDb

P12003.

PRIDE

P12003.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

396422.

KEGG

gga:396422.

Organism-specific databases

CTD

7414.

Phylogenomic databases

eggNOG

NOG329927.

HOGENOM

HOG000007828.

HOVERGEN

HBG079758.

InParanoid

P12003.

KO

K05700.

OrthoDB

EOG4P5K8C.

Family and domain databases

InterPro

IPR017997. Vinculin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]

Pfam

PF01044. Vinculin. 3 hits.
[Graphical view]

PRINTS

PR00806. VINCULIN.

SUPFAM

SSF47220. Vinculin/catenin. 8 hits.

PROSITE

PS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P12003.

NextBio

20816463.

Entry information

Entry name

VINC_CHICK

Accession

Primary (citable) accession number: P12003
Secondary accession number(s): Q91024

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 126 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program