Vinculin family

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1tr2B:3-1133 1syqA:3-257 1rkeA:3-257 1rkcA:3-257 1qkrB:973-1134 1u6hA:3-258 1st6A:3-1134 1zvzA:3-258 1zw2A:3-258 1zw3A:3-258 1t01A:3-253 1xwjA:3-258 1dovA:82-262 1dowA:57-261 1h6gB:377-632 1l7cC:385-651

Vinculin family
Vinculin family
Identifiers
Symbol	Vinculin
Pfam	PF01044
InterPro	IPR006077
PROSITE	PDOC00568
SCOP2	1dow / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	1tr2B:3-1133 1syqA:3-257 1rkeA:3-257 1rkcA:3-257 1qkrB:973-1134 1u6hA:3-258 1st6A:3-1134 1zvzA:3-258 1zw2A:3-258 1zw3A:3-258 1t01A:3-253 1xwjA:3-258 1dovA:82-262 1dowA:57-261 1h6gB:377-632 1l7cC:385-651

Vinculin is a eukaryotic protein that seems to be involved in the attachment of the actin-based microfilaments to the plasma membrane. Vinculin is located at the cytoplasmic side of focal contacts or adhesion plaques.^[1] In addition to actin, vinculin interacts with other structural proteins such as talin and alpha-actinins.

Vinculin is a large protein of 116 kDa (about a 1000 residues). Structurally the protein consists of an acidic N-terminal domain of about 90 kDa separated from a basic C-terminal domain of about 25 kDa by a proline-rich region of about 50 residues. The central part of the N-terminal domain consists of a variable number (3 in vertebrates, 2 in Caenorhabditis elegans) of repeats of a 110 amino acids domain.

Alpha-catenins are evolutionary related to vinculin.^[2] Catenins are proteins that associate with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Three different types of catenins seem to exist: alpha, beta, and gamma. Alpha-catenins are proteins of about 100 kDa which are evolutionary related to vinculin. In terms of their structure the most significant differences are the absence, in alpha-catenin, of the repeated domain and of the proline-rich segment.

Subfamilies edit

Vinculin InterPro: IPR000633
Alpha-catenin InterPro: IPR001033

Human proteins containing this domain edit

CTNNA1; CTNNA2; CTNNA3; CTNNAL1; VCL;

References edit

^ Otto JJ (1990). "Vinculin". Cell Motil. Cytoskeleton. 16 (1): 1–6. doi:10.1002/cm.970160102. PMID 2112986.
^ Lottspeich F, Eckerskorn C, Herrenknecht K, Ozawa M, Lenter M, Kemler R (1991). "The uvomorulin-anchorage protein alpha catenin is a vinculin homologue". Proc. Natl. Acad. Sci. U.S.A. 88 (20): 9156–9160. Bibcode:1991PNAS...88.9156H. doi:10.1073/pnas.88.20.9156. PMC 52671. PMID 1924379.

This article incorporates text from the public domain Pfam and InterPro: IPR006077

[PUB00000977-1] Otto JJ (1990). "Vinculin". Cell Motil. Cytoskeleton. 16 (1): 1–6. doi:10.1002/cm.970160102. PMID 2112986.

[PUB00004758-2] Lottspeich F, Eckerskorn C, Herrenknecht K, Ozawa M, Lenter M, Kemler R (1991). "The uvomorulin-anchorage protein alpha catenin is a vinculin homologue". Proc. Natl. Acad. Sci. U.S.A. 88 (20): 9156–9160. Bibcode:1991PNAS...88.9156H. doi:10.1073/pnas.88.20.9156. PMC 52671. PMID 1924379.

[1]

[2]