Integrins [1,2] are a large family of cell surface receptors that mediate cell
to cell as well as cell to matrix adhesion. Some integrins recognize the R-G-D
sequence in their extracellular matrix protein ligand. Structurally, integrins
consist of a dimer of an α and a β chain. Each subunit has a large
N-terminal extracellular domain followed by a transmembrane domain and a short
C-terminal cytoplasmic region. Some α subunits are cleaved post-translationally to produce a heavy and a light chain linked by a disulfide
bond. The sequence of a number of α chains has been obtained and are
The α-1 chain (VLA-1) (CD49a) which, with the β-1 chain, acts as a
receptor for laminin and collagen.
The α-2 chain (VLA-2) (CD49b) which, with the β-1 chain, acts as a
receptor that binds collagen.
The α-3 chain (VLA-3) (Galactoprotein B3).
The α-4 chain (VLA-4) (CD49d) which, with the β-1 chain, interacts
with vascular cell adhesion protein 1 (VCAM-1).
The α-5 chain (VLA-5) (CD49e) which, with the β-1 chain, forms a
receptor specific to fibronectin.
The α-6 chain (VLA-6) which, with the β-1 chain, forms a platelet
The α-7 chain which, with the β-1 chain, forms a skeletal myoblast
The α-8 chain which, with the β-1 chain plays a possible role in
cell-cell interactions during axon-growth and fasciculation.
The α-L chain (LFA-1) (CD11a) which, with the β-2 chain, interacts
with intercellular adhesion molecule 1 (ICAM-1).
The α-M chain (MAC-1) (CD11b) which, with the β-2 chain, forms the
receptor for the iC3b fragment of the third complement component.
The α-X chain (p150,95) (CD11c) which, with the β-2 chain, probably
forms a receptor for the iC3b fragment of the third complement component.
The α-V chain (CD51) which, with the β-3 chain, forms a receptor
that binds vitronectin.
The α-IIB chain (CD41) (also known as platelet glycoprotein IIb) which,
with the β-3 chain, forms a receptor which binds VWF, fibrinogen,
fibronectin, and vitronectin.
The Drosophila position-specific antigen 2 α chain (PS2).
Caenorhabditis elegans hypothetical proteins F54F2.1 and F54G8.3.
All these integrin α chains share a conserved sequence which is found at
the beginning of the cytoplasmic domain, just after the end of the
transmembrane region. This motif is probably involved in heterodimer
association and may lock the heterodimer into a low affinity conformation in
the abscence of activating signals. We have used this conserved region as a
In position 7 of the pattern all vertebrate integrins have Lys, while
Drosophila PS2 has Asn.
December 2001 / Text revised.
PROSITE method (with tools and information) covered by this documentation:
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.