The osteopontin SVVYGLR motif binds the integrins α4β1 and α9β1. We show that α4β7 also interacts with this motif and that an SVVYGLR-OH peptide antagonises the α4β7 MAdCAM interaction. The important elements of this motif required to bind α4β1 and α4β7 were probed using a series of mutated peptides based around SVVYGLR. Leu167 is important for the interaction with α4 integrins, as is the C-terminal carboxylic acid of Arg168 exposed by thrombin cleavage. The importance of the acidic group means that SVVYGLR has structural elements in common with other α4 integrin-binding motifs and suggests why thrombin cleavage activates this motif.