The TAP1 and TAP2 proteins form a heterodimer that transports short pe
ptides from the cytosol into the endoplasmic reticulum lumen, Extensiv
e allelic polymorphism of the rat TAP transporter has been shown to af
fect the repertoire of peptides presented by MHC class I molecules, St
ructural polymorphism in the human TAP genes is much more limited and
has not been observed to have functional consequences, We have examine
d the polymorphism in mouse TAP1 and TAP2 in inbred mice, While the nu
mber of polymorphic positions in these molecules is more similar to th
at in human than to that in the rat, all strains examined have a struc
turally unique TAP transporter, suggesting the possibility of function
al polymorphism, Furthermore, allelic variations in the mouse transpor
ter are predominantly located in or adjacent to membrane-spanning doma
ins, although no significant bias in the ratio of nonsynonymous to syn
onymous substitutions is observed, We also report that mouse TAP1 begi
ns 172 amino acids upstream of the previously published start site and
report the genomic organization of mouse Tap-1 and Tap-2.