The KTR2 gene from Saccharomyces cerevisiae was identified by polymerase chain reaction amplification of genomic DNA using primers derived from regions of high homology between the products of three yeast genes, KRE2, YUR1 and KTR1. The product encoded by the KTR2 gene is a predicted type II membrane protein of 425 amino acid residues with a short cytoplasmic N-terminus, a membrane-spanning region and a large lumenal domain containing residues with a short cytoplasmic N-terminus, a membrane-spanning region and a large lumenal domain containing four potential N-glycosylation sites. Ktr2p has 58% identity with Yur1p, 39% with Ktr1p and 34% with Kre2p. One member of this gene family, KRE2 (also known as MNT1; Häusler and Robbins, 1992), encodes an alpha-1,2 mannosyltransferase which adds the third mannose onto O-linked glycoprotein side-chains (Häusler et al., 1992). In contrast to KRE2 null mutants, which produce shortened (two-mannose) chains, mutants harboring a KTR2 gene disruption synthesize O-linked chains with the wild-type patterns of five mannose residues. A null mutation in KTR2 leads to partial resistance to killer toxin and hints that KTR2, which encodes a putative mannosyltransferase, is involved in extracellular matrix assembly.