Protein mannosyltransferase (PMT) involved in hyphal growth and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Essential protein that plays an important role in virulence. a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+) a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] = 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate + H(+) Protein modification; protein glycosylation. PMT1 and PMT2 form a functional heterodimer. Associates with lipid rafts in a RTA2-dependent manner. Transcribed in the yeast form, but expression is increased two to threefold during hyphal induction. Also induced during cell wall regeneration. Up-regulated more than twofold when PMT1 expression is impaired. MSB2 functions not only to secure basal levels of the PMT2 transcripts but is needed also for up-regulation of both transcripts upon PMT1 inhibition. Disruption of both alleles leads to letality. Disruption of only one allele impairs filamentation and leads to an altered cell wall composition with reduced amounts of beta-1,6-glucan and shows reduced virulence in a mouse model of hematogenously disseminated candidiasis (HDC) and using reconstituted human epithelium (RHE). Belongs to the glycosyltransferase 39 family.