protein disulfide-isomerase-like protein of the testis (PDILT)

Function

• probable redox-inactive chaperone involved in spermatogenesis
• interacts with ERO1L & CLGN

Structure

• homodimer, not disulfide-linked
• N-glycosylated
• thioredoxin domain lacks the conserved redox-active Cys at position 417 which is replaced by a Ser residue, suggesting that it lacks thioredoxin activity
• belongs to the protein disulfide isomerase family contains 1 thioredoxin domain

Compartment

endoplasmic reticulum

Expression

testis-specific

More general terms

• glycoprotein
• chaperonin; chaperone
• testis-specific protein

Database

• UniProt: http://www.uniprot.org/uniprot/Q8N807.html