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

General

chaperonin; chaperone glycoprotein testis-specific protein

Properties

SIZE: entity length = 584 aa MW = 67 kD COMPARTMENT: endoplasmic reticulum MOTIF: signal sequence {1-20} N-glycosylation site {N58} N-glycosylation site {N128} N-glycosylation site {N160} N-glycosylation site {N340} thioredoxin domain SITE: 388-451 MOTIF: cysteine residue {X1} MODIFICATION: cysteine residue {X2} cysteine residue {X2} MODIFICATION: cysteine residue {X1} N-glycosylation site {N540} Prevents secretion from ER {581-584}

Database Correlations

UniProt Q8N807 Pfam PF00085

References

UniProt :accession Q8N807