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Gene: H06O01.1   

H06O01.1SMapS_parentSequenceSUPERLINK_CB_I
ChromosomeI
Identity (5)
Gene_info Gene_classpdi
GO_term GO:0016853 IEA Inferred_automatically
GO:0005783 IEA Inferred_automatically
GO:0005489 IEA Inferred_automatically
GO:0006118 IEA Inferred_automatically
Structured_description Provisional_description pdi-3 encodes a protein disulfide isomerase (PDI) required for normal cuticle collagen deposition and, subliminally, for maintenance of normal body shape; PDI-3 has both PDI and calcium-dependent transglutaminase activity in vitro, crosslinking proteins through a gamma-glutamyl epsilon-lysine dual residue; PDI-3 is homologous to the human PDI ERp60, as well as a homolog in the dog heartworm Dirofilaria immitis that is required for larval molting; the joint PDI/transglutaminase activity of PDI-3 is biochemically conserved in nematodes and mammals; pdi-3 is constitutively and broadly expressed, particularly in gut and hypodermis. Paper_evidence (8)
Person_evidenceWBPerson567
Curator_confirmedWBPerson567
Date_last_updated17 Jun 2004 00:00:00
While pdi-3(RNAi) animals have no grossly obvious phenotype in mass RNAi assays, their localization of the collagen DPY-7 is mildly abnormal in annular furrows of the cuticle.
More strikingly, pdi-3(RNAi) animals have strong, specific phenotypes with RNAi in a mutant background of alleles with weakened cuticles, such as sqt-3(e2117), dpy-18(e364), dpy-18(ok162), or dpy-18(bx26).
pdi-3(RNAi) animals with a dpy-18(-) or sqt-3(-) background are severely dumpy, with disorderly lateral alae, abnormally weak cuticle, erratically distributed lateral seam cells, protruding vulvas, egg-laying defects, and abnormally slow growth.
Defective tails are seen with sqt-3(-).
These defects are not observed for background mutations of prolyl isomerase subunits other than DPY-18, or for mutations of collagens other than sqt-3.
The second cysteine residue of the Cys-Gly-His-Cys motif in the thioredoxin domain of PDI-3 is the active site of the transamidation reaction; chemical modification of the His residue in this motif blocks transglutaminase activity.
The PDI-3 protein is predicted to be mitochondrial with 52% accuracy.
Proteins localized to a given organelle by experiments tend to share a characteristic phylogenetic distribution of their homologs, called a phylogenetic profile.
For instance, mitochondrial proteins can be identified effectively by their phylogenetic profiles.
By applying phylogenetic profile analysis to the C. elegans genome, Eisenberg and coworkers inferred that this gene, along with 2-4% of all the nuclear genes in C. elegans, encodes a mitochondrial protein.
The large fraction of organism-specific and eukaryote-derived genes suggests that C. elegans mitochondria perform specialized roles absent from prokaryotic mitochondrial ancestors.
Concise_descriptionpdi-3 encodes a protein disulfide isomerase (PDI) required for normal cuticle collagen deposition and, subliminally, for maintenance of normal body shape; PDI-3 has both PDI and calcium-dependent transglutaminase activity in vitro, crosslinking proteins through a gamma-glutamyl epsilon-lysine dual residue; PDI-3 is homologous to the human PDI ERp60, as well as a homolog in the dog heartworm Dirofilaria immitis that is required for larval molting; the joint PDI/transglutaminase activity of PDI-3 is biochemically conserved in nematodes and mammals; pdi-3 is constitutively and broadly expressed, particularly in gut and hypodermis.
Molecular_info (5)
Experimental_info RNAi_result (5)
WB_RNAi_result (6)
Expr_pattern (5)
Y2H_target Y2H005923
Y2H008449
Y2H009457
Reference WBPaper00005704
WBPaper00024269
WBPaper00006361
WBPaper00026640
MethodGene