PDIA3 information

PDIA3
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2ALB, 2DMM, 2H8L, 3F8U
Identifiers
Aliases	PDIA3, protein disulfide isomerase family A, member 3, ER60, ERp57, ERp60, ERp61, GRP57, GRP58, HEL-S-269, HEL-S-93n, HsT17083, P58, PI-PLC, protein disulfide isomerase family A member 3
External IDs	OMIM: 602046 MGI: 95834 HomoloGene: 68454 GeneCards: PDIA3
Gene location (Human)
Chr.	Chromosome 15 (human)
End	43,773,279 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	121,269,168 bp
RNA expression pattern
	Top expressed in
	corpus epididymis; ; stromal cell of endometrium; ; caput epididymis; ; left lobe of thyroid gland; ; right lobe of thyroid gland; ; anterior pituitary; ; smooth muscle tissue; ; rectum; ; jejunal mucosa; ; body of pancreas;
	Top expressed in
	seminal vesicula; ; molar; ; dermis; ; calvaria; ; maxillary prominence; ; abdominal wall; ; somite; ; belly cord; ; optic nerve; ; islet of Langerhans;
	More reference expression data
	n/a
Gene ontology
Molecular function	disulfide oxidoreductase activity; isomerase activity; protein binding; phospholipase C activity; cysteine-type endopeptidase activity; RNA binding; protein disulfide isomerase activity; identical protein binding;
Cellular component	endoplasmic reticulum lumen; focal adhesion; melanosome; myelin sheath; cell surface; endoplasmic reticulum; extracellular exosome; nucleus; phagocytic vesicle; recycling endosome membrane; extracellular space; MHC class I peptide loading complex;
Biological process	protein import into nucleus; antigen processing and presentation of peptide antigen via MHC class I; protein folding in endoplasmic reticulum; cell redox homeostasis; response to endoplasmic reticulum stress; protein retention in ER lumen; protein folding; positive regulation of extrinsic apoptotic signaling pathway; signal transduction; proteolysis; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; cellular response to interleukin-7;
	Sources:Amigo / QuickGO
Orthologs
	2923
	14827
	ENSG00000167004
	ENSMUSG00000027248
	P30101
	P27773
	NM_005313
	NM_007952
	NP_005304
	NP_031978
	Wikidata
View/Edit Human	View/Edit Mouse

Protein disulfide-isomerase A3 (PDIA3), also known as glucose-regulated protein, 58-kD (GRP58), is an isomerase enzyme encoded by the autosomal gene PDIA3 in humans.^[5]^[6]^[7]^[8] This protein localizes to the endoplasmic reticulum (ER) and interacts with lectin chaperones calreticulin and calnexin (CNX) to modulate folding of newly synthesized glycoproteins. It is thought that complexes of lectins and this protein mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates.^[9]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000167004 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000027248 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Symbol report for PDIA3". HGNC. HUGO Gene Nomenclature Committee. Retrieved 7 February 2024.
^ Bourdi M, Demady D, Martin JL, Jabbour SK, Martin BM, George JW, Pohl LR (Nov 1995). "cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase". Archives of Biochemistry and Biophysics. 323 (2): 397–403. doi:10.1006/abbi.1995.0060. PMID 7487104.
^ Hirano N, Shibasaki F, Sakai R, Tanaka T, Nishida J, Yazaki Y, Takenawa T, Hirai H (Nov 1995). "Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation". European Journal of Biochemistry. 234 (1): 336–42. doi:10.1111/j.1432-1033.1995.336_c.x. PMID 8529662.
^ Koivunen P, Helaakoski T, Annunen P, Veijola J, Räisänen S, Pihlajaniemi T, Kivirikko KI (Jun 1996). "ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase". The Biochemical Journal. 316. 316 (2): 599–605. doi:10.1042/bj3160599. PMC 1217390. PMID 8687406.
^ "Entrez Gene: PDIA3 protein disulfide isomerase family A, member 3".

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000167004 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000027248 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] "Symbol report for PDIA3". HGNC. HUGO Gene Nomenclature Committee. Retrieved 7 February 2024.

[pmid7487104-6] Bourdi M, Demady D, Martin JL, Jabbour SK, Martin BM, George JW, Pohl LR (Nov 1995). "cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase". Archives of Biochemistry and Biophysics. 323 (2): 397–403. doi:10.1006/abbi.1995.0060. PMID 7487104.

[pmid8529662-7] Hirano N, Shibasaki F, Sakai R, Tanaka T, Nishida J, Yazaki Y, Takenawa T, Hirai H (Nov 1995). "Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation". European Journal of Biochemistry. 234 (1): 336–42. doi:10.1111/j.1432-1033.1995.336_c.x. PMID 8529662.

[pmid8687406-8] Koivunen P, Helaakoski T, Annunen P, Veijola J, Räisänen S, Pihlajaniemi T, Kivirikko KI (Jun 1996). "ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase". The Biochemical Journal. 316. 316 (2): 599–605. doi:10.1042/bj3160599. PMC 1217390. PMID 8687406.

[entrez-9] "Entrez Gene: PDIA3 protein disulfide isomerase family A, member 3".

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