PDIA3

Protein disulfide isomerase family A, member 3
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsPDIA3 ; ER60; ERp57; ERp60; ERp61; GRP57; GRP58; HEL-S-269; HEL-S-93n; HsT17083; P58; PI-PLC
External IDsOMIM: 602046 HomoloGene: 68454 GeneCards: PDIA3 Gene
EC number5.3.4.1
Orthologs
SpeciesHumanMouse
Entrez292314827
EnsemblENSG00000167004ENSMUSG00000027248
UniProtP30101P27773
RefSeq (mRNA)NM_005313NM_007952
RefSeq (protein)NP_005304NP_031978
Location (UCSC)Chr 15:
43.75 – 43.77 Mb		Chr 2:
121.41 – 121.44 Mb
PubMed search

Protein disulfide-isomerase A3 (PDIA3) also known as glucose-regulated protein, 58-kD (GRP58) is an isomerase enzyme.[1][2][3]

Function

The PDIA3 protein has protein disulfide isomerase activity.[3] PDIA3 is also part of the major histocompatibility complex (MHC) class I peptide-loading complex, which is essential for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.[4] This protein of the endoplasmic reticulum interacts with lectin chaperones such as calreticulin and calnexin in order to modulate the folding of proteins that are newly synthesized. It is believed that PDIA3 plays a role in protein folding by promoting the formation of disulfide bonds.

Interactions

It has been demonstrated that PDIA3 interacts with BACE1, CRT and CNX.[5]

Clinical significance

It has been demonstrated that the downregulation of ERp57 expression is correlated with poor prognosis in early-stage cervical cancer.[6] It has also been demonstrated that ERp57/PDIA3 binds specific DNA fragments in a melanoma cell line.[7]

See also

References

  1. ↑ Bourdi M, Demady D, Martin JL, Jabbour SK, Martin BM, George JW et al. (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.
  2. ↑ Hirano N, Shibasaki F, Sakai R, Tanaka T, Nishida J, Yazaki Y et al. (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 / FEBS 234 (1): 336–42. doi:10.1111/j.1432-1033.1995.336_c.x. PMID 8529662.
  3. ↑ 3.0 3.1 Koivunen P, Helaakoski T, Annunen P, Veijola J, Räisänen S, Pihlajaniemi T et al. (Jun 1996). "ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase". The Biochemical Journal. 316. 316 ( Pt 2): 599–605. PMC 1217390. PMID 8687406.
  4. ↑ Garbi N, Tanaka S, Momburg F, Hämmerling GJ (Jan 2006). "Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57". Nature Immunology 7 (1): 93–102. doi:10.1038/ni1288. PMID 16311600.
  5. ↑ Leach MR, Cohen-Doyle MF, Thomas DY, Williams DB (Aug 2002). "Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin". The Journal of Biological Chemistry 277 (33). doi:10.1074/jbc.M202405200. PMID 12052826.
  6. ↑ Chung H, Cho H, Perry C, Song J, Ylaya K, Lee H et al. (Nov 2013). "Downregulation of ERp57 expression is associated with poor prognosis in early-stage cervical cancer". Biomarkers 18 (7). doi:10.3109/1354750X.2013.827742. PMID 23957851.
  7. ↑ Aureli C, Gaucci E, Arcangeli V, Grillo C, Eufemi M, Chichiarelli S (Jul 2013). "ERp57/PDIA3 binds specific DNA fragments in a melanoma cell line". Gene 524 (2). doi:10.1016/j.gene.2013.04.004. PMID 23587917.

External links