Protein disulfide isomerase family A member 2 is a
protein that in humans is encoded by the PDIA2gene.[5]
Function
This gene encodes a member of the
disulfide isomerase (PDI) family of
endoplasmic reticulum (ER) proteins that catalyze
protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, two catalytically active
thioredoxin (TRX) domains, two TRX-like domains and a C-terminal ER-retention sequence. The protein plays a role in the folding of nascent proteins in the endoplasmic reticulum by forming
disulfide bonds through its thiol isomerase,
oxidase, and
reductase activity. The encoded protein also possesses estradiol-binding activity and can modulate intracellular
estradiol levels. [provided by RefSeq, Sep 2017].
Clissold PM, Bicknell R (2003). "The thioredoxin-like fold: hidden domains in protein disulfide isomerases and other chaperone proteins". BioEssays. 25 (6): 603–11.
doi:
10.1002/bies.10287.
PMID12766950.
Otsu M, Bertoli G, Fagioli C, Guerini-Rocco E, Nerini-Molteni S, Ruffato E, Sitia R (2006). "Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44". Antioxid. Redox Signal. 8 (3–4): 274–82.
doi:
10.1089/ars.2006.8.274.
PMID16677073.
Protein disulfide isomerase family A member 2 is a
protein that in humans is encoded by the PDIA2gene.[5]
Function
This gene encodes a member of the
disulfide isomerase (PDI) family of
endoplasmic reticulum (ER) proteins that catalyze
protein folding and thiol-disulfide interchange reactions. The encoded protein has an N-terminal ER-signal sequence, two catalytically active
thioredoxin (TRX) domains, two TRX-like domains and a C-terminal ER-retention sequence. The protein plays a role in the folding of nascent proteins in the endoplasmic reticulum by forming
disulfide bonds through its thiol isomerase,
oxidase, and
reductase activity. The encoded protein also possesses estradiol-binding activity and can modulate intracellular
estradiol levels. [provided by RefSeq, Sep 2017].
Clissold PM, Bicknell R (2003). "The thioredoxin-like fold: hidden domains in protein disulfide isomerases and other chaperone proteins". BioEssays. 25 (6): 603–11.
doi:
10.1002/bies.10287.
PMID12766950.
Otsu M, Bertoli G, Fagioli C, Guerini-Rocco E, Nerini-Molteni S, Ruffato E, Sitia R (2006). "Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44". Antioxid. Redox Signal. 8 (3–4): 274–82.
doi:
10.1089/ars.2006.8.274.
PMID16677073.