PDIA2 protein disulfide isomerase family A member 2 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PDIA2provided by HGNC
Official Full Name: protein disulfide isomerase family A member 2provided by HGNC
Primary source: HGNC:HGNC:14180
See related: Ensembl:ENSG00000185615 MIM:608012; AllianceGenome:HGNC:14180
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: PDI; PDA2; PDIP; PDIR
Summary: 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]
Expression: Biased expression in pancreas (RPKM 284.3) and stomach (RPKM 33.5) See more
Orthologs: mouse all
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Genomic context

Location:: 16p13.3

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	16	NC_000016.10 (283164..287215)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	16	NC_060940.1 (278036..282088)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	16	NC_000016.9 (333164..337215)

Chromosome 16 - NC_000016.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

PDIA2 has a dual function in promoting androgen deprivation therapy induced venous thrombosis events and castrate resistant prostate cancer progression.
Title: PDIA2 has a dual function in promoting androgen deprivation therapy induced venous thrombosis events and castrate resistant prostate cancer progression.
Protein Disulfide Isomerase A2 Is Correlated with Immune Infiltrates and Is a Novel Prognostic Biomarker in Glioma Patients.
Title: Protein Disulfide Isomerase A2 Is Correlated with Immune Infiltrates and Is a Novel Prognostic Biomarker in Glioma Patients.
The involvement of PDIA2 gene in the progression of renal cell carcinoma is potentially through regulation of JNK signaling pathway.
Title: The involvement of PDIA2 gene in the progression of renal cell carcinoma is potentially through regulation of JNK signaling pathway.
De-dimerization of PTB is catalyzed by PDI and is involved in the regulation of p53 translation.
Title: De-dimerization of PTB is catalyzed by PDI and is involved in the regulation of p53 translation.
Non-native proteins inhibit the ER oxidoreductin 1 (Ero1)-protein disulfide-isomerase relay when protein folding capacity is exceeded.
Title: Non-native proteins inhibit the ER oxidoreductin 1 (Ero1)-protein disulfide-isomerase relay when protein folding capacity is exceeded.
Galectin-9, a soluble lectin expressed by T cells, endothelial cells and dendritic cells, binds to and retains PDI on the cell surface.
Title: Galectin-9 binds to O-glycans on protein disulfide isomerase.
PDI overexpression is associated with Multiple Myeloma.
Title: Novel Protein Disulfide Isomerase Inhibitor with Anticancer Activity in Multiple Myeloma.
Tissue factor-regulated vascular smooth cell migration and microvessel formation is under the control of the ER-protein PDIA2.
Title: Protein disulphide-isomerase A2 regulated intracellular tissue factor mobilisation in migrating human vascular smooth muscle cells.
It was found that PDI interacts with dengue virus nonstructural protein 1 (NS1) intracellularly as well as on the surface in the lipid raft domain.
Title: Protein disulfide isomerase mediates dengue virus entry in association with lipid rafts.
Data show that cell surface disulfide isomerase (PDI) expression and function regulate the capacity of natriuretic peptides to generate cyclic guanosine monophosphate (cGMP) through interaction with their receptors.
Title: Cell surface protein disulfide isomerase regulates natriuretic peptide generation of cyclic guanosine monophosphate.

Submit: New GeneRIF Correction See all GeneRIFs (60)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Protein interactions

Protein	Gene	Interaction	Pubs
Envelope surface glycoprotein gp120	env	HIV-1 gp120 co-localizes with the endoplasmic reticulum protein PDI in HIV-transfected 293T cells	PubMed
	env	PDI is predominantly involved in HIV-1 entry and infection of the T cell line PM-1 and PHA-stimulated primary T lymphocytes, suggesting the preferential use of PDI relevant to the HIV-1 entry and establishment of virus reservoirs in resting CD4+ cells	PubMed
	env	Protein-disulfide isomerase (PDI) cleaves disulfide bonds in recombinant HIV-1 envelope glycoprotein gp120, and gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors	PubMed
	env	The disulfide cross-linking interaction between gp120 and PDI is enhanced by CD4 protein	PubMed
Envelope surface glycoprotein gp160, precursor	env	HIV-1 gp160 interacts with PDIA2; predicted interaction to be within the endoplasmic reticulum and function as thioredoxin reductase	PubMed
	env	HIV-1 gp160 co-localizes with the endoplasmic reticulum protein PDI in HIV-transfected 293T cells	PubMed
	env	Treatment of trimeric HIV-1 rgp140 with protein disulfide isomerase yields monomers by disruption of the intermolecular disulfide bonds	PubMed
	env	HIV-1 gp160 C1, V1/V2, and the CD4-binding domains are required for its binding to protein-disulfide isomerase (PDI)	PubMed

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

NoName (e-PCR)
- UniSTS:482328

RH11656 (e-PCR)
- UniSTS:67369

REN95374 (e-PCR)
- UniSTS:420172

REN95375 (e-PCR)
- UniSTS:420173

REN95376 (e-PCR)
- UniSTS:420174

REN95377 (e-PCR)
- UniSTS:420175

REN95378 (e-PCR)
- UniSTS:420176

REN95379 (e-PCR)
- UniSTS:420177

REN95380 (e-PCR)
- UniSTS:420178

REN95382 (e-PCR)
- UniSTS:420180

REN95383 (e-PCR)
- UniSTS:420181

REN95384 (e-PCR)
- UniSTS:420182

REN95385 (e-PCR)
- UniSTS:420183

REN95386 (e-PCR)
- UniSTS:420184

REN95387 (e-PCR)
- UniSTS:420185

REN95388 (e-PCR)
- UniSTS:420186

REN95389 (e-PCR)
- UniSTS:420187

REN95390 (e-PCR)
- UniSTS:420188

REN95391 (e-PCR)
- UniSTS:420189

REN95392 (e-PCR)
- UniSTS:420190

REN95393 (e-PCR)
- UniSTS:420191

REN95394 (e-PCR)
- UniSTS:420192

REN95396 (e-PCR)
- UniSTS:420194

REN95397 (e-PCR)
- UniSTS:420195

REN95398 (e-PCR)
- UniSTS:420196

REN95399 (e-PCR)
- UniSTS:420197

REN95400 (e-PCR)
- UniSTS:420198

REN95401 (e-PCR)
- UniSTS:420199

REN95402 (e-PCR)
- UniSTS:420200

REN95403 (e-PCR)
- UniSTS:420201

ECD05777 (e-PCR)
- UniSTS:286839

ECD03496 (e-PCR)
- UniSTS:284578

NoName (e-PCR)
- UniSTS:486820

ECD05568 (e-PCR)
- UniSTS:286631

RH71265 (e-PCR)
- UniSTS:7118

RH44784 (e-PCR)
- UniSTS:28633

NoName (e-PCR)
- UniSTS:481267

ECD02030 (e-PCR)
- UniSTS:283131

ECD07716 (e-PCR)
- UniSTS:288766

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables disulfide oxidoreductase activity	TAS Traceable Author Statement more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
NOT enables protein disulfide isomerase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein disulfide isomerase activity	IEA Inferred from Electronic Annotation more info
enables protein-disulfide reductase activity	IDA Inferred from Direct Assay more info	PubMed
enables steroid binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in platelet aggregation	IEA Inferred from Electronic Annotation more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding in endoplasmic reticulum	TAS Traceable Author Statement more info	PubMed
involved_in protein retention in ER lumen	TAS Traceable Author Statement more info	PubMed
involved_in response to endoplasmic reticulum stress	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
is_active_in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum lumen	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: protein disulfide-isomerase A2

Names: Rho GDP dissociation inhibitor gamma; pancreas-specific protein disulfide isomerase; pancreatic protein disulfide isomerase; protein disulfide isomerase, pancreatic; protein disulfide isomerase-associated 2

NP_006840.2

EC 5.3.4.1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_006849.4 → NP_006840.2 protein disulfide-isomerase A2 precursor

See identical proteins and their annotated locations for NP_006840.2

Status: REVIEWED

Source sequence(s)

Z69667

Consensus CDS

CCDS42089.1

UniProtKB/Swiss-Prot

A6ZJ64, B4DI27, Q13087, Q2WGM4, Q4TT67, Q6B010, Q96KJ6, Q9BW95

UniProtKB/TrEMBL

A4L733

Related

ENSP00000219406.7, ENST00000219406.11

Conserved Domains (5) summary

cd02981
Location:157 → 254

PDI_b_family; Protein Disulfide Isomerase (PDIb) family, redox inactive TRX-like domain b; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family ...

cd02982
Location:259 → 368

PDI_b'_family; Protein Disulfide Isomerase (PDIb') family, redox inactive TRX-like domain b'; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family ...

cd02995
Location:389 → 491

PDI_a_PDI_a'_C; PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein ...

TIGR01130
Location:42 → 497

ER_PDI_fam; protein disulfide isomerase, eukaryotic

cl00388
Location:62 → 151

Thioredoxin_like; Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold