PDIA5 protein disulfide isomerase family A member 5 [Homo sapiens (human)] - Gene

Summary

Official Symbol: PDIA5provided by HGNC
Official Full Name: protein disulfide isomerase family A member 5provided by HGNC
Primary source: HGNC:HGNC:24811
See related: Ensembl:ENSG00000065485 MIM:616942; AllianceGenome:HGNC:24811
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: 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, three catalytically active thioredoxin (TRX) domains, a TRX-like domain, and a C-terminal ER-retention sequence. The N-terminal TRX-like domain is the primary binding site for the major ER chaperone calreticulin and possibly other proteins and substrates as well. Alternative splicing results in multiple protein- and non-protein-coding transcript variants. [provided by RefSeq, Dec 2016]
Expression: Ubiquitous expression in placenta (RPKM 25.8), prostate (RPKM 23.2) and 24 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 3q21.1

Exon count:: 17

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	3	NC_000003.12 (123067025..123162104)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	3	NC_060927.1 (125787101..125882179)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	3	NC_000003.11 (122785872..122880951)

Chromosome 3 - NC_000003.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: 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?

RUNX1-PDIA5 Axis Promotes Malignant Progression of Glioblastoma by Regulating CCAR1 Protein Expression.
Title: RUNX1-PDIA5 Axis Promotes Malignant Progression of Glioblastoma by Regulating CCAR1 Protein Expression.
Pan-Cancer Analysis of the Immunological Role of PDIA5: A Potential Target for Immunotherapy.
Title: Pan-Cancer Analysis of the Immunological Role of PDIA5: A Potential Target for Immunotherapy.
PDIA5 is Correlated With Immune Infiltration and Predicts Poor Prognosis in Gliomas.
Title: PDIA5 is Correlated With Immune Infiltration and Predicts Poor Prognosis in Gliomas.
Data suggest that upon activation of integrins, protein disulfide isomerase (PDI) is released from endothelial cells and forms a disulfide bond complex with alphaVbeta3 integrin.
Title: Contribution of activated beta3 integrin in the PDI release from endothelial cells.
This study demonistrated that Protein disulfide isomerase P5-immunopositive inclusions in patients with Alzheimer's disease.
Title: Protein disulfide isomerase P5-immunopositive inclusions in patients with Alzheimer's disease.
PDIA5 is a key regulator ATF6alpha-mediated cellular functions in cancer.
Title: Endoplasmic reticulum stress-activated transcription factor ATF6α requires the disulfide isomerase PDIA5 to modulate chemoresistance.
protein disulfide isomerase 5 is deregulated in the mucopolysaccharidoses, although the unfolded protein response is not activated
Title: Unfolded protein response is not activated in the mucopolysaccharidoses but protein disulfide isomerase 5 is deregulated.
Protein disulfide isomerases are enzymes that mediate oxidative protein folding in the endoplasmic reticulum.
Title: A structural overview of the PDI family of proteins.
Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)
Title: Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
Three thioredoxin motifs (CXXC) of purified PDIR were found to contribute to its isomerase activity.
Title: Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding.

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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

EBI GWAS Catalog

Description
New gene functions in megakaryopoiesis and platelet formation. EBI GWAS Catalog EBI GWAS CatalogPubMed

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	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	The disulfide cross-linking interaction between gp120 and PDI is enhanced by CD4 protein	PubMed
	env	HIV-1 gp120 is identified to have a physical interaction with protein disulfide isomerase family A, member 5 (PDIA5) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses	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
Envelope surface glycoprotein gp160, precursor	env	Treatment of trimeric HIV-1 rgp140 with protein disulfide isomerase yields monomers by disruption of the intermolecular disulfide bonds	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

SHGC-79570 (e-PCR)
- UniSTS:103690

SHGC-80611 (e-PCR)
- UniSTS:102182

SHGC-111245 (e-PCR)
- UniSTS:168246

sY3084 (e-PCR)
- UniSTS:515126

SHGC-150764 (e-PCR)
- UniSTS:173641

D3S3645 (e-PCR)
- UniSTS:47757

RH71326 (e-PCR)
- UniSTS:73621

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables oxidoreductase activity	TAS Traceable Author Statement more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein disulfide isomerase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein disulfide isomerase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein disulfide isomerase activity	TAS Traceable Author Statement more info	PubMed
enables protein-disulfide reductase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in electron transport chain	TAS Traceable Author Statement more info	PubMed
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IDA Inferred from Direct Assay more info	PubMed
involved_in protein folding	TAS Traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
is_active_in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum lumen	TAS Traceable Author Statement more info	PubMed
located_in endoplasmic reticulum membrane	TAS Traceable Author Statement more info

General protein information

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Preferred Names: protein disulfide-isomerase A5

Names: protein disulfide isomerase-associated 5; protein disulfide isomerase-related protein

NP_006801.1

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_006810.4 → NP_006801.1 protein disulfide-isomerase A5 precursor

See identical proteins and their annotated locations for NP_006801.1

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longer transcript and encodes the functional protein.

Source sequence(s)

BM549365, CA414869, D49490

Consensus CDS

CCDS3020.1

UniProtKB/Swiss-Prot

D3DN95, Q14554, Q9BV43

Related

ENSP00000323313.7, ENST00000316218.12

Conserved Domains (3) summary

cd02997
Location:398 → 501

PDI_a_PDIR; PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved ...

cd03067
Location:28 → 139

PDI_b_PDIR_N; PDIb family, PDIR subfamily, N-terminal TRX-like b domain; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. ...

PTZ00102
Location:168 → 512

PTZ00102; disulphide isomerase; Provisional

RNA

NR_028444.2 RNA Sequence

Status: VALIDATED

Description

Transcript Variant: This variant (2) lacks an internal exon and uses an internal alternate splice site, compared to variant 1. This variant is represented as non-coding because the use of the supported translational start codon, as used in variant 1, renders the transcript a candidate for nonsense-mediated mRNA decay (NMD).

Source sequence(s)

BC001625, BM549365

Related

ENST00000489923.5