P4hb prolyl 4-hydroxylase, beta polypeptide [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: P4hbprovided by MGI
Official Full Name: prolyl 4-hydroxylase, beta polypeptideprovided by MGI
Primary source: MGI:MGI:97464
See related: Ensembl:ENSMUSG00000025130 AllianceGenome:MGI:97464
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: PDI; Thbp; ERp59; Pdia1
Summary: Enables integrin binding activity. Acts upstream of or within cellular response to interleukin-7. Located in endoplasmic reticulum and external side of plasma membrane. Part of endoplasmic reticulum chaperone complex. Is expressed in several structures, including alimentary system; central nervous system; genitourinary system; heart; and sensory organ. Human ortholog(s) of this gene implicated in Cole-Carpenter syndrome. Orthologous to human P4HB (prolyl 4-hydroxylase subunit beta). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Ubiquitous expression in placenta adult (RPKM 477.0), liver adult (RPKM 327.1) and 27 other tissues See more
Orthologs: human all
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Genomic context

Location:: 11 E2; 11 84.27 cM

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	11	NC_000077.7 (120451124..120464079, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	11	NC_000077.6 (120560298..120573253, complement)

Chromosome 11 - NC_000077.7 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: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Conditional hepatocyte ablation of PDIA1 uncovers indispensable roles in both APOB and MTTP folding to support VLDL secretion.
Title: Conditional hepatocyte ablation of PDIA1 uncovers indispensable roles in both APOB and MTTP folding to support VLDL secretion.
Protein disulfide isomerase A1 as a novel redox sensor in VEGFR2 signaling and angiogenesis.
Title: Protein disulfide isomerase A1 as a novel redox sensor in VEGFR2 signaling and angiogenesis.
A discovery-based proteomics approach identifies protein disulphide isomerase (PDIA1) as a biomarker of beta cell stress in type 1 diabetes.
Title: A discovery-based proteomics approach identifies protein disulphide isomerase (PDIA1) as a biomarker of β cell stress in type 1 diabetes.
PDIA1 acts as master organizer of NOX1/NOX4 balance and phenotype response in vascular smooth muscle.
Title: PDIA1 acts as master organizer of NOX1/NOX4 balance and phenotype response in vascular smooth muscle.
findings demonstrate that protein disulfide isomerase A1 (PDIA1/P4HB) contributes to oxidative maturation of proinsulin in the endoplasmic reticulum (ER) to support insulin production and ss cell health.
Title: PDIA1/P4HB is required for efficient proinsulin maturation and ß cell health in response to diet induced obesity.
this study uncovers a molecular link between PDIA1 and Drp1 oxidoreduction.
Title: Redox Regulation of Mitochondrial Fission Protein Drp1 by Protein Disulfide Isomerase Limits Endothelial Senescence.
these results suggest that overexpression of PDI may protect transplanted cells from hypoxia and other possibly occurring endoplasmic reticulum stresses, and consequently enhance their regenerative properties.
Title: Protein disulfide isomerase as a prosurvival factor in cell therapy for muscular and vascular diseases.
Neutrophil surface PDI is important for alphaMbeta2 integrin-mediated adhesion of human neutrophils under shear and static conditions and for binding of soluble fibrinogen to activated alphaMbeta2 integrin.
Title: Extracellular protein disulfide isomerase regulates ligand-binding activity of αMβ2 integrin and neutrophil recruitment during vascular inflammation.
Unfolded protein response caused by protein misfolding, may lead to PDI-dependent NOX activation and contribute to neurotoxicity in neurodegenerative diseases including ALS.
Title: Protein disulfide isomerase in ALS mouse glia links protein misfolding with NADPH oxidase-catalyzed superoxide production.
These results indicate that both endothelial and platelet beta3 integrins contribute to extracellular PDI binding at the vascular injury site.
Title: Protein disulfide isomerase capture during thrombus formation in vivo depends on the presence of β3 integrins.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Gene trapped (1)
Targeted (4) 1 citation
Endonuclease-mediated (5)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Pdia3 (e-PCR), detects polymorphism
- UniSTS:470674

P4hb (e-PCR), detects polymorphism
- UniSTS:144111

NoName (e-PCR)
- UniSTS:236789

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables actin binding	ISO Inferred from Sequence Orthology more info
enables enzyme binding	ISO Inferred from Sequence Orthology more info
enables integrin binding	IPI Inferred from Physical Interaction more info	PubMed
enables integrin binding	ISO Inferred from Sequence Orthology more info
enables isomerase activity	IEA Inferred from Electronic Annotation more info
contributes_to procollagen-proline 4-dioxygenase activity	ISO Inferred from Sequence Orthology more info
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	ISO Inferred from Sequence Orthology more info
enables protein heterodimerization activity	ISO Inferred from Sequence Orthology more info
enables protein-containing complex binding	ISO Inferred from Sequence Orthology more info
enables protein-disulfide reductase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables protein-disulfide reductase activity	ISO Inferred from Sequence Orthology more info
enables thiol oxidase activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in cellular response to hypoxia	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within cellular response to interleukin-7	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_positive_effect endoplasmic reticulum to Golgi vesicle-mediated transport	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in insulin processing	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within peptidyl-proline hydroxylation to 4-hydroxy-L-proline	ISO Inferred from Sequence Orthology more info	PubMed
involved_in positive regulation of cell adhesion	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of substrate adhesion-dependent cell spreading	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of viral entry into host cell	ISO Inferred from Sequence Orthology more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
involved_in regulation of oxidative stress-induced intrinsic apoptotic signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in response to endoplasmic reticulum stress	IBA Inferred from Biological aspect of Ancestor more info
involved_in response to endoplasmic reticulum stress	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in cytoskeleton	ISO Inferred from Sequence Orthology more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
is_active_in endoplasmic reticulum	IBA Inferred from Biological aspect of Ancestor more info
located_in endoplasmic reticulum	IDA Inferred from Direct Assay more info	PubMed
located_in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info	PubMed
part_of endoplasmic reticulum chaperone complex	IDA Inferred from Direct Assay more info	PubMed
is_active_in endoplasmic reticulum lumen	IMP Inferred from Mutant Phenotype more info	PubMed
located_in endoplasmic reticulum-Golgi intermediate compartment	ISO Inferred from Sequence Orthology more info
is_active_in external side of plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in external side of plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in external side of plasma membrane	ISO Inferred from Sequence Orthology more info
located_in lamellipodium	ISO Inferred from Sequence Orthology more info
located_in membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
part_of procollagen-proline 4-dioxygenase complex	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: protein disulfide-isomerase

Names: ER protein 59; cellular thyroid hormone-binding protein; endoplasmic reticulum resident protein 59; p55; prolyl 4-hydroxylase subunit beta

NP_035162.1

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_011032.3 → NP_035162.1 protein disulfide-isomerase precursor

See identical proteins and their annotated locations for NP_035162.1

Status: VALIDATED

Source sequence(s)

AK159606, BP766087, CA317831

Consensus CDS

CCDS25742.1

UniProtKB/Swiss-Prot

P09103, Q922C8

UniProtKB/TrEMBL

Q3TF72, Q3TGS0, Q3THC3, Q3TIM0, Q3TWE3, Q3UA23, Q3UBY9, Q3UJA8, Q3URP6

Related

ENSMUSP00000026122.5, ENSMUST00000026122.11

Conserved Domains (5) summary

cd02981
Location:139 → 234

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:246 → 349

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:370 → 472

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:26 → 476

ER_PDI_fam; protein disulfide isomerase, eukaryotic

cl00388
Location:31 → 135

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