P4hb prolyl 4-hydroxylase subunit beta [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: P4hbprovided by RGD
Official Full Name: prolyl 4-hydroxylase subunit betaprovided by RGD
Primary source: RGD:3244
See related: Ensembl:ENSRNOG00000036689 AllianceGenome:RGD:3244
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: PDI; PDIR
Summary: Enables enzyme binding activity and protein disulfide isomerase activity. Predicted to be involved in several processes, including positive regulation of substrate adhesion-dependent cell spreading; positive regulation of viral entry into host cell; and protein folding in endoplasmic reticulum. Predicted to act upstream of or within cellular response to interleukin-7 and peptidyl-proline hydroxylation to 4-hydroxy-L-proline. Predicted to be located in several cellular components, including cytosol; endoplasmic reticulum-Golgi intermediate compartment; and lamellipodium. Predicted to be part of endoplasmic reticulum chaperone complex and procollagen-proline 4-dioxygenase complex. Predicted to be active in endoplasmic reticulum and external side of plasma membrane. 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: Biased expression in Liver (RPKM 4265.2), Kidney (RPKM 1696.5) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 10q32.3

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	10	NC_086028.1 (106335300..106346911, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	10	NC_051345.1 (105836972..105848583, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	10	NC_005109.4 (109736459..109748070, complement)

Chromosome 10 - NC_086028.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

PDI knockdown inhibited the reduction of disulfide bonds on NMDAR subunits, resulting in decreased seizure susceptibility in response to PILO.
Title: PDI regulates seizure activity via NMDA receptor redox in rats.
As the XBP-1/PDI/MTP axis has been suggested to represent a significant lipogenic mechanism in the liver response to ER stress, our data indicate that hypertriglyceridemia and liver steatosis occurring MSG rats are associated with increased MTP.
Title: Mechanisms underlying hypertriglyceridemia in rats with monosodium L-glutamate-induced obesity: evidence of XBP-1/PDI/MTP axis activation.
space group of the native bb' crystals of protein disulfide isomerase was found to be C222, with unit-cell parameters a = 94.8, b = 114.9, c = 182.9 A
Title: Crystallization and preliminary crystallographic analysis of the complex between triiodothyronine and the bb' fragment of rat protein disulfide isomerase.
Butylphthalide improves the learning and memory abilities of rats with experimental Alzheimer's disease, the mechanism of which may involve inhibition of P53 expression and enhancement of PDI expression in the brain tissues.
Title: [Butylphthalide improves learning and memory abilities of rats with Alzheimer's disease possibly by enhancing protein disulfide isomerase and inhibiting P53 expressions].
phenolic compounds specifically bind to PDI and inhibit isomerase activity
Title: Interaction between bisphenol derivatives and protein disulphide isomerase (PDI) and inhibition of PDI functions: requirement of chemical structure for binding to PDI.
Over-expression of PDI suppressed GH mRNA expression and GH release, suggesting that PDI modulates the T3-induced gene expression.
Title: Over-expression of protein disulfide isomerase reduces the release of growth hormone induced by bisphenol A and/or T3.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables actin binding	ISO Inferred from Sequence Orthology more info
enables enzyme binding	IPI Inferred from Physical Interaction more info	PubMed
enables integrin binding	ISO Inferred from Sequence Orthology more info
contributes_to procollagen-proline 4-dioxygenase activity	ISO Inferred from Sequence Orthology more info
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 isomerase activity	IMP Inferred from Mutant Phenotype more info	PubMed
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	IPI Inferred from Physical Interaction 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	ISO Inferred from Sequence Orthology more info
acts_upstream_of_positive_effect endoplasmic reticulum to Golgi vesicle-mediated transport	ISO Inferred from Sequence Orthology more info
involved_in insulin processing	ISO Inferred from Sequence Orthology more info
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
is_active_in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
located_in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
located_in endoplasmic reticulum	ISS Inferred from Sequence or Structural Similarity more info
part_of endoplasmic reticulum chaperone complex	ISO Inferred from Sequence Orthology more info
located_in endoplasmic reticulum lumen	IEA Inferred from Electronic Annotation more info
is_active_in endoplasmic reticulum lumen	ISO Inferred from Sequence Orthology more info
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	ISO Inferred from Sequence Orthology more info
located_in lamellipodium	ISO Inferred from Sequence Orthology more info
located_in melanosome	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: Protein disulfide isomerase (Prolyl 4-hydroxylase, beta polypeptide); cellular thyroid hormone-binding protein; prolyl 4-hydroxylase, beta polypeptide

NP_037130.2

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.