Ppia peptidylprolyl isomerase A [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Ppiaprovided by RGD
Official Full Name: peptidylprolyl isomerase Aprovided by RGD
Primary source: RGD:3372
See related: Ensembl:ENSRNOG00000027864 AllianceGenome:RGD:3372
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: p31; CYCA; CyP-A; p1B15
Summary: Enables cyclosporin A binding activity. Involved in negative regulation of phosphoprotein phosphatase activity. Predicted to be located in cytosol; extracellular region; and nucleus. Predicted to be part of protein-containing complex. Predicted to be active in cytoplasm and intracellular membrane-bounded organelle. Used to study epilepsy. Human ortholog(s) of this gene implicated in cholangiocarcinoma and human immunodeficiency virus infectious disease. Orthologous to human PPIA (peptidylprolyl isomerase A). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in Thymus (RPKM 7555.4), Brain (RPKM 6423.6) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 14q21

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	14	NC_086032.1 (85491223..85496884)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	14	NC_051349.1 (81279292..81282960)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	14	NC_005113.4 (86673775..86677443)

Chromosome 14 - NC_086032.1 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: 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?

Secreted cyclophilin A is non-genotoxic but acts as a tumor promoter.
Title: Secreted cyclophilin A is non-genotoxic but acts as a tumor promoter.
Inhibiting the cyclophilin A-CD147 interaction attenuates aAcute pulmonary embolism -associated RV cardiomyocyte injury and dysfunction by suppressing inflammation.
Title: Inhibition of the cyclophilin A-CD147 interaction attenuates right ventricular injury and dysfunction after acute pulmonary embolism in rats.
the action of Ang II was primarily dependent on the angiotensin type 2 receptor (AT2R), not the type 1 receptor. These results provided an insight into the role of the AT2R signaling pathway in Ang IIinduced myocardial hypertrophy
Title: Angiotensin II upregulates cyclophilin A by enhancing ROS production in rat cardiomyocytes.
ox-LDL-induced CyPA secretion requires vesicle transportation, actin remodeling and ROCK-dependent diphosphorylation of myosin light chains in vascular smooth muscle cells.
Title: Oxidized Low-Density Lipoprotein-Induced Cyclophilin A Secretion Requires ROCK-Dependent Diphosphorylation of Myosin Light Chain.
CypA promotes pancreatic damage by upregulating expression of inflammatory cytokines of acinar cells via the NF-kappaB pathway.
Title: Pancreatic acinar cells-derived cyclophilin A promotes pancreatic damage by activating NF-κB pathway in experimental pancreatitis.
CyPA is an important regulator for AngII-induced ROS generation in VSMC through interaction with p47phox and cell cytoskeleton, which enhances the translocation of p47phox to caveolae.
Title: Cyclophilin A is required for angiotensin II-induced p47phox translocation to caveolae in vascular smooth muscle cells.
Cyclophilin-A and EMMPRIN play roles in the maturation of dental hard tissue and the formation of a molar eruption pathway.
Title: Differential expression of cyclophilin A and EMMPRIN in developing molars of rats.
CyPA is required for Ang II-mediated cardiac hypertrophy by directly potentiating ROS production, stimulating the proliferation and migration of cardiac fibroblasts, and promoting cardiac myocyte hypertrophy.
Title: Cyclophilin A promotes cardiac hypertrophy in apolipoprotein E-deficient mice.
CypA is associated with the inflammatory infiltration and alveolar bone destruction of periodontitis.
Title: Cyclophilin A (CypA) is associated with the inflammatory infiltration and alveolar bone destruction in an experimental periodontitis.

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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

RH125522 (e-PCR)
- UniSTS:162338

Ppia (e-PCR), detects polymorphism
- UniSTS:531290

Ppia (e-PCR), detects polymorphism
- UniSTS:531291

Ppia (e-PCR), detects polymorphism
- UniSTS:186228

Ppi-rs (e-PCR), detects polymorphism
- UniSTS:144251

PMC262691P6 (e-PCR)
- UniSTS:272328

UniSTS:265677 (e-PCR)
- UniSTS:265677

Ppia (e-PCR), detects polymorphism
- UniSTS:265677

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables cyclosporin A binding	IBA Inferred from Biological aspect of Ancestor more info
enables cyclosporin A binding	IDA Inferred from Direct Assay more info	PubMed
enables cyclosporin A binding	ISO Inferred from Sequence Orthology more info
enables heparan sulfate binding	ISO Inferred from Sequence Orthology more info
enables heparan sulfate binding	ISS Inferred from Sequence or Structural Similarity more info
enables integrin binding	ISO Inferred from Sequence Orthology more info
enables integrin binding	ISS Inferred from Sequence or Structural Similarity more info
enables peptidyl-prolyl cis-trans isomerase activity	IBA Inferred from Biological aspect of Ancestor more info
enables peptidyl-prolyl cis-trans isomerase activity	IEA Inferred from Electronic Annotation more info
enables peptidyl-prolyl cis-trans isomerase activity	ISO Inferred from Sequence Orthology more info
enables peptidyl-prolyl cis-trans isomerase activity	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in apoptotic process	IEA Inferred from Electronic Annotation more info
involved_in apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in apoptotic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in cell adhesion molecule production	ISO Inferred from Sequence Orthology more info
involved_in cell adhesion molecule production	ISS Inferred from Sequence or Structural Similarity more info
involved_in cellular response to oxidative stress	ISO Inferred from Sequence Orthology more info
involved_in cellular response to oxidative stress	ISS Inferred from Sequence or Structural Similarity more info
involved_in endothelial cell activation	ISO Inferred from Sequence Orthology more info
involved_in endothelial cell activation	ISS Inferred from Sequence or Structural Similarity more info
involved_in leukocyte chemotaxis	ISO Inferred from Sequence Orthology more info
involved_in leukocyte chemotaxis	ISS Inferred from Sequence or Structural Similarity more info
involved_in lipid droplet organization	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of protein K48-linked ubiquitination	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of protein K48-linked ubiquitination	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of protein phosphorylation	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of protein phosphorylation	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of stress-activated MAPK cascade	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of stress-activated MAPK cascade	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of viral life cycle	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within neuron differentiation	ISO Inferred from Sequence Orthology more info
involved_in neutrophil chemotaxis	ISO Inferred from Sequence Orthology more info
involved_in neutrophil chemotaxis	ISS Inferred from Sequence or Structural Similarity more info
involved_in platelet activation	ISO Inferred from Sequence Orthology more info
involved_in platelet activation	ISS Inferred from Sequence or Structural Similarity more info
involved_in platelet aggregation	ISO Inferred from Sequence Orthology more info
involved_in platelet aggregation	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of MAPK cascade	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of MAPK cascade	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of protein dephosphorylation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of protein dephosphorylation	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of protein phosphorylation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of protein phosphorylation	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of protein secretion	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of viral genome replication	ISO Inferred from Sequence Orthology more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IEA Inferred from Electronic Annotation more info
involved_in protein peptidyl-prolyl isomerization	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of apoptotic signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in regulation of apoptotic signaling pathway	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulation of viral genome replication	ISO Inferred from Sequence Orthology more info
involved_in regulation of viral genome replication	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	ISS Inferred from Sequence or Structural Similarity more info
located_in cytosol	ISS Inferred from Sequence or Structural Similarity more info
located_in extracellular region	IEA Inferred from Electronic Annotation more info
located_in extracellular region	ISO Inferred from Sequence Orthology more info
located_in extracellular region	ISS Inferred from Sequence or Structural Similarity more info
located_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in nucleus	ISS Inferred from Sequence or Structural Similarity more info
part_of protein-containing complex	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: peptidyl-prolyl cis-trans isomerase A

Names: PPIase A; cyclophilin A; cyclosporin A-binding protein; rotamase A

NP_058797.1

EC 5.2.1.8

XP_017454574.2

EC 5.2.1.8

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_017101.1 → NP_058797.1 peptidyl-prolyl cis-trans isomerase A

See identical proteins and their annotated locations for NP_058797.1

Status: PROVISIONAL

Source sequence(s)

M19533

UniProtKB/Swiss-Prot

P10111, P18303, Q5BK98

UniProtKB/TrEMBL

A6IKT9, A6IKU0

Conserved Domains (1) summary

cd01926
Location:4 → 162

cyclophilin_ABH_like; Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding ...