Ppia peptidylprolyl isomerase A [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ppiaprovided by MGI
Official Full Name: peptidylprolyl isomerase Aprovided by MGI
Primary source: MGI:MGI:97749
See related: Ensembl:ENSMUSG00000071866 AllianceGenome:MGI:97749
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: Cphn; CypA; SP18; CyP-18
Summary: Enables integrin binding activity and peptidyl-prolyl cis-trans isomerase activity. Involved in platelet aggregation. Acts upstream of or within neuron differentiation. Located in extracellular space. Is expressed in several structures, including early conceptus; gonad; hemolymphoid system gland; liver; and skeletal muscle. 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, Nov 2024]
Expression: Ubiquitous expression in liver E14 (RPKM 1110.7), CNS E11.5 (RPKM 1109.1) and 28 other tissues See more
Orthologs: human all
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Genomic context

Location:: 11 A1; 11 3.97 cM

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	11	NC_000077.7 (6365867..6369817)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	11	NC_000077.6 (6415867..6419817)

Chromosome 11 - NC_000077.7 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: 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?

Inhibition of Cyclophilin A-Metalloproteinase-9 Pathway Alleviates the Development of Neuropathic Pain by Promoting Repair of the Blood-Spinal Cord Barrier.
Title: Inhibition of Cyclophilin A-Metalloproteinase-9 Pathway Alleviates the Development of Neuropathic Pain by Promoting Repair of the Blood-Spinal Cord Barrier.
Intracellular and extracellular Cyclophilin a promote cardiac fibrosis through TGF-beta signaling in response to angiotensin .
Title: Intracellular and extracellular Cyclophilin a promote cardiac fibrosis through TGF-β signaling in response to angiotensin Ⅱ.
High-Mannose-Type Glycan of Basigin in Endothelial Cells Is Essential for the Opening of the Blood-Brain Barrier Induced by Hypoxia, Cyclophilin A, or Tumor Necrosis Factor-alpha.
Title: High-Mannose-Type Glycan of Basigin in Endothelial Cells Is Essential for the Opening of the Blood-Brain Barrier Induced by Hypoxia, Cyclophilin A, or Tumor Necrosis Factor-α.
Mice lacking cyclophilin B, but not cyclophilin A, are protected from the development of NASH in a diet and chemical-induced model.
Title: Mice lacking cyclophilin B, but not cyclophilin A, are protected from the development of NASH in a diet and chemical-induced model.
APOE4 accelerates advanced-stage vascular and neurodegenerative disorder in old Alzheimer's mice via cyclophilin A independently of amyloid-beta.
Title: APOE4 accelerates advanced-stage vascular and neurodegenerative disorder in old Alzheimer's mice via cyclophilin A independently of amyloid-β.
Cyclophilin A Is Not Acetylated at Lysine-82 and Lysine-125 in Resting and Stimulated Platelets.
Title: Cyclophilin A Is Not Acetylated at Lysine-82 and Lysine-125 in Resting and Stimulated Platelets.
Defective cyclophilin A induces TDP-43 proteinopathy: implications for amyotrophic lateral sclerosis and frontotemporal dementia.
Title: Defective cyclophilin A induces TDP-43 proteinopathy: implications for amyotrophic lateral sclerosis and frontotemporal dementia.
Cyclophilin A Impairs Efferocytosis and Accelerates Atherosclerosis by Overexpressing CD 47 and Down-Regulating Calreticulin.
Title: Cyclophilin A Impairs Efferocytosis and Accelerates Atherosclerosis by Overexpressing CD 47 and Down-Regulating Calreticulin.
Ppia is the most stable housekeeping gene for qRT-PCR normalization in kidneys of three Pkd1-deficient mouse models.
Title: Ppia is the most stable housekeeping gene for qRT-PCR normalization in kidneys of three Pkd1-deficient mouse models.
Interleukin 37 (IL-37) Reduces High Glucose-Induced Inflammation, Oxidative Stress, and Apoptosis of Podocytes by Inhibiting the STAT3-Cyclophilin A (CypA) Signaling Pathway.
Title: Interleukin 37 (IL-37) Reduces High Glucose-Induced Inflammation, Oxidative Stress, and Apoptosis of Podocytes by Inhibiting the STAT3-Cyclophilin A (CypA) Signaling Pathway.

Submit: New GeneRIF Correction See all GeneRIFs (49)

Variation

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Alleles

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

Endonuclease-mediated (6)
Targeted (1) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Ppia (e-PCR), detects polymorphism
- UniSTS:158754

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 MGI

Function	Evidence Code	Pubs
enables RNA polymerase II CTD heptapeptide repeat P3 isomerase activity	IEA Inferred from Electronic Annotation more info
enables RNA polymerase II CTD heptapeptide repeat P6 isomerase activity	IEA Inferred from Electronic Annotation more info
enables cyclosporin A binding	IBA Inferred from Biological aspect of Ancestor more info
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	IDA Inferred from Direct Assay more info	PubMed
enables peptidyl-prolyl cis-trans isomerase activity	IBA Inferred from Biological aspect of Ancestor more info
enables peptidyl-prolyl cis-trans isomerase activity	IMP Inferred from Mutant Phenotype more info	PubMed
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
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in activation of protein kinase B activity	ISO Inferred from Sequence Orthology more info
involved_in activation of protein kinase B activity	ISS Inferred from Sequence or Structural Similarity 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	IEA Inferred from Electronic Annotation 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 kinase activity	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of protein kinase activity	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	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of viral life cycle	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within neuron differentiation	IMP Inferred from Mutant Phenotype more info	PubMed
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	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in platelet aggregation	IMP Inferred from Mutant Phenotype more info	PubMed
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 NF-kappaB transcription factor activity	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of NF-kappaB transcription factor activity	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	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of protein secretion	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of viral genome replication	IEA Inferred from Electronic Annotation 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	ISO Inferred from Sequence Orthology more info
involved_in protein peptidyl-prolyl isomerization	ISS Inferred from Sequence or Structural Similarity 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 transcription by RNA polymerase II	IEA Inferred from Electronic Annotation 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	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	ISO Inferred from Sequence Orthology more info
located_in extracellular region	ISS Inferred from Sequence or Structural Similarity more info
located_in extracellular space	HDA more info	PubMed
located_in extracellular space	IDA Inferred from Direct Assay more info	PubMed
located_in myelin sheath	HDA more info	PubMed
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	IEA Inferred from Electronic Annotation 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_032933.1

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_008907.2 → NP_032933.1 peptidyl-prolyl cis-trans isomerase A

See identical proteins and their annotated locations for NP_032933.1

Status: VALIDATED

Source sequence(s)

AK160780

Consensus CDS

CCDS24419.1

UniProtKB/Swiss-Prot

P17742, Q9CWJ5, Q9R137

UniProtKB/TrEMBL

Q3TE63, Q3UAJ1, Q5SVY2

Related

ENSMUSP00000117987.2, ENSMUST00000132846.2

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 ...