Ppid peptidylprolyl isomerase D [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Ppidprovided by RGD
Official Full Name: peptidylprolyl isomerase Dprovided by RGD
Primary source: RGD:1303174
See related: EnsemblRapid:ENSRNOG00000027408 AllianceGenome:RGD:1303174
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: CypD; Cyp-40
Summary: Enables cyclosporin A binding activity; enzyme binding activity; and peptidyl-prolyl cis-trans isomerase activity. Involved in several processes, including protein peptidyl-prolyl isomerization; regulation of mitochondrial membrane potential; and response to oxidative stress. Predicted to be located in nucleolus and nucleoplasm. Predicted to be active in cytosol. Orthologous to human PPID (peptidylprolyl isomerase D). [provided by Alliance of Genome Resources, Dec 2024]
Annotation information: Note: This gene encodes a 370 aa protein that is found in the cytoplasm. In some databases, it has been labeled incorrectly as 'cyclophilin D'. This same name has also been applied to a different protein, found in the mitochondrion, which is represented by GeneID 282819, Ppif. [13 Feb 2013]
Expression: Biased expression in Thymus (RPKM 324.9), Brain (RPKM 259.9) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 2q33

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	2	NC_086020.1 (167025985..167037998)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	2	NC_051337.1 (164727803..164740168)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	2	NC_005101.4 (178354830..178366843)

Chromosome 2 - NC_086020.1 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

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

In cardiomyocytes the protective effects of metformin-induced AMPK activation against oxidative stress converge on mitochondria and are mediated, at least in part, through the dissociation of PPARalpha-CypD interactions.
Title: The beneficial effects of AMP kinase activation against oxidative stress are associated with prevention of PPARα-cyclophilin D interaction in cardiomyocytes.
Ppid expression was predicted by plasma estradiol & 34% lower in control adolescent females than males. After chronic adolescent stress, females had elevated hippocampal Ppid expression that was not seen in males.
Title: Glucocorticoid sensitizers Bag1 and Ppid are regulated by adolescent stress in a sex-dependent manner.
NIM811 attenuates liver fibrosis in a CCl(4)-induced rat liver fibrosis model, which may be related to binding with cyclophilin B and D.
Title: N-methyl-4-isoleucine cyclosporine attenuates CCl -induced liver fibrosis in rats by interacting with cyclophilin B and D.

Submit: New GeneRIF Correction

General gene information

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Markers

RH128961 (e-PCR)
- UniSTS:212269

BE106923 (e-PCR)
- UniSTS:246471

Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables Hsp70 protein binding	ISS Inferred from Sequence or Structural Similarity more info
enables Hsp90 protein binding	ISO Inferred from Sequence Orthology more info
enables Hsp90 protein binding	ISS Inferred from Sequence or Structural Similarity more info
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	IDA Inferred from Direct Assay more info
enables enzyme binding	IPI Inferred from Physical Interaction more info	PubMed
enables heat shock protein binding	ISO Inferred from Sequence Orthology more info
enables nuclear estrogen receptor 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	IDA Inferred from Direct Assay 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 protein binding	IPI Inferred from Physical Interaction more info

Process	Evidence Code	Pubs
involved_in apoptotic process	IEA Inferred from Electronic Annotation more info
involved_in cellular response to UV-A	ISO Inferred from Sequence Orthology more info
involved_in cellular response to UV-A	ISS Inferred from Sequence or Structural Similarity more info
involved_in chaperone-mediated protein folding	ISO Inferred from Sequence Orthology more info
involved_in chaperone-mediated protein folding	ISS Inferred from Sequence or Structural Similarity more info
involved_in lipid droplet organization	ISO Inferred from Sequence Orthology more info
involved_in lipid droplet organization	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of apoptotic process	IMP Inferred from Mutant Phenotype more info
involved_in negative regulation of transcription by RNA polymerase II	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of transcription by RNA polymerase II	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of apoptotic process	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 folding	ISS Inferred from Sequence or Structural Similarity more info
involved_in protein peptidyl-prolyl isomerization	IDA Inferred from Direct Assay more info
involved_in protein transport	IEA Inferred from Electronic Annotation more info
involved_in protein-containing complex assembly	ISO Inferred from Sequence Orthology more info
involved_in protein-containing complex assembly	ISS Inferred from Sequence or Structural Similarity more info
involved_in regulation of mitochondrial membrane potential	IMP Inferred from Mutant Phenotype more info
involved_in response to oxidative stress	IMP Inferred from Mutant Phenotype 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
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in nucleolus	ISO Inferred from Sequence Orthology more info
located_in nucleolus	ISS Inferred from Sequence or Structural Similarity more info
located_in nucleoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	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

General protein information

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Preferred Names: peptidyl-prolyl cis-trans isomerase D

Names: 40 kDa peptidyl-prolyl cis-trans isomerase; Cyclophilin D; PPIase D; cyclophilin-40; rotamase D

NP_001004279.1

EC 5.2.1.8

XP_063138186.1

EC 5.2.1.8

XP_063138187.1

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_001004279.1 → NP_001004279.1 peptidyl-prolyl cis-trans isomerase D

See identical proteins and their annotated locations for NP_001004279.1

Status: PROVISIONAL

Source sequence(s)

BC076386

UniProtKB/Swiss-Prot

Q6DGG0

UniProtKB/TrEMBL

A0A8I6GKS0

Related

ENSRNOP00000093695.2, ENSRNOT00000097015.2

Conserved Domains (3) summary

cd01926
Location:16 → 182

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 ...

TIGR00990
Location:192 → 330

3a0801s09; mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70)

sd00006
Location:223 → 251

TPR; TPR repeat [structural motif]

RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCr8

Genomic

NC_086020.1 Reference GRCr8

Range

167025985..167037998

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_063282116.1 → XP_063138186.1 peptidyl-prolyl cis-trans isomerase D isoform X1

UniProtKB/TrEMBL

A6J5S1
XM_063282117.1 → XP_063138187.1 peptidyl-prolyl cis-trans isomerase D isoform X1

UniProtKB/TrEMBL

A6J5S1