Peptidylprolyl isomerase F

mammalian protein found in Rattus norvegicus
Protein protein Q28560058
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Peptidylprolyl isomerase F

Summary

Peptidylprolyl isomerase F is a protein[1].

Key Facts

  • Peptidylprolyl isomerase F's instance of is recorded as protein[2].
  • Peptidylprolyl isomerase F's subclass of is recorded as protein[3].
  • Peptidylprolyl isomerase F's UniProt protein ID is recorded as P29117[4].
  • Peptidylprolyl isomerase F's part of is recorded as cyclophilin[5].
  • Peptidylprolyl isomerase F's part of is recorded as Cyclophilin-like domain superfamily[6].
  • Peptidylprolyl isomerase F's part of is recorded as Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain, protein family[7].
  • Peptidylprolyl isomerase F's part of is recorded as Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site, protein family[8].
  • Peptidylprolyl isomerase F's has part is recorded as Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain[9].
  • Peptidylprolyl isomerase F's has part is recorded as Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site[10].
  • Peptidylprolyl isomerase F's RefSeq protein ID is recorded as NP_758443[11].
  • Peptidylprolyl isomerase F's molecular function is recorded as peptidyl-prolyl cis-trans isomerase activity[12].
  • Peptidylprolyl isomerase F's molecular function is recorded as protein binding[13].
  • Peptidylprolyl isomerase F's molecular function is recorded as cyclosporin A binding[14].
  • Peptidylprolyl isomerase F's molecular function is recorded as isomerase activity[15].
  • Peptidylprolyl isomerase F's molecular function is recorded as peptide binding[16].
  • Peptidylprolyl isomerase F's molecular function is recorded as unfolded protein binding[17].
  • Peptidylprolyl isomerase F's cell component is recorded as mitochondrion[18].
  • Peptidylprolyl isomerase F's cell component is recorded as mitochondrial inner membrane[19].
  • Peptidylprolyl isomerase F's cell component is recorded as mitochondrial proton-transporting ATP synthase complex[20].
  • Peptidylprolyl isomerase F's cell component is recorded as mitochondrial permeability transition pore complex[21].
  • Peptidylprolyl isomerase F's cell component is recorded as mitochondrial matrix[22].
  • Peptidylprolyl isomerase F's biological process is recorded as protein peptidyl-prolyl isomerization[23].
  • Peptidylprolyl isomerase F's biological process is recorded as response to ischemia[24].
  • Peptidylprolyl isomerase F's biological process is recorded as protein folding[25].
  • Peptidylprolyl isomerase F's biological process is recorded as apoptotic process[26].

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [2] . Q905695. Retrieved . wikidata.org.
  2. [3] . Q905695. Retrieved . wikidata.org.
  3. [4] . Q905695. Retrieved . wikidata.org.
  4. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] . wikidata.org.
  7. [8] . wikidata.org.
  8. [9] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . Q20641742. Retrieved . wikidata.org.
  11. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . Cyclophilin-D promotes the mitochondrial permeability transition but has opposite effects on apoptosis and necrosis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] . Wikidata. wikidata.org.

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Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Peptidylprolyl isomerase F. Retrieved May 3, 2026, from https://4ort.xyz/entity/peptidylprolyl-isomerase-f-q28560058
MLA “Peptidylprolyl isomerase F.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/peptidylprolyl-isomerase-f-q28560058.
BibTeX @misc{4ortxyz_peptidylprolyl-isomerase-f-q28560058_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Peptidylprolyl isomerase F}}, year = {2026}, url = {https://4ort.xyz/entity/peptidylprolyl-isomerase-f-q28560058}, note = {Accessed: 2026-05-03}}
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