PPIF information

PPIF
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2BIT, 2BIU, 2Z6W, 3QYU, 3R49, 3R4G, 3R54, 3R56, 3R57, 3R59, 3RCF, 3RCG, 3RCI, 3RCK, 3RCL, 3RD9, 3RDA, 3RDB, 3RDC, 4J58, 4J59, 4J5A, 4J5B, 4J5C, 4J5D, 4J5E, 4O8H, 4O8I, 4XNC, 4ZSC, 4ZSD, 5A0E, 5CCS, 5CCN, 5CCQ, 5CBT, 5CCR
Identifiers
Aliases	PPIF, CYP3, CyP-M, Cyp-D, CypD, peptidylprolyl isomerase F
External IDs	OMIM: 604486 MGI: 2145814 HomoloGene: 38696 GeneCards: PPIF
Gene location (Human)
Chr.	Chromosome 10 (human)
End	79,355,334 bp
Gene location (Mouse)
Chr.	Chromosome 14 (mouse)
End	25,700,892 bp
RNA expression pattern
	Top expressed in
	amniotic fluid; ; left adrenal gland; ; periodontal fiber; ; body of tongue; ; right lobe of liver; ; left ventricle; ; monocyte; ; body of pancreas; ; body of stomach; ; gastrocnemius muscle;
	Top expressed in
	pyloric antrum; ; interventricular septum; ; right ventricle; ; myocardium of ventricle; ; cardiac muscles; ; epithelium of stomach; ; lip; ; mucous cell of stomach; ; atrium; ; thoracic diaphragm;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	peptide binding; isomerase activity; protein binding; peptidyl-prolyl cis-trans isomerase activity; cyclosporin A binding; unfolded protein binding;
Cellular component	mitochondrial proton-transporting ATP synthase complex; membrane; mitochondrial inner membrane; mitochondrion; mitochondrial matrix; mitochondrial permeability transition pore complex;
Biological process	regulation of apoptotic process; cellular response to calcium ion; programmed cell death; negative regulation of intrinsic apoptotic signaling pathway; negative regulation of ATP-dependent activity; negative regulation of release of cytochrome c from mitochondria; negative regulation of apoptotic process; response to oxidative stress; regulation of necrotic cell death; regulation of mitochondrial membrane permeability involved in programmed necrotic cell death; response to ischemia; protein folding; cellular response to arsenic-containing substance; negative regulation of oxidative phosphorylation uncoupler activity; regulation of proton-transporting ATPase activity, rotational mechanism; positive regulation of release of cytochrome c from mitochondria; necroptosis; negative regulation of oxidative phosphorylation; cellular response to hydrogen peroxide; apoptotic process; apoptotic mitochondrial changes; regulation of mitochondrial membrane permeability; mitochondrial outer membrane permeabilization involved in programmed cell death; protein peptidyl-prolyl isomerization; protein refolding;
	Sources:Amigo / QuickGO
Orthologs
	10105
	105675
	ENSG00000108179
	ENSMUSG00000021868
	P30405
	Q99KR7
	NM_005729
	NM_134084
	NP_005720
	NP_598845
	Wikidata
View/Edit Human	View/Edit Mouse

Peptidyl-prolyl cis-trans isomerase, mitochondrial (PPIF) is an enzyme that in humans is encoded by the PPIF gene. It has also been referred to as, but should not be confused with, cyclophilin D (CypD), which is encoded by the PPID gene.^[5]^[6] As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins.^[6] PPIF is a major component of the mitochondrial permeability transition pore (MPTP) and, thus, highly involved in mitochondrial metabolism and apoptosis, as well as in mitochondrial diseases and related conditions, including cardiac diseases, neurodegenerative diseases, and muscular dystrophy.^[7] In addition, PPIF participates in inflammation, as well as in ischemic reperfusion injury, AIDS, and cancer.^[8]^[9]^[10]^[11]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000108179 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000021868 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Bergsma DJ, Eder C, Gross M, Kersten H, Sylvester D, Appelbaum E, Cusimano D, Livi GP, McLaughlin MM, Kasyan K (Dec 1991). "The cyclophilin multigene family of peptidyl-prolyl isomerases. Characterization of three separate human isoforms". The Journal of Biological Chemistry. 266 (34): 23204–14. doi:10.1016/S0021-9258(18)54484-7. PMID 1744118.
^ ^a ^b "Entrez Gene: PPIF peptidylprolyl isomerase F (cyclophilin F)".
^ Hansson MJ, Morota S, Chen L, Matsuyama N, Suzuki Y, Nakajima S, Tanoue T, Omi A, Shibasaki F, Shimazu M, Ikeda Y, Uchino H, Elmér E (Jan 2011). "Cyclophilin D-sensitive mitochondrial permeability transition in adult human brain and liver mitochondria". Journal of Neurotrauma. 28 (1): 143–53. doi:10.1089/neu.2010.1613. PMC 3025768. PMID 21121808.
^ Kazui T, Inoue N, Yamada O, Komatsu S (Jan 1992). "Selective cerebral perfusion during operation for aneurysms of the aortic arch: a reassessment". The Annals of Thoracic Surgery. 53 (1): 109–14. doi:10.1016/0003-4975(92)90767-x. PMID 1530810.
^ Yao Q, Li M, Yang H, Chai H, Fisher W, Chen C (Mar 2005). "Roles of cyclophilins in cancers and other organ systems". World Journal of Surgery. 29 (3): 276–80. doi:10.1007/s00268-004-7812-7. PMID 15706440. S2CID 11678319.
^ Wang T, Yun CH, Gu SY, Chang WR, Liang DC (Aug 2005). "1.88 A crystal structure of the C domain of hCyP33: a novel domain of peptidyl-prolyl cis-trans isomerase". Biochemical and Biophysical Research Communications. 333 (3): 845–9. doi:10.1016/j.bbrc.2005.06.006. PMID 15963461.
^ Stocki P, Chapman DC, Beach LA, Williams DB (Aug 2014). "Depletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasis". The Journal of Biological Chemistry. 289 (33): 23086–96. doi:10.1074/jbc.M114.570911. PMC 4132807. PMID 24990953.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000108179 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021868 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1744118-5] Bergsma DJ, Eder C, Gross M, Kersten H, Sylvester D, Appelbaum E, Cusimano D, Livi GP, McLaughlin MM, Kasyan K (Dec 1991). "The cyclophilin multigene family of peptidyl-prolyl isomerases. Characterization of three separate human isoforms". The Journal of Biological Chemistry. 266 (34): 23204–14. doi:10.1016/S0021-9258(18)54484-7. PMID 1744118.

[entrez-6] "Entrez Gene: PPIF peptidylprolyl isomerase F (cyclophilin F)".

[pmid21121808-7] Hansson MJ, Morota S, Chen L, Matsuyama N, Suzuki Y, Nakajima S, Tanoue T, Omi A, Shibasaki F, Shimazu M, Ikeda Y, Uchino H, Elmér E (Jan 2011). "Cyclophilin D-sensitive mitochondrial permeability transition in adult human brain and liver mitochondria". Journal of Neurotrauma. 28 (1): 143–53. doi:10.1089/neu.2010.1613. PMC 3025768. PMID 21121808.

[pmid1530810-8] Kazui T, Inoue N, Yamada O, Komatsu S (Jan 1992). "Selective cerebral perfusion during operation for aneurysms of the aortic arch: a reassessment". The Annals of Thoracic Surgery. 53 (1): 109–14. doi:10.1016/0003-4975(92)90767-x. PMID 1530810.

[pmid15706440-9] Yao Q, Li M, Yang H, Chai H, Fisher W, Chen C (Mar 2005). "Roles of cyclophilins in cancers and other organ systems". World Journal of Surgery. 29 (3): 276–80. doi:10.1007/s00268-004-7812-7. PMID 15706440. S2CID 11678319.

[pmid15963461-10] Wang T, Yun CH, Gu SY, Chang WR, Liang DC (Aug 2005). "1.88 A crystal structure of the C domain of hCyP33: a novel domain of peptidyl-prolyl cis-trans isomerase". Biochemical and Biophysical Research Communications. 333 (3): 845–9. doi:10.1016/j.bbrc.2005.06.006. PMID 15963461.

[pmid24990953-11] Stocki P, Chapman DC, Beach LA, Williams DB (Aug 2014). "Depletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasis". The Journal of Biological Chemistry. 289 (33): 23086–96. doi:10.1074/jbc.M114.570911. PMC 4132807. PMID 24990953.

PPIF information

and 5 Related for: PPIF information

PPIF

Cyclophilin

Housekeeping gene

Peptidylprolyl isomerase D

152nd Airlift Wing