Search Results

Overview

Uniprot IDP30405
Protein NamePeptidyl-prolyl cis-trans isomerase F, mitochondrial
Gene NamePPIF
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
118 NHNGTGGKSIYGSRF
160 QFFICTIKTDWLDGK
167 KTDWLDGKHVVFGHV
175 HVVFGHVKEGMDVVK
183 EGMDVVKKIESFGSK
190 KIESFGSKSGRTSKK
57 LDVDANGKPLGRVVL
67 GRVVLELKADVVPKT
73 LKADVVPKTAENFRA
86 RALCTGEKGFGYKGS
91 GEKGFGYKGSTFHRV

Function

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:26387735). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated (PubMed:26387735). In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:22726440). Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (PubMed:19228691)

Protein Sequence

10 MLALRCGSRW 20 LGLLSVPRSV 30 PLRLPAARAC 40 SKGSGDPSSS 50 SSSGNPLVYL 60 DVDANGKPLG 70 RVVLELKADV 80 VPKTAENFRA 90 LCTGEKGFGY 100 KGSTFHRVIP 110 SFMCQAGDFT 120 NHNGTGGKSI 130 YGSRFPDENF 140 TLKHVGPGVL 150 SMANAGPNTN 160 GSQFFICTIK 170 TDWLDGKHVV 180 FGHVKEGMDV 190 VKKIESFGSK 200 SGRTSKKIVI TDCGQLS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0016020 membrane
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005757 mitochondrial permeability transition pore complex
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:0016018 cyclosporin A binding
Molecular Function GO:0004857 enzyme inhibitor activity
Molecular Function GO:0003755 peptidyl-prolyl cis-trans isomerase activity
Biological Process GO:0006915 apoptotic process
Biological Process GO:0071243 cellular response to arsenic-containing substance
Biological Process GO:0071277 cellular response to calcium ion
Biological Process GO:0070301 cellular response to hydrogen peroxide
Biological Process GO:1902686 mitochondrial outer membrane permeabilization involved in programmed cell death
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:2001243 negative regulation of intrinsic apoptotic signaling pathway
Biological Process GO:0090324 negative regulation of oxidative phosphorylation
Biological Process GO:0090201 negative regulation of release of cytochrome c from mitochondria
Biological Process GO:0006457 protein folding
Biological Process GO:0046902 regulation of mitochondrial membrane permeability
Biological Process GO:1902445 regulation of mitochondrial membrane permeability involved in programmed necrotic cell death
Biological Process GO:0002931 response to ischemia

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.