Search Results
Overview
| Uniprot ID | Q9UII2 |
|---|---|
| Protein Name | ATPase inhibitor, mitochondrial |
| Gene Name | ATP5IF1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 49 | EAGGAFGKREQAEEE |
| 71 | REQLAALKKHHEEEI |
| 72 | EQLAALKKHHEEEIV |
| 82 | EEEIVHHKKEIERLQ |
| 83 | EEIVHHKKEIERLQK |
Function
Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix (PubMed:35926043). Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase. Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0043532 | angiostatin binding |
| Molecular Function | GO:0051117 | ATPase binding |
| Molecular Function | GO:0042030 | ATPase inhibitor activity |
| Molecular Function | GO:0005516 | calmodulin binding |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0004857 | enzyme inhibitor activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0140260 | mitochondrial proton-transporting ATP synthase complex binding |
| Biological Process | GO:0001525 | angiogenesis |
| Biological Process | GO:0030218 | erythrocyte differentiation |
| Biological Process | GO:0006091 | generation of precursor metabolites and energy |
| Biological Process | GO:0006783 | heme biosynthetic process |
| Biological Process | GO:0051882 | mitochondrial depolarization |
| Biological Process | GO:0010667 | negative regulation of cardiac muscle cell apoptotic process |
| Biological Process | GO:0001937 | negative regulation of endothelial cell proliferation |
| Biological Process | GO:0051346 | negative regulation of hydrolase activity |
| Biological Process | GO:1905707 | negative regulation of mitochondrial ATP synthesis coupled proton transport |
| Biological Process | GO:1903052 | positive regulation of proteolysis involved in protein catabolic process |
| Biological Process | GO:1905091 | positive regulation of type 2 mitophagy |
| Biological Process | GO:1903578 | regulation of ATP metabolic process |
| Biological Process | GO:1903214 | regulation of protein targeting to mitochondrion |
| 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] 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.
[3] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.