| IED ID | IndEnz0002018535 |
| Enzyme Type ID | protease018535 |
| Protein Name |
ATPase inhibitor, mitochondrial ATP synthase F1 subunit epsilon Inhibitor of F 1 F o -ATPase IF 1 IF1 |
| Gene Name | ATP5IF1 ATPI ATPIF1 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAVTALAARTWLGVWGVRTMQARGFGSDQSENVDRGAGSIREAGGAFGKREQAEEERYFRAQSREQLAALKKHHEEEIVHHKKEIERLQKEIERHKQKIKMLKHDD |
| Enzyme Length | 106 |
| Uniprot Accession Number | Q9UII2 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | 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. 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. {ECO:0000269|PubMed:12110673, ECO:0000269|PubMed:15528193, ECO:0000269|PubMed:19559621, ECO:0000269|PubMed:23135403}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Chain (1); Coiled coil (1); Erroneous initiation (1); Modified residue (3); Region (3); Sequence conflict (1); Transit peptide (1) |
| Keywords | Alternative splicing;Coiled coil;Direct protein sequencing;Mitochondrion;Phosphoprotein;Reference proteome;Transit peptide |
| Interact With | P01023; P07550; P06576; P28329-3; G5E9A7; O75190-2; P50570-2; P22607; Q53GS7; P28799-2; P06396; P01112; Q9HAQ2; O14901; P51608; I6L9F6; Q9BVL2; Q99650; Q9NRD5; D3DTS7; Q7Z699; O14656-2 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12110673}. |
| Modified Residue | MOD_RES 39; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 63; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163; MOD_RES 103; /note=N6-succinyllysine; /evidence=ECO:0000250|UniProtKB:O35143 |
| Post Translational Modification | PTM: Exhibits variability in chain length, mitochondria have distinct pools of protein cleaved after the 24th, 25th, and 26th amino acid. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15809073; 16169070; 16713569; 17851741; 18624398; 20374090; 20379614; 20538613; 20711500; 20877624; 21900206; 22342343; 23348567; 23722655; 23794714; 24005319; 24255178; 24521670; 24685140; 25042864; 25605724; 25776485; 25852190; 26381881; 26387949; 26484591; 26496610; 26595676; 26659871; 26752685; 26876430; 28173810; 28183315; 28228254; 28298645; 29097244; 30204502; 30600215; 31894674; 33065099; 33922643; |
| Motif | |
| Gene Encoded By | |
| Mass | 12,249 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |