Detail Information for IndEnz0002018535
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