ID A0A2Y9LD45_DELLE Unreviewed; 107 AA.
AC A0A2Y9LD45;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ATPase inhibitor, mitochondrial {ECO:0000256|ARBA:ARBA00019626, ECO:0000256|RuleBase:RU368087};
DE AltName: Full=ATP synthase F1 subunit epsilon {ECO:0000256|RuleBase:RU368087};
GN Name=ATP5IF1 {ECO:0000313|RefSeq:XP_022407604.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022407604.1};
RN [1] {ECO:0000313|RefSeq:XP_022407604.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022407604.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion
CC when the mitochondrial membrane potential falls below a threshold and
CC the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of
CC the mitochondrial matrix. Required to avoid the consumption of cellular
CC ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase.
CC {ECO:0000256|RuleBase:RU368087}.
CC -!- FUNCTION: Indirectly acts as a regulator of heme synthesis in erythroid
CC tissues: regulates heme synthesis by modulating the mitochondrial pH
CC and redox potential, allowing fech to efficiently catalyze the
CC incorporation of iron into protoporphyrin IX to produce heme.
CC {ECO:0000256|RuleBase:RU368087}.
CC -!- SUBUNIT: Homodimer; represents the active form and is present at a pH
CC value below 6.5. Homotetramer; represents the inactive form and is
CC present at a pH value above 7.0. {ECO:0000256|ARBA:ARBA00026043,
CC ECO:0000256|RuleBase:RU368087}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|RuleBase:RU368087}.
CC -!- DOMAIN: Forms an alpha-helical dimer with monomers associated via an
CC antiparallel alpha-helical coiled coil, leaving each N-terminal
CC inhibitory region accessible for interaction with an F1 catalytic
CC domain. The inhibitory N-terminal region binds the alpha(ADP-bound)-
CC beta(ADP-bound) (ATP5F1A-ATP5F1B) interface of F1-ATPase, and also
CC contact the central gamma subunit (ATP5F1C). This dimeric state is
CC favored by pH values below 7.0, and at higher values the dimers
CC associate to form inactive homotetramer, where the inhibitory region is
CC occluded, masking its inhibitory activity.
CC {ECO:0000256|RuleBase:RU368087}.
CC -!- SIMILARITY: Belongs to the ATPase inhibitor family.
CC {ECO:0000256|ARBA:ARBA00010901, ECO:0000256|RuleBase:RU368087}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_022407604.1; XM_022551896.2.
DR AlphaFoldDB; A0A2Y9LD45; -.
DR STRING; 9749.A0A2Y9LD45; -.
DR Ensembl; ENSDLET00000020132; ENSDLEP00000018248; ENSDLEG00000013329.
DR KEGG; dle:111163316; -.
DR InParanoid; A0A2Y9LD45; -.
DR OrthoDB; 4627437at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0043532; F:angiostatin binding; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0042030; F:ATPase inhibitor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140260; F:mitochondrial proton-transporting ATP synthase complex binding; IEA:Ensembl.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:Ensembl.
DR GO; GO:0051882; P:mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:1904925; P:positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1903052; P:positive regulation of proteolysis involved in protein catabolic process; IEA:Ensembl.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:1903578; P:regulation of ATP metabolic process; IEA:Ensembl.
DR GO; GO:1903214; P:regulation of protein targeting to mitochondrion; IEA:Ensembl.
DR Gene3D; 1.20.5.500; Single helix bin; 2.
DR InterPro; IPR007648; ATPase_inhibitor_mt.
DR PANTHER; PTHR48329; FI01416P; 1.
DR PANTHER; PTHR48329:SF1; FI01416P; 1.
DR Pfam; PF04568; IATP; 1.
DR SUPFAM; SSF64602; F1 ATPase inhibitor, IF1, C-terminal domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU368087};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT COILED 71..105
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 107 AA; 12068 MW; 49E8EAE589F04FD8 CRC64;
MAATALAART RFGVWSVWAM QGRGFGSESA DNLGSSAGAV RDAGGAFGKR EQAEEERYFR
ARAKEQLAAL KKHHENEISH HMKEIEHLQK EIERHKQSIK KLKHDDD
//
