ID A0A3Q3GPW4_9LABR Unreviewed; 108 AA.
AC A0A3Q3GPW4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=ATPase inhibitor, mitochondrial {ECO:0000256|RuleBase:RU368087};
DE AltName: Full=ATP synthase F1 subunit epsilon {ECO:0000256|RuleBase:RU368087};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000036142.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000036142.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
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DR AlphaFoldDB; A0A3Q3GPW4; -.
DR Ensembl; ENSLBET00000037660.1; ENSLBEP00000036142.1; ENSLBEG00000027073.1.
DR GeneTree; ENSGT00940000165091; -.
DR InParanoid; A0A3Q3GPW4; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0042030; F:ATPase inhibitor activity; IEA:UniProtKB-UniRule.
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:UP000261660}.
FT COILED 66..107
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 108 AA; 12115 MW; 3D50A3A9F73A6358 CRC64;
MTVCCCGETL TGLVLAEDPL TLVWLGELGK GAGKGGGGGG SVREAGGAFG KRQVAEEERY
FRQKEKEQME SLRKHHAEEI DHHKKEIERL QKEIHRHEGK IRKLKHDD
//
