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Database: UniProt
Entry: A0A3Q2EI79_CYPVA
LinkDB: A0A3Q2EI79_CYPVA
Original site: A0A3Q2EI79_CYPVA 
ID   A0A3Q2EI79_CYPVA        Unreviewed;        98 AA.
AC   A0A3Q2EI79;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=ATPase inhibitor, mitochondrial {ECO:0000256|RuleBase:RU368087};
DE   AltName: Full=ATP synthase F1 subunit epsilon {ECO:0000256|RuleBase:RU368087};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000031544.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000031544.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A3Q2EI79; -.
DR   Ensembl; ENSCVAT00000026501.1; ENSCVAP00000031544.1; ENSCVAG00000021172.1.
DR   GeneTree; ENSGT00940000165091; -.
DR   OMA; SFHQEQI; -.
DR   Proteomes; UP000265020; 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   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|SAM:Coils};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU368087};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..98
FT                   /note="ATPase inhibitor, mitochondrial"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018711595"
FT   REGION          21..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          63..97
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   98 AA;  11127 MW;  8AF00DCFE31401D3 CRC64;
     MALLILSCFY SFLQLGELGK GAGKGGGGGG SIREAGGSMG KKQAAEEEMY FKRKEQEQLN
     ALRQHHLEEI DHHKKEIERL QREIDRHKGK IRKLKHDD
//
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