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Database: UniProt
Entry: A0A3Q2D9N0_CYPVA
LinkDB: A0A3Q2D9N0_CYPVA
Original site: A0A3Q2D9N0_CYPVA 
ID   A0A3Q2D9N0_CYPVA        Unreviewed;       108 AA.
AC   A0A3Q2D9N0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 27.
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:ENSCVAP00000015496.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000015496.1}
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   RefSeq; XP_015229179.1; XM_015373693.1.
DR   AlphaFoldDB; A0A3Q2D9N0; -.
DR   STRING; 28743.ENSCVAP00000015496; -.
DR   Ensembl; ENSCVAT00000031542.1; ENSCVAP00000015496.1; ENSCVAG00000018316.1.
DR   GeneID; 107084050; -.
DR   KEGG; cvg:107084050; -.
DR   CTD; 100037369; -.
DR   GeneTree; ENSGT00940000165091; -.
DR   OMA; GCERSAN; -.
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   GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:Ensembl.
DR   GO; GO:0007634; P:optokinetic behavior; IEA:Ensembl.
DR   GO; GO:0150077; P:regulation of neuroinflammatory response; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; IEA:Ensembl.
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}.
FT   COILED          52..107
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   108 AA;  12346 MW;  2927A94ACD704963 CRC64;
     MARLFLRGNL QRCIATQIRL SSDQLGELGK GAGRGGGGGG YVRSAGGAFG KREAAEEERY
     FREREREQLE ALRKHHAEEI EHHKKEIERL QKEIDRHKGK IRKLSHDD
//
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