ID A0A151PGL2_ALLMI Unreviewed; 117 AA.
AC A0A151PGL2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-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};
GN Name=ATPIF1 {ECO:0000313|EMBL:KYO48082.1};
GN ORFNames=Y1Q_0001899 {ECO:0000313|EMBL:KYO48082.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO48082.1};
RN [1] {ECO:0000313|EMBL:KYO48082.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO48082.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO48082.1}.
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DR EMBL; AKHW03000257; KYO48082.1; -; Genomic_DNA.
DR RefSeq; XP_014460523.1; XM_014605037.2.
DR AlphaFoldDB; A0A151PGL2; -.
DR STRING; 8496.A0A151PGL2; -.
DR GeneID; 102558812; -.
DR KEGG; amj:102558812; -.
DR CTD; 93974; -.
DR eggNOG; ENOG502S8MH; Eukaryota.
DR PhylomeDB; A0A151PGL2; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
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:UP000050525}.
FT REGION 21..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 72..113
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 117 AA; 12984 MW; DE7312FAE98AAFC8 CRC64;
MAAGVLRSGL RGAFLMQQQR GWSSGSGADQ LGELGKGAGK GGGGGGSIRE AGGAFGKRQA
AEEERYFREK EREQLAALRK HHEEEIDHHK KQIDLLQKEI ERHKYKIKKL KNDDDDD
//
