ATIF1_PONAB
ID ATIF1_PONAB Reviewed; 106 AA.
AC Q5RFJ9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=ATPase inhibitor, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase F1 subunit epsilon {ECO:0000250|UniProtKB:Q9UII2};
DE AltName: Full=Inhibitor of F(1)F(o)-ATPase;
DE Short=IF(1);
DE Short=IF1;
DE Flags: Precursor;
GN Name=ATP5IF1 {ECO:0000250|UniProtKB:Q9UII2}; Synonyms=ATPI, ATPIF1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). Indirectly acts as a regulator of heme synthesis in
CC erythroid tissues: regulates heme synthesis by modulating the
CC mitochondrial pH and redox potential, allowing FECH to efficiently
CC catalyze the incorporation of iron into protoporphyrin IX to produce
CC heme (By similarity). {ECO:0000250|UniProtKB:O35143,
CC ECO:0000250|UniProtKB:P01096}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- DOMAIN: Forms an alpha-helical dimer with monomers associated via an
CC antiparallel alpha-helical coiled coil composed of residues 74-106,
CC leaving each N-terminal inhibitory region (residues 26-52) accessible
CC for interaction with an F1 catalytic domain. The inhibitory N-terminal
CC region (residues 26-52) binds the alpha(ADP-bound)-beta(ADP-bound)
CC (ATP5F1A-ATP5F1B) interface of F1-ATPase, and also contact the central
CC gamma subunit (ATP5F1C). This dimeric state is favored by pH values
CC below 7.0, and at higher values the dimers associate to form inactive
CC homotetramer, where the inhibitory region is occluded, masking its
CC inhibitory activity (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase inhibitor family. {ECO:0000305}.
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DR EMBL; CR857157; CAH89458.1; -; mRNA.
DR RefSeq; NP_001124626.1; NM_001131154.2.
DR AlphaFoldDB; Q5RFJ9; -.
DR SMR; Q5RFJ9; -.
DR STRING; 9601.ENSPPYP00000001900; -.
DR PRIDE; Q5RFJ9; -.
DR Ensembl; ENSPPYT00000049692; ENSPPYP00000025022; ENSPPYG00000001644.
DR GeneID; 100171464; -.
DR KEGG; pon:100171464; -.
DR CTD; 93974; -.
DR eggNOG; ENOG502S4JP; Eukaryota.
DR GeneTree; ENSGT00390000006264; -.
DR HOGENOM; CLU_147479_0_0_1; -.
DR InParanoid; Q5RFJ9; -.
DR OrthoDB; 1566610at2759; -.
DR TreeFam; TF320659; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0043532; F:angiostatin binding; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISS:UniProtKB.
DR GO; GO:0042030; F:ATPase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0140260; F:mitochondrial proton-transporting ATP synthase complex binding; IEA:Ensembl.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006783; P:heme biosynthetic process; ISS:UniProtKB.
DR GO; GO:0051882; P:mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IEA:Ensembl.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; ISS:UniProtKB.
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 InterPro; IPR007648; ATPase_inhibitor_mt.
DR Pfam; PF04568; IATP; 1.
PE 3: Inferred from homology;
KW Coiled coil; Mitochondrion; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 26..106
FT /note="ATPase inhibitor, mitochondrial"
FT /id="PRO_0000002550"
FT REGION 26..52
FT /note="N-terminal inhibitory region"
FT /evidence="ECO:0000250"
FT REGION 26..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..106
FT /note="Antiparallel alpha-helical coiled coil region"
FT /evidence="ECO:0000250"
FT COILED 63..106
FT /evidence="ECO:0000255"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UII2"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UII2"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35143"
SQ SEQUENCE 106 AA; 12249 MW; A6144431125D5A86 CRC64;
MAVTALAART WLGVWGVRTM QARGFGSDQS ENVDRGAGSI REAGGAFGKR EQAEEERYFR
AQSREQLAAL KKHHEEEIVH HKKEIERLQK EIERHKQKIK MLKHDD
