ATIF1_PIG
ID ATIF1_PIG Reviewed; 108 AA.
AC Q29307; A1XQV8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=8672129; DOI=10.1007/s003359900153;
RA Winteroe A.K., Fredholm M., Davies W.;
RT "Evaluation and characterization of a porcine small intestine cDNA library:
RT analysis of 839 clones.";
RL Mamm. Genome 7:509-517(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Longissimus dorsi muscle;
RA Cai G., Chen Y., Wang C., Li J., Peng G., Zhang H.;
RT "Generation and analysis of cDNA sequences derived from a porcine skeletal
RT muscle library.";
RL Submitted (MAY-2006) 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; F14683; CAA23195.1; -; mRNA.
DR EMBL; DQ629180; ABK55664.1; -; mRNA.
DR RefSeq; NP_001090955.1; NM_001097486.1.
DR PDB; 6J5I; EM; 3.34 A; J=26-108.
DR PDB; 6J5J; EM; 3.45 A; J=26-108.
DR PDB; 6J5K; EM; 6.20 A; AJ/BJ/CJ/J=26-108.
DR PDBsum; 6J5I; -.
DR PDBsum; 6J5J; -.
DR PDBsum; 6J5K; -.
DR AlphaFoldDB; Q29307; -.
DR SMR; Q29307; -.
DR IntAct; Q29307; 1.
DR STRING; 9823.ENSSSCP00000023669; -.
DR PaxDb; Q29307; -.
DR PeptideAtlas; Q29307; -.
DR PRIDE; Q29307; -.
DR Ensembl; ENSSSCT00000029874; ENSSSCP00000023669; ENSSSCG00000027072.
DR Ensembl; ENSSSCT00005036359; ENSSSCP00005022200; ENSSSCG00005022913.
DR Ensembl; ENSSSCT00015096369; ENSSSCP00015039617; ENSSSCG00015071631.
DR Ensembl; ENSSSCT00025037194; ENSSSCP00025015578; ENSSSCG00025027404.
DR Ensembl; ENSSSCT00030063742; ENSSSCP00030029180; ENSSSCG00030045646.
DR Ensembl; ENSSSCT00035100867; ENSSSCP00035042877; ENSSSCG00035074291.
DR Ensembl; ENSSSCT00040093142; ENSSSCP00040041154; ENSSSCG00040067989.
DR Ensembl; ENSSSCT00045050908; ENSSSCP00045035419; ENSSSCG00045029732.
DR Ensembl; ENSSSCT00050063813; ENSSSCP00050027446; ENSSSCG00050046864.
DR Ensembl; ENSSSCT00055006453; ENSSSCP00055005076; ENSSSCG00055003291.
DR Ensembl; ENSSSCT00060042419; ENSSSCP00060018064; ENSSSCG00060031333.
DR Ensembl; ENSSSCT00065035016; ENSSSCP00065014604; ENSSSCG00065026077.
DR GeneID; 100038002; -.
DR KEGG; ssc:100038002; -.
DR CTD; 93974; -.
DR VGNC; VGNC:85656; ATP5IF1.
DR eggNOG; ENOG502S4JP; Eukaryota.
DR GeneTree; ENSGT00390000006264; -.
DR HOGENOM; CLU_147479_0_0_1; -.
DR InParanoid; Q29307; -.
DR OMA; YFRARNK; -.
DR OrthoDB; 1566610at2759; -.
DR TreeFam; TF320659; -.
DR Proteomes; UP000008227; Chromosome 6.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000027072; Expressed in blood and 47 other tissues.
DR ExpressionAtlas; Q29307; baseline and differential.
DR Genevisible; Q29307; SS.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Mitochondrion; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 26..108
FT /note="ATPase inhibitor, mitochondrial"
FT /id="PRO_0000002549"
FT REGION 25..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..52
FT /note="N-terminal inhibitory region"
FT /evidence="ECO:0000250"
FT REGION 74..106
FT /note="Antiparallel alpha-helical coiled coil region"
FT /evidence="ECO:0000250"
FT COILED 69..108
FT /evidence="ECO:0000255"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35143"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 53..64
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:6J5I"
SQ SEQUENCE 108 AA; 12184 MW; 4913E7FA3429C87A CRC64;
MAATALAVRS RIGAWSVWAM QSRGFSSDTP EGVRSGAGAV RDAGGAFGKK EQADEERYFR
ARAREQLAAL KKHHENEISH HVKEIERLQK EIERHKQSIK KLKNDDDD
