ATIF1_XENTR
ID ATIF1_XENTR Reviewed; 109 AA.
AC F7BK26; B4F6Y2;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 54.
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 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=TGA IC; TISSUE=Bone;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2008) 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:A3KNL5,
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 78-109,
CC leaving each N-terminal inhibitory region (residues 27-56) accessible
CC for interaction with an F1 catalytic domain. The inhibitory N-terminal
CC region (residues 27-56) 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; AAMC01085068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC168056; AAI68056.1; -; mRNA.
DR RefSeq; NP_001135565.1; NM_001142093.1.
DR AlphaFoldDB; F7BK26; -.
DR SMR; F7BK26; -.
DR STRING; 8364.ENSXETP00000015454; -.
DR PaxDb; F7BK26; -.
DR Ensembl; ENSXETT00000015454; ENSXETP00000015454; ENSXETG00000007103.
DR GeneID; 100216112; -.
DR KEGG; xtr:100216112; -.
DR CTD; 93974; -.
DR Xenbase; XB-GENE-956790; atp5if1.
DR eggNOG; ENOG502S4JP; Eukaryota.
DR HOGENOM; CLU_147479_1_2_1; -.
DR InParanoid; F7BK26; -.
DR OMA; YFRRQQK; -.
DR TreeFam; TF320659; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000007103; Expressed in testis and 13 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; ISS:UniProtKB.
DR GO; GO:0042030; F:ATPase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006783; P:heme biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032780; P:negative regulation of ATP-dependent activity; IBA:GO_Central.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR InterPro; IPR007648; ATPase_inhibitor_mt.
DR Pfam; PF04568; IATP; 1.
PE 3: Inferred from homology;
KW Coiled coil; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..109
FT /note="ATPase inhibitor, mitochondrial"
FT /id="PRO_0000421770"
FT REGION 27..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 27..56
FT /note="N-terminal inhibitory region"
FT /evidence="ECO:0000250"
FT REGION 78..109
FT /note="Antiparallel alpha-helical coiled coil region"
FT /evidence="ECO:0000250"
FT COILED 71..109
FT /evidence="ECO:0000255"
FT COMPBIAS 52..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 83
FT /note="R -> H (in Ref. 2; AAI68056)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 109 AA; 12191 MW; F73D1268E6D0DE0A CRC64;
MAGSSSLLRA GIRNVLLMQM RRSSDQLGEL GKGAGKGGGG GGSVREAGGA FGKRQAAEEE
RYFRQKEQEQ IASLRKHHEE EIRHHKGEIE RLQKEIERHK SKIKKLNDD
