ID   ATIF_CYBJA              Reviewed;          63 AA.
AC   P09940;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=ATPase inhibitor, mitochondrial {ECO:0000305};
DE   AltName: Full=ATP synthase F1 subunit epsilon {ECO:0000250|UniProtKB:Q9UII2};
OS   Cyberlindnera jadinii (Torula yeast) (Pichia jadinii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=4903;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2949971; DOI=10.1111/j.1432-1033.1987.tb10749.x;
RA   Dianoux A.C., Hoppe J.;
RT   "Complete amino-acid sequence of the natural ATPase inhibitor from the
RT   mitochondria of the yeast Candida utilis.";
RL   Eur. J. Biochem. 163:155-160(1987).
CC   -!- FUNCTION: This protein forms a one-to-one complex with ATPase to
CC       inhibit the enzyme activity completely.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the ATPase inhibitor family. {ECO:0000305}.
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DR   PIR; A27536; A27536.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042030; F:ATPase inhibitor activity; IEA:InterPro.
DR   GO; GO:0032780; P:negative regulation of ATP-dependent activity; IEA:InterPro.
DR   InterPro; IPR007648; ATPase_inhibitor_mt.
DR   Pfam; PF04568; IATP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Mitochondrion.
FT   CHAIN           1..63
FT                   /note="ATPase inhibitor, mitochondrial"
FT                   /id="PRO_0000193522"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          18..62
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   63 AA;  7192 MW;  767D5869CE1752B5 CRC64;
     TAGATGATRQ DGSTDAFEKR EKAQEDLYIR QHEKEQLEAL KESLKKQKKS LDDLEBKIDD
     LTK