ID   ATIF2_CAEEL             Reviewed;         109 AA.
AC   O44441;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=ATPase inhibitor mai-2, mitochondrial {ECO:0000305};
DE   AltName: Full=ATP synthase F1 subunit epsilon {ECO:0000250|UniProtKB:Q9UII2};
DE   Flags: Precursor;
GN   Name=mai-2; ORFNames=B0546.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Bristol N2;
RA   Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA   Thierry-Mieg D., Thierry-Mieg J.;
RT   "The Caenorhabditis elegans transcriptome project, a complementary view of
RT   the genome.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=16897438; DOI=10.1007/s10863-006-9009-2;
RA   Ichikawa N., Ando C., Fumino M.;
RT   "Caenorhabditis elegans MAI-1 protein, which is similar to mitochondrial
RT   ATPase inhibitor (IF1), can inhibit yeast F0F1-ATPase but cannot be
RT   transported to yeast mitochondria.";
RL   J. Bioenerg. Biomembr. 38:93-99(2006).
CC   -!- FUNCTION: Thought to be a regulatory component of the ATP-synthesizing
CC       complex in the mitochondria. Activity is pH dependent.
CC       {ECO:0000269|PubMed:16897438}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- MISCELLANEOUS: Mai-2 and tin-9.2 are transcribed on a dicistronic
CC       transcript where exos-4.1 is the upstream transcript and tin-9.2 the
CC       downstream.
CC   -!- SIMILARITY: Belongs to the ATPase inhibitor family. {ECO:0000305}.
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DR   EMBL; FO080229; CCD62188.1; -; Genomic_DNA.
DR   EMBL; AF326939; AAG49389.1; -; mRNA.
DR   PIR; T32588; T32588.
DR   RefSeq; NP_500336.1; NM_067935.6.
DR   AlphaFoldDB; O44441; -.
DR   SMR; O44441; -.
DR   BioGRID; 42246; 13.
DR   STRING; 6239.B0546.1.2; -.
DR   EPD; O44441; -.
DR   PaxDb; O44441; -.
DR   PeptideAtlas; O44441; -.
DR   EnsemblMetazoa; B0546.1.1; B0546.1.1; WBGene00015248.
DR   GeneID; 177106; -.
DR   KEGG; cel:CELE_B0546.1; -.
DR   CTD; 177106; -.
DR   WormBase; B0546.1; CE16792; WBGene00015248; mai-2.
DR   eggNOG; ENOG502S8MH; Eukaryota.
DR   GeneTree; ENSGT00850000133005; -.
DR   HOGENOM; CLU_147479_1_1_1; -.
DR   InParanoid; O44441; -.
DR   OMA; QEVDHHK; -.
DR   OrthoDB; 1596356at2759; -.
DR   PhylomeDB; O44441; -.
DR   PRO; PR:O44441; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00015248; Expressed in adult organism and 4 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0042030; F:ATPase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central.
DR   GO; GO:0032780; P:negative regulation of ATP-dependent activity; IDA:WormBase.
DR   GO; GO:0045980; P:negative regulation of nucleotide metabolic process; IC: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..?
FT                   /note="Mitochondrion"
FT   CHAIN           ?..109
FT                   /note="ATPase inhibitor mai-2, mitochondrial"
FT                   /id="PRO_0000002552"
FT   REGION          18..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          55..109
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   109 AA;  12031 MW;  AE79F12221D2FF79 CRC64;
     MLSVSRAATR MTGMVARFSA GGHGDGAGRG GGSGGSIRDA GGAFGKMEAA REDEYFYKKQ
     KAQLQELREH IQEEVKHHEG QLENHKKVLE RHQQRISEIE AQERALGKE