ID   MIEAP_DANRE             Reviewed;         490 AA.
AC   Q503Q1; A5WWB1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Mitochondria-eating protein;
DE   AltName: Full=Spermatogenesis-associated protein 18;
GN   Name=spata18; Synonyms=mieap; ORFNames=si:ch73-16a12.2, zgc:110352;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Key regulator of mitochondrial quality that mediates the
CC       repairing or degradation of unhealthy mitochondria in response to
CC       mitochondrial damage. Mediator of mitochondrial protein catabolic
CC       process (also named MALM) by mediating the degradation of damaged
CC       proteins inside mitochondria by promoting the accumulation in the
CC       mitochondrial matrix of hydrolases that are characteristic of the
CC       lysosomal lumen. Also involved in mitochondrion degradation of damaged
CC       mitochondria by promoting the formation of vacuole-like structures
CC       (named MIV), which engulf and degrade unhealthy mitochondria by
CC       accumulating lysosomes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8TC71}.
CC       Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8TC71}.
CC       Note=Localizes to the cytoplasm under normal conditions. Relocalizes to
CC       mitochondrion outer membrane following cellular stress.
CC       {ECO:0000250|UniProtKB:Q8TC71}.
CC   -!- SIMILARITY: Belongs to the MIEAP family. {ECO:0000305}.
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DR   EMBL; CT827859; CAN88314.1; -; Genomic_DNA.
DR   EMBL; BC095228; AAH95228.1; -; mRNA.
DR   RefSeq; NP_001018198.1; NM_001018678.1.
DR   AlphaFoldDB; Q503Q1; -.
DR   SMR; Q503Q1; -.
DR   STRING; 7955.ENSDARP00000103183; -.
DR   PaxDb; Q503Q1; -.
DR   Ensembl; ENSDART00000109234; ENSDARP00000103183; ENSDARG00000052343.
DR   GeneID; 497395; -.
DR   KEGG; dre:497395; -.
DR   CTD; 132671; -.
DR   ZFIN; ZDB-GENE-050522-306; spata18.
DR   eggNOG; ENOG502QQMJ; Eukaryota.
DR   GeneTree; ENSGT00390000013532; -.
DR   HOGENOM; CLU_041752_0_0_1; -.
DR   InParanoid; Q503Q1; -.
DR   OMA; NDNKYRR; -.
DR   OrthoDB; 1178636at2759; -.
DR   PhylomeDB; Q503Q1; -.
DR   TreeFam; TF328808; -.
DR   PRO; PR:Q503Q1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 20.
DR   Bgee; ENSDARG00000052343; Expressed in swim bladder and 25 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0035694; P:mitochondrial protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0035695; P:mitophagy by induced vacuole formation; ISS:UniProtKB.
DR   GO; GO:0048545; P:response to steroid hormone; IEP:ZFIN.
DR   InterPro; IPR026169; MIEAP.
DR   InterPro; IPR031981; MIEAP_C.
DR   PANTHER; PTHR21771; PTHR21771; 1.
DR   Pfam; PF16026; MIEAP; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Reference proteome.
FT   CHAIN           1..490
FT                   /note="Mitochondria-eating protein"
FT                   /id="PRO_0000254168"
FT   REGION          224..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          112..210
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        229..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        223
FT                   /note="R -> K (in Ref. 2; AAH95228)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="S -> L (in Ref. 2; AAH95228)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   490 AA;  55450 MW;  C6801B21715B9754 CRC64;
     MADTLRRLVN SSPYSVLQDK LDAWYKDYHV YSCDQNLNRC CELVELTSKI QGQLFTILNL
     TAQEGGHYSG VDTLKSRLLP WLGSCFTIAA SAVSSDTSLS LIQESVEKDR KIRELSSVHE
     SNLQKIEDQL CSTRIELDSV KRELVDTHIE LDSTKNKSAT TLLATEDEIL HLKSELRVAQ
     DQLDLYKRKL DVLDDYERQV RILRDEVSFL NAEKTVLQDR LARSRSPSPL LRRSRSVSPV
     RGESPTRAQL TSSSRHARLV SRFSDLYATE RLESQSLLLK YIDDLETVQR ILFIAAVESF
     QAAKLAYRQF KSRVRKTLSS THIGPESLED AVVDYIVRNL DLYDVQTSIN DVINAMNVNP
     RISFPPEVDF VLISSFIREA CRIAFAMQTL DPPLDLAFSS DGELYSDVKY RRSFDSEFTA
     PLVAFHVWPA LLEGDTVILK GEAVTRRGAL WKSRSRSSSP VRSRSGSPSR TFMASHSRSP
     SPGRLSSSRL