ID   MIEAP_CHICK             Reviewed;         479 AA.
AC   E1BW58;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Mitochondria-eating protein;
DE   AltName: Full=Spermatogenesis-associated protein 18;
GN   Name=SPATA18; Synonyms=MIEAP;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
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). The physical interaction of
CC       SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane
CC       regulates the opening of a pore in the mitochondrial double membrane in
CC       order to mediate the translocation of lysosomal proteins from the
CC       cytoplasm to the mitochondrial matrix (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. Colocalizes
CC       with BNIP3 and BNIP3L at the mitochondrion outer membrane.
CC       {ECO:0000250|UniProtKB:Q8TC71}.
CC   -!- SIMILARITY: Belongs to the MIEAP family. {ECO:0000305}.
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DR   EMBL; AADN02031293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E1BW58; -.
DR   SMR; E1BW58; -.
DR   STRING; 9031.ENSGALP00000022597; -.
DR   PaxDb; E1BW58; -.
DR   VEuPathDB; HostDB:geneid_422759; -.
DR   eggNOG; ENOG502QQMJ; Eukaryota.
DR   InParanoid; E1BW58; -.
DR   OrthoDB; 1178636at2759; -.
DR   PhylomeDB; E1BW58; -.
DR   TreeFam; TF328808; -.
DR   Proteomes; UP000000539; Unplaced.
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   InterPro; IPR026169; MIEAP.
DR   InterPro; IPR031981; MIEAP_C.
DR   PANTHER; PTHR21771; PTHR21771; 1.
DR   Pfam; PF16026; MIEAP; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasm; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Reference proteome.
FT   CHAIN           1..479
FT                   /note="Mitochondria-eating protein"
FT                   /id="PRO_0000408331"
FT   REGION          220..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          109..161
FT                   /evidence="ECO:0000255"
FT   COILED          187..223
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        463..479
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  54575 MW;  B8F808F956D72133 CRC64;
     MAGSLKKLAK AESCRLMQEK LESWSKDYEI NSCDQNLNQC CELIEMTSVI QGQLFTILNE
     TSRESGHYAG VDTIKTRLLP WLGTWFSHAT SGRLFETGLF LNQDSTETER KLRQLATSQT
     LQLQDLQEEL TSTRLELNHV QQDLAQTQLA LEDTKTQLAT TLLTAADEII QLRAVLKASR
     AQEEDSLRRL DHLNDCEQQI ERLRDELSIL DAQKSVLQSR IARSRSPSPR RIRSRSPSPL
     PLRSCSPGRA RSTNASRHAF LVARFGDIYS KDRFDAERIL RTYISDMEMV QRIIYTAAVE
     SFHAAKMAYR QFKMRVRKTL SIGHSGPESL EDTVMDYIVR HEDLYDVQAS VNEVIRSMNI
     NPKISSTPEC DFAVISSFIR ELCRVAFSMQ TLTPPLDVAF GMDGEFFSET KYHRSVDSDY
     TAALVAYHVW PALMENDVVI VKGEAVTKRG ALWSHRSRSR SQNRSRSVSP LLSHLSRSR