MIEAP_BOVIN
ID MIEAP_BOVIN Reviewed; 537 AA.
AC E1BLK7;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Mitochondria-eating protein;
DE AltName: Full=Spermatogenesis-associated protein 18;
GN Name=SPATA18; Synonyms=MIEAP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
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 -!- SUBUNIT: Interacts (via coiled-coil domains) with BNIP3L (via BH3
CC domain). Interacts (via coiled-coil domains) with BNIP3 (via BH3
CC domain). {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; AAFC03100124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03100125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03100129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03100133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03104636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03104637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03122887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BLK7; -.
DR SMR; E1BLK7; -.
DR STRING; 9913.ENSBTAP00000024097; -.
DR PaxDb; E1BLK7; -.
DR PRIDE; E1BLK7; -.
DR eggNOG; ENOG502QQMJ; Eukaryota.
DR HOGENOM; CLU_041752_0_0_1; -.
DR InParanoid; E1BLK7; -.
DR Proteomes; UP000009136; 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; Phosphoprotein; Reference proteome.
FT CHAIN 1..537
FT /note="Mitochondria-eating protein"
FT /id="PRO_0000408328"
FT REGION 171..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 115..253
FT /evidence="ECO:0000255"
FT COMPBIAS 175..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0P557"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
SQ SEQUENCE 537 AA; 60584 MW; F12EEB23D1EAF7DF CRC64;
MADNLRRLVS NEALRSLQDK LESWLREYNA NSCDQNLNHC LELIEQVAKV QGQLFGILTI
AAQEGGHYDG VETIKSRLLP WLEASFTAAS LGKPVDSKVP SLQDTFDKDR HKESGTRDIQ
QLDADLSATR NQLNQVQDDM AETEKTLEEP KNRSAISLLA AEEEINQLKK QLKSLQAQEE
SRHRNSDRRR SEKRGSERRR VELRGSEQRV SDLDRRSANQ RNAEAVCDYE KQLRTLKDEI
AVLSAEKSVL QGRSARSRSP SPAPCSRSHS RSRSTSPSSA KARTPSPNRA KLSSVARKAA
LLSRFSDAYS QGRLDAQCLL RRCIDKAETV QRIIYIATVE AFHVAKMAFR HFKIRVRKSL
TPSCAGSNDF EDAVSDYIIC HLDLYDSQSS VNDVIRAMNV NPKISFPPEV DFCLLSNFIQ
EICCIAFAMQ TLEPPLDIAF GADGEIFNDC KYRRSYDSDF TAPLVFYHVW PALMENDCVI
MKGEAVTRRG AFWNSVRSVS RCRSRSLSPI CPRTRIGLGM ISRSRSPSPI RCGLPRF
