MIEAP_PIG
ID MIEAP_PIG Reviewed; 560 AA.
AC D5K8A2;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu Y.G.;
RL Submitted (JAN-2010) 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). 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). Colocalizes with BNIP3 and BNIP3L at the mitochondrion outer
CC membrane. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GU475004; ADE28540.1; -; mRNA.
DR RefSeq; NP_001171386.1; NM_001177915.1.
DR AlphaFoldDB; D5K8A2; -.
DR SMR; D5K8A2; -.
DR STRING; 9823.ENSSSCP00000009421; -.
DR PaxDb; D5K8A2; -.
DR PeptideAtlas; D5K8A2; -.
DR PRIDE; D5K8A2; -.
DR GeneID; 100415808; -.
DR KEGG; ssc:100415808; -.
DR CTD; 132671; -.
DR eggNOG; ENOG502QQMJ; Eukaryota.
DR InParanoid; D5K8A2; -.
DR OrthoDB; 1178636at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..560
FT /note="Mitochondria-eating protein"
FT /id="PRO_0000408330"
FT REGION 178..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 118..186
FT /evidence="ECO:0000255"
FT COILED 223..248
FT /evidence="ECO:0000255"
FT COMPBIAS 243..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..291
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
SQ SEQUENCE 560 AA; 63300 MW; C44C4C6A04DECFFB CRC64;
MADNLRKLVS TESLRSMQDK LENWLREYNN NSCDQNLNYC LELIEQVAKV QGQLFGILTT
AAQEGGHYDG VETIKSRLLP WLEASFTAAS LGKPVDSKIP SLQDTFDKER QKESVIRDRN
IHQLDADLNT TRNQLNQVQD DLAETEKTLE ETKNRSAISL LAAEEEINQL RKQLKCLQAQ
EESRHRPPEH RSSEKRGSER RRVEPRGADR CGAAQRKAEE ICDYEKQLRT LKDEIAVLSA
EKSVLQGRST RSRSPSPASC SRSRSHSHSR SRSHSHSRSG SHSRSHSRNH SRSRSASPST
AVSGVRSPSP NRAKLSSVAR KAALLSRFSD AYSQARLDAQ CLLRRCIDKA ETVQRIIYIA
TVEAFHVAKM AFRHFKIRVR KSLTPSYAGS NDFEDAVLDY IICHLDLYDS QSSVNDVIRA
MNVNPKISFP PEVDFCLLSN FIQEICCIAF AMQTLDPPLD IAFGADGEIF NDCKYRRSYD
SDFTAPLVFY HVWPALMEND CVIMKGEAVT RRGAFWNSVR SVTRCRSRSL SPICPRSRVG
LSTISRSRSP SPIRCGLPRF
