MIEAP_MACFA
ID MIEAP_MACFA Reviewed; 538 AA.
AC Q95K37; Q4R7M3; Q4R8N1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Mitochondria-eating protein;
DE AltName: Full=Spermatogenesis-associated protein 18;
GN Name=SPATA18; Synonyms=MIEAP; ORFNames=QtsA-10472, QtsA-12015, QtsA-14813;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-357 AND 249-538.
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-538.
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB62935.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE00541.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB168420; BAE00541.1; ALT_INIT; mRNA.
DR EMBL; AB168792; BAE00899.1; -; mRNA.
DR EMBL; AB069990; BAB62935.1; ALT_INIT; mRNA.
DR RefSeq; XP_005555362.1; XM_005555305.2.
DR AlphaFoldDB; Q95K37; -.
DR SMR; Q95K37; -.
DR STRING; 9541.XP_005555361.1; -.
DR GeneID; 101865904; -.
DR KEGG; mcf:101865904; -.
DR CTD; 132671; -.
DR VEuPathDB; HostDB:ENSMFAG00000043327; -.
DR eggNOG; ENOG502QQMJ; Eukaryota.
DR OrthoDB; 1178636at2759; -.
DR Proteomes; UP000233100; Chromosome 5.
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..538
FT /note="Mitochondria-eating protein"
FT /id="PRO_0000254166"
FT REGION 92..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 118..186
FT /evidence="ECO:0000255"
FT COILED 220..256
FT /evidence="ECO:0000255"
FT COMPBIAS 103..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..292
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 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 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT CONFLICT 341..357
FT /note="EAFHVAKMAFRHFKIRV -> GLANHDLWTISGPGSYF (in Ref. 1;
FT BAE00899)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 538 AA; 60966 MW; 90D9658F7ECA66B8 CRC64;
MAENLKRLVS NEALRTLQEK LDSWLKEYNT NTCDQNLNHC LELIEQVAKV QGQLFGILTT
AAQEGGHNDG VETIKSRLLP WLEASFTAAS MGKPVDSKVP SLQNTFDRER RKDPSPRDRD
MQQLDSNLNS TRSQLNQVQD DLAETEKNLE ETKNRSAISL LAAEEEINQL KKQLKTLQAQ
EDARHRHTDQ RSSENRRSEP RSSEERRCEQ WSSLKRNADQ RDTEVTSDYK KQLRNLKEEI
AVLSAEKSAL QGRSSRSRSP SPAPRSRSCS RSRSASPSTA VKVRSPSPNR SKLSNVARKA
ALLSRFSDSY SQARLDAQCL LRRCIDKAET VQRIIYIATV EAFHVAKMAF RHFKIRVRKS
LTPSYVGSND FENAVSDYVI CHLDLYDSQS SVNDVIRAMN VNPKISFPPV VDFCLLSDFI
QEICCIAFAM QALEPPLDIA YGADGEVFND CKYRRSYDSD FTAPLVLYHV WPALMENDCV
IMKGEAVTRR GAFWNSVRSL SRCRSRSLSP ICPRSQIGLS TMSRSRSPSP IRCGLPRF
