MIEAP_XENLA
ID MIEAP_XENLA Reviewed; 485 AA.
AC Q498J5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, 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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-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; BC100193; AAI00194.1; -; mRNA.
DR RefSeq; NP_001089651.1; NM_001096182.1.
DR AlphaFoldDB; Q498J5; -.
DR SMR; Q498J5; -.
DR DNASU; 734711; -.
DR GeneID; 734711; -.
DR KEGG; xla:734711; -.
DR CTD; 734711; -.
DR Xenbase; XB-GENE-5812351; spata18b.S.
DR OrthoDB; 1178636at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 734711; Expressed in testis and 12 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 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..485
FT /note="Mitochondria-eating protein"
FT /id="PRO_0000254169"
FT REGION 214..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 112..210
FT /evidence="ECO:0000255"
SQ SEQUENCE 485 AA; 55139 MW; 8793BE801CE0904C CRC64;
MADILRRLTN SERCRLLQDK LDDWYKDYHI NSCDSNLNVC CELLELNSKV QGQLFKILSV
TAQEGGQYAG VETIKSRFLP WLGTCFSTAS PGSFSENSFV TLNESMERKL STSHERELNE
VESKLSSTRI ELNSVRQELL ETQMDLEDTK TKSANTLLAT EEEILQLRAE LRAAREKLEL
RSLDSIDEYE RQIRLLKDEI SILSSESSIL KSRLSRSRSP SPIRHSSRSS SPFARSESPT
SAKLTSASRQ ARLISRFNDI FANDRLDAQT LLRRYIQDLD MVQRIIFIAT VESFHSAKMA
FRQFRLRVCK SLSPSHMGPE SLEDAVIDYI VGNLDLYDVQ SSVNEVISAM NVNPKISFPP
EVDFILISGF IQEVCRVAFT MQTLDPPLDI AFTVDGELFT DSKYRRTYDS EHTAPLVYYH
VWPALMENDN VIVKGEAVTK RGALWNSIRS RSRSASPLRS HSDSPGHNLT RSRSPSPRRS
GTPRF