MIEAP_MOUSE
ID MIEAP_MOUSE Reviewed; 537 AA.
AC Q0P557; B7ZMP4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Mitochondria-eating protein;
DE AltName: Full=Spermatogenesis-associated protein 18;
GN Name=Spata18; Synonyms=Mieap;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-537 (ISOFORM 1), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-537 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-127, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=21300779; DOI=10.1128/mcb.01072-10;
RA Bornstein C., Brosh R., Molchadsky A., Madar S., Kogan-Sakin I.,
RA Goldstein I., Chakravarti D., Flores E.R., Goldfinger N., Sarig R.,
RA Rotter V.;
RT "SPATA18, a spermatogenesis-associated gene, is a novel transcriptional
RT target of p53 and p63.";
RL Mol. Cell. Biol. 31:1679-1689(2011).
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. May have a role in spermatogenesis, especially
CC in cell differentiation from late elongate spermatids to mature
CC spermatozoa (By similarity). The physical interaction of SPATA18/MIEAP,
CC BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the
CC opening of a pore in the mitochondrial double membrane in order to
CC mediate the translocation of lysosomal proteins from the cytoplasm to
CC 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Alpha, Mieap-alpha;
CC IsoId=Q0P557-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta, Mieap-beta;
CC IsoId=Q0P557-2; Sequence=VSP_041057;
CC Name=3;
CC IsoId=Q0P557-3; Sequence=VSP_041058;
CC -!- TISSUE SPECIFICITY: In testis, expressed primarily in spermatids.
CC {ECO:0000269|PubMed:21300779}.
CC -!- INDUCTION: By p53/TP53 and p63/TP63. Directly activated by p53/TP53.
CC {ECO:0000269|PubMed:21300779}.
CC -!- SIMILARITY: Belongs to the MIEAP family. {ECO:0000305}.
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DR EMBL; AC140429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120503; AAI20504.1; -; mRNA.
DR EMBL; BC120505; AAI20506.1; -; mRNA.
DR EMBL; BC144721; AAI44722.1; -; mRNA.
DR EMBL; BC144723; AAI44724.1; -; mRNA.
DR CCDS; CCDS57351.1; -. [Q0P557-1]
DR RefSeq; NP_848474.2; NM_178387.3. [Q0P557-1]
DR RefSeq; XP_006504218.1; XM_006504155.2. [Q0P557-3]
DR RefSeq; XP_006504223.1; XM_006504160.2. [Q0P557-2]
DR AlphaFoldDB; Q0P557; -.
DR STRING; 10090.ENSMUSP00000137444; -.
DR iPTMnet; Q0P557; -.
DR PhosphoSitePlus; Q0P557; -.
DR MaxQB; Q0P557; -.
DR PaxDb; Q0P557; -.
DR PRIDE; Q0P557; -.
DR ProteomicsDB; 290239; -. [Q0P557-1]
DR ProteomicsDB; 290240; -. [Q0P557-2]
DR ProteomicsDB; 290241; -. [Q0P557-3]
DR Antibodypedia; 49630; 121 antibodies from 24 providers.
DR Ensembl; ENSMUST00000071077; ENSMUSP00000064308; ENSMUSG00000029155. [Q0P557-1]
DR GeneID; 73472; -.
DR KEGG; mmu:73472; -.
DR UCSC; uc008xte.2; mouse. [Q0P557-1]
DR CTD; 132671; -.
DR MGI; MGI:1920722; Spata18.
DR VEuPathDB; HostDB:ENSMUSG00000029155; -.
DR eggNOG; ENOG502QQMJ; Eukaryota.
DR GeneTree; ENSGT00390000013532; -.
DR InParanoid; Q0P557; -.
DR OMA; NDNKYRR; -.
DR OrthoDB; 1178636at2759; -.
DR BioGRID-ORCS; 73472; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q0P557; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q0P557; protein.
DR Bgee; ENSMUSG00000029155; Expressed in seminiferous tubule of testis and 21 other tissues.
DR ExpressionAtlas; Q0P557; baseline and differential.
DR Genevisible; Q0P557; MM.
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:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0036126; C:sperm flagellum; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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 GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR026169; MIEAP.
DR InterPro; IPR031981; MIEAP_C.
DR PANTHER; PTHR21771; PTHR21771; 1.
DR Pfam; PF16026; MIEAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Developmental protein;
KW Differentiation; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Reference proteome; Spermatogenesis.
FT CHAIN 1..537
FT /note="Mitochondria-eating protein"
FT /id="PRO_0000408329"
FT REGION 109..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 152..184
FT /evidence="ECO:0000255"
FT COILED 210..243
FT /evidence="ECO:0000255"
FT COMPBIAS 110..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..290
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 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 283
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 508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYL6"
FT VAR_SEQ 139..171
FT /note="DLAESGKSLEGAKNGSTISLLAAEEEINQLKKQ -> E (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041057"
FT VAR_SEQ 520
FT /note="T -> TVHSCVAIPAENL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041058"
FT CONFLICT 400
FT /note="V -> I (in Ref. 2; AAI44724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 537 AA; 60398 MW; F8FBD3DB3767F679 CRC64;
MAESLKKLAK SESLQALQDK VTYWVNDYNS NSCDQNLNYC IELIEQVAKV QAQLFGILTV
TAQEGGNNEG VETIKCRLLP LLQTSFSSVN MGKTAESEMC ATQDFQLRSK NRDNSPDQDQ
HQSDNESFSE TQPTQVQDDL AESGKSLEGA KNGSTISLLA AEEEINQLKK QLKSLQAQED
ARHKTSENRR SEALKSDHRS TKRTQDQRPQ DVVSNYEKHL QNLKEEIAVL SAEKSGLQGR
SARSPSPSTG TRSHRRGRSR SHSRSRSHSR SNSPCTTVAK IRSPSPNRAK MSSVARKAAL
LSRFSDAYSQ ARLDAQCLLR RCIDRAETVQ RIIYIATVEA FHVAKMAFRH FKIRVRKMLT
PSNVGSNTDF ETAVSEYIVC HLDLYDSQSS VNDVIRAMNV NPKISFPPEV DFCLLTDFIQ
EICCIAFAMQ SLEPPLDIAF GADGEIFNDC KYRRSYDSDF TAPLVFYHVW PALMENDCVI
MKGEAVTKRG AFWSSVRPVM RCRSRSLSPI CPRNHFGIST VSRSRSPSPI RCTFARY