位置:首页 > 蛋白库 > MIEAP_MOUSE
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}.
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; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024