MIEAP_RAT
ID MIEAP_RAT Reviewed; 568 AA.
AC Q6AYL6; D3ZEU0; Q764P0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Mitochondria-eating protein;
DE AltName: Full=Spermatid-expressing gene 1 protein;
DE Short=Spetex-1;
DE AltName: Full=Spermatogenesis-associated protein 18;
GN Name=Spata18; Synonyms=Mieap, Spetex1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, FUNCTION,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=15236321; DOI=10.1002/mrd.20101;
RA Iida H., Ichinose J., Kaneko T., Mori T., Shibata Y.;
RT "Complementary DNA cloning of rat spetex-1, a spermatid-expressing gene-1,
RT encoding a 63 kDa cytoplasmic protein of elongate spermatids.";
RL Mol. Reprod. Dev. 68:385-393(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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-13; SER-85; SER-123; SER-154;
RP SER-157; SER-303; SER-305 AND SER-527, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-541 (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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). May have a role
CC in spermatogenesis, especially in cell differentiation from late
CC elongate spermatids to mature spermatozoa. {ECO:0000250,
CC ECO:0000269|PubMed:15236321}.
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:0000269|PubMed:15236321}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6AYL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6AYL6-2; Sequence=VSP_021189;
CC -!- TISSUE SPECIFICITY: High expressed in testis and weakly expressed in
CC lung, intestine, and spleen. Not expressed in spermatogonia,
CC spermatocytes, and round spematids in adult testis but specifically
CC detected in elongated spermatids. {ECO:0000269|PubMed:15236321}.
CC -!- DEVELOPMENTAL STAGE: Expressed at late stages of spermatogenesis, from
CC late to maturing spermatids. {ECO:0000269|PubMed:15236321}.
CC -!- SIMILARITY: Belongs to the MIEAP family. {ECO:0000305}.
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DR EMBL; AB116526; BAD02927.1; -; mRNA.
DR EMBL; BC078996; AAH78996.1; -; mRNA.
DR RefSeq; NP_955406.2; NM_199374.2. [Q6AYL6-1]
DR RefSeq; XP_006250953.1; XM_006250891.3. [Q6AYL6-2]
DR AlphaFoldDB; Q6AYL6; -.
DR STRING; 10116.ENSRNOP00000002899; -.
DR iPTMnet; Q6AYL6; -.
DR PhosphoSitePlus; Q6AYL6; -.
DR PaxDb; Q6AYL6; -.
DR GeneID; 289586; -.
DR KEGG; rno:289586; -.
DR UCSC; RGD:735208; rat. [Q6AYL6-1]
DR CTD; 132671; -.
DR RGD; 735208; Spata18.
DR eggNOG; ENOG502QQMJ; Eukaryota.
DR HOGENOM; CLU_041752_0_0_1; -.
DR InParanoid; Q6AYL6; -.
DR OrthoDB; 1178636at2759; -.
DR PhylomeDB; Q6AYL6; -.
DR TreeFam; TF328808; -.
DR PRO; PR:Q6AYL6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; NAS:RGD.
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..568
FT /note="Mitochondria-eating protein"
FT /id="PRO_0000254167"
FT REGION 110..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..313
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 175..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..283
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0P557"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 541..552
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15236321"
FT /id="VSP_021189"
FT MOD_RES Q6AYL6-2:541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 568 AA; 63884 MW; 551981E551F59D73 CRC64;
MAENLKKLAQ SESFLSLQDK VCFWANDYQT NSCDQNLNCC IELIEQVAKV QAQLFAILTA
TAQEGGHNEG VETIKSRLLP LLQTSFSSLG VGKIIQTEIR PIQDFQLRSK NRQSSLDQEQ
QQSDGDSFIE SQPTQVQDDL TESGKNLEGT KNGSAISLLA AEEEINQLKK QLKSLQAQED
ARHKTSENRR AEISRTDRRP SGKRNSERPQ DVVSNYEKHL KNLKDEIAVL SAEKSGLQAS
HRQTRSRSPS PGPRGPRGPR GRRRSRSHSR SHSRSHSRSH SHSNSHSNSR SNSPCTTVAK
IRSPSPNRSK MSSVARKAAL LSRFSDAYSQ ARLDAQCLLR RCIDRAETVQ RIIYIATVEA
FHIAKMAFRH FKIRVRKMLT PSHVGSNDFE TAVSDYIVCH LDLYDSQSSV NDVIRAMNVN
PKISFPPEVD FCLLTDFIQE ICCIAFAMQS LEPPLDIAFG ADGEVFNEAK YRRSYDSDFT
APLVFYHVWP ALMENDCVIM KGEAVTKRGA FWTTVRPVMR CRSRSLSPIC PRSRFGISTV
HSCVTIPADD LVSRSRSPSP IRCTFARY
