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Overview

Uniprot IDQ8TC71
Protein NameMitochondria-eating protein
Gene NameSPATA18
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
147 DDLVETEKNLEESKN
237 KKQLRNLKEEIAVLS
292 RPSPNRSKLSNVARK
327 LLRRCIDKAETVQRI

Function

Key regulator of mitochondrial quality that mediates the repairing or degradation of unhealthy mitochondria in response to mitochondrial damage (PubMed:21264221, PubMed:21264228, PubMed:22292033, PubMed:22532927). Mediator of mitochondrial protein catabolic process (also named MALM) by mediating the degradation of damaged proteins inside mitochondria by promoting the accumulation in the mitochondrial matrix of hydrolases that are characteristic of the lysosomal lumen (PubMed:21264221, PubMed:21264228, PubMed:22292033, PubMed:22532927). Also involved in mitochondrion degradation of damaged mitochondria by promoting the formation of vacuole-like structures (named MIV), which engulf and degrade unhealthy mitochondria by accumulating lysosomes (PubMed:21264228). The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix (PubMed:22292033). Binds cardiolipin (PubMed:38322995). May form molecular condensates (non-membrane-bounded organelles) within mitochondria that compartmentalize and promote cardiolipin metabolism (PubMed:38322995)

Protein Sequence

10 MAENLKRLVS 20 NETLRTLQEK 30 LDFWLKEYNT 40 NTCDQNLNHC 50 LELIEQVAKV 60 QGQLFGILTA 70 AAQEGGRNDG 80 VETIKSRLLP 90 WLEASFTAAS 100 LGKSVDSKVP 110 SLQDTFDRER 120 HKDPSPRDRD 130 MQQLDSNLNS 140 TRSQCNQVQD 150 DLVETEKNLE 160 ESKNRSAISL 170 LAAEEEINQL 180 KKQLKSLQAQ 190 EDARHRNTDQ 200 RSSENRRSEP 210 WSLEERKREQ 220 WNSLKQNADQ 230 QDTEAMSDYK 240 KQLRNLKEEI 250 AVLSAEKSAL 260 QGRSSRSRSP 270 SPAPRSRSCS 280 RSRSASPSTA 290 VKVRRPSPNR 300 SKLSNVARKA 310 ALLSRFSDSY 320 SQARLDAQCL 330 LRRCIDKAET 340 VQRIIYIATV 350 EAFHVAKMAF 360 RHFKIHVRKS 370 LTPSYVGSND 380 FENAVLDYVI 390 CHLDLYDSQS 400 SVNDVIRAMN 410 VNPKISFPPV 420 VDFCLLSDFI 430 QEICCIAFAM 440 QALEPPLDIA 450 YGADGEVFND 460 CKYRRSYDSD 470 FTAPLVLYHV 480 WPALMENDCV 490 IMKGEAVTRR 500 GAFWNSVRSV 510 SRCRSRSLSP 520 ICPRSQIGLN 530 TMSRSRSPSP IRCGLPRF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0043231 intracellular membrane-bounded organelle
Cellular Component GO:0005759 mitochondrial matrix
Cellular Component GO:0005741 mitochondrial outer membrane
Cellular Component GO:0005739 mitochondrion
Molecular Function GO:1901612 cardiolipin binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0140693 molecular condensate scaffold activity
Biological Process GO:0035694 mitochondrial protein catabolic process
Biological Process GO:0035695 mitophagy by internal vacuole formation
Biological Process GO:1900210 positive regulation of cardiolipin metabolic process

Reference

[1] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[2] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.