ID MDM12_CANAL Reviewed; 428 AA. AC Q59S52; A0A1D8PQR1; Q3MPM0; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 27-MAR-2024, entry version 99. DE RecName: Full=Mitochondrial distribution and morphology protein 12 {ECO:0000255|HAMAP-Rule:MF_03104}; DE AltName: Full=Mitochondrial inheritance component MDM12 {ECO:0000255|HAMAP-Rule:MF_03104}; GN Name=MDM12 {ECO:0000255|HAMAP-Rule:MF_03104}; GN OrderedLocusNames=CAALFM_C701180WA; ORFNames=CaJ7.0134, CaO19.6900; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15937140; DOI=10.1534/genetics.104.034652; RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T., RA Mikami Y.; RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 and RT syntenic analysis against the Saccharomyces cerevisiae genome."; RL Genetics 170:1525-1537(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [3] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). CC -!- FUNCTION: Component of the ERMES/MDM complex, which serves as a CC molecular tether to connect the endoplasmic reticulum (ER) and CC mitochondria. Components of this complex are involved in the control of CC mitochondrial shape and protein biogenesis, and function in CC nonvesicular lipid trafficking between the ER and mitochondria. MDM12 CC is required for the interaction of the ER-resident membrane protein CC MMM1 and the outer mitochondrial membrane-resident beta-barrel protein CC MDM10. The MDM12-MMM1 subcomplex functions in the major beta-barrel CC assembly pathway that is responsible for biogenesis of all CC mitochondrial outer membrane beta-barrel proteins, and acts in a late CC step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further CC acts in the TOM40-specific pathway after the action of the MDM12-MMM1 CC complex. Essential for establishing and maintaining the structure of CC mitochondria and maintenance of mtDNA nucleoids. {ECO:0000255|HAMAP- CC Rule:MF_03104}. CC -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES) CC or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. A MMM1 CC homodimer associates with one molecule of MDM12 on each side in a CC pairwise head-to-tail manner, and the SMP-LTD domains of MMM1 and MDM12 CC generate a continuous hydrophobic tunnel for phospholipid trafficking. CC {ECO:0000255|HAMAP-Rule:MF_03104}. CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP- CC Rule:MF_03104}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_03104}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03104}. CC Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03104}; CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03104}; CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03104}. Note=The ERMES/MDM CC complex localizes to a few discrete foci (around 10 per single cell), CC that represent mitochondria-endoplasmic reticulum junctions. These foci CC are often found next to mtDNA nucleoids. {ECO:0000255|HAMAP- CC Rule:MF_03104}. CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that can bind CC various types of glycerophospholipids in its interior and mediate their CC transfer between two adjacent bilayers. {ECO:0000255|HAMAP- CC Rule:MF_03104}. CC -!- SIMILARITY: Belongs to the MDM12 family. {ECO:0000255|HAMAP- CC Rule:MF_03104}. 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; AP006852; BAE44640.1; -; Genomic_DNA. DR EMBL; CP017629; AOW30488.1; -; Genomic_DNA. DR RefSeq; XP_712472.1; XM_707379.1. DR AlphaFoldDB; Q59S52; -. DR SMR; Q59S52; -. DR STRING; 237561.Q59S52; -. DR EnsemblFungi; C7_01180W_A-T; C7_01180W_A-T-p1; C7_01180W_A. DR GeneID; 3645915; -. DR KEGG; cal:CAALFM_C701180WA; -. DR CGD; CAL0000201825; MDM12. DR VEuPathDB; FungiDB:C7_01180W_A; -. DR eggNOG; ENOG502S3PB; Eukaryota. DR HOGENOM; CLU_026794_2_0_1; -. DR InParanoid; Q59S52; -. DR OMA; KRAHFCF; -. DR OrthoDB; 5559at2759; -. DR Proteomes; UP000000559; Chromosome 7. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032865; C:ERMES complex; IBA:GO_Central. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule. DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IBA:GO_Central. DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central. DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IEA:UniProtKB-UniRule. DR CDD; cd21672; SMP_Mdm12; 1. DR HAMAP; MF_03104; Mdm12; 1. DR InterPro; IPR027532; Mdm12. DR InterPro; IPR031468; SMP_LBD. DR PANTHER; PTHR28204; MITOCHONDRIAL DISTRIBUTION AND MORPHOLOGY PROTEIN 12; 1. DR PANTHER; PTHR28204:SF1; MITOCHONDRIAL DISTRIBUTION AND MORPHOLOGY PROTEIN 12; 1. DR PROSITE; PS51847; SMP; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane; KW Mitochondrion; Mitochondrion outer membrane; Reference proteome; Transport. FT CHAIN 1..428 FT /note="Mitochondrial distribution and morphology protein FT 12" FT /id="PRO_0000384277" FT DOMAIN 1..387 FT /note="SMP-LTD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03104" FT REGION 75..168 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 387..428 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 80..94 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 105..135 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 142..161 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 387..407 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 408..428 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 428 AA; 48101 MW; 9603798B40CBFDC4 CRC64; MSFDINWNQL TIDDTINQSI KEFLDQQFKN ISLPSFISNL AVTDFNLGEI PPEVTIRHIG DPFEEFYEDE NNLGVMNEAN NDSKDEHLKN HGDGINKDSG YNSQNLDDED EDDEDDDEDD EDEEEEDEDD YDDHDLGTIN EGISLLNFNE NSTTPSANSF AGSAAPPLPP PLNPSRDSFH SILHPYGVNS IIGATGAGSE TPTNILNQNY LSSRVLPKIS VKQKQPHHDD NDIQLIVEIN YKGDMHINLL VNLLVNYPSP NFISLPIKLH ITDIVIHSIA TIAYLKKSVF LSFLCDVDDT FPDFDSNVQT PTSTTGGNFV DYYSNDATIN KERIDIVKKI KIESEIGEVE NNILRNVGKV EKFLVEQLRN ILRDEIAWPS WICIDMNDDD DEEEEEEESE DNDGGNSDLN DNDGKHGDGR TDETEAGE //