ID   MDM12_POSPM             Reviewed;         316 AA.
AC   B8P9E4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 50.
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}; ORFNames=POSPLDRAFT_90856;
OS   Postia placenta (strain ATCC 44394 / Madison 698-R) (Brown rot fungus)
OS   (Poria monticola).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Dacryobolaceae; Postia.
OX   NCBI_TaxID=561896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 44394 / Madison 698-R;
RX   PubMed=19193860; DOI=10.1073/pnas.0809575106;
RA   Martinez D., Challacombe J., Morgenstern I., Hibbett D., Schmoll M.,
RA   Kubicek C.P., Ferreira P., Ruiz-Duenas F.J., Martinez A.T., Kersten P.,
RA   Hammel K.E., Vanden Wymelenberg A., Gaskell J., Lindquist E., Sabat G.,
RA   Splinter BonDurant S., Larrondo L.F., Canessa P., Vicuna R., Yadav J.,
RA   Doddapaneni H., Subramanian V., Pisabarro A.G., Lavin J.L., Oguiza J.A.,
RA   Master E., Henrissat B., Coutinho P.M., Harris P., Magnuson J.K.,
RA   Baker S.E., Bruno K., Kenealy W., Hoegger P.J., Kuees U., Ramaiya P.,
RA   Lucas S., Salamov A., Shapiro H., Tu H., Chee C.L., Misra M., Xie G.,
RA   Teter S., Yaver D., James T., Mokrejs M., Pospisek M., Grigoriev I.V.,
RA   Brettin T., Rokhsar D., Berka R., Cullen D.;
RT   "Genome, transcriptome, and secretome analysis of wood decay fungus Postia
RT   placenta supports unique mechanisms of lignocellulose conversion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:1954-1959(2009).
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}.
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DR   EMBL; EQ966286; EED82486.1; -; Genomic_DNA.
DR   RefSeq; XP_002472318.1; XM_002472273.1.
DR   AlphaFoldDB; B8P9E4; -.
DR   SMR; B8P9E4; -.
DR   STRING; 561896.B8P9E4; -.
DR   EnsemblFungi; EED82486; EED82486; POSPLDRAFT_90856.
DR   KEGG; ppl:POSPLDRAFT_90856; -.
DR   HOGENOM; CLU_026794_1_0_1; -.
DR   InParanoid; B8P9E4; -.
DR   OMA; AAWPSWI; -.
DR   Proteomes; UP000001743; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032865; C:ERMES complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR   GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03104; Mdm12; 1.
DR   InterPro; IPR027532; Mdm12.
DR   InterPro; IPR019411; MMM1_dom.
DR   InterPro; IPR031468; SMP_LBD.
DR   PANTHER; PTHR28204; PTHR28204; 1.
DR   Pfam; PF10296; MMM1; 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..316
FT                   /note="Mitochondrial distribution and morphology protein
FT                   12"
FT                   /id="PRO_0000384307"
FT   DOMAIN          1..312
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03104"
SQ   SEQUENCE   316 AA;  35503 MW;  897B4BFC5154BE9E CRC64;
     MSIDLEWNGL DSSLASSLID ALNRQLSSTS RPSFIGPIEV TSFDFGSVSP DIELVDLRDI
     YRDFLEDDED AEDVEKEAVK ESQWTDEEDD FEWISRKAVR GKGLPQDVPA YHLLPPHMRY
     GRGVPMDMFA STPSLRPTRD IVSVTFPLRV RNGSRPPHQP DGQEPNPHPN LQLHLHITWN
     SNLRLTLTTS LLINYPSPMF MSLPIKLSVT GLLFNGEVVV AYEGERRRVH FETPPEADED
     MPAAAAGTAR AGKPLPIGQR LLPSIYIESE IGQADKHVLK NVTRVERFIQ DVIRKTIEEE
     LVFPNFHTLV LGDSGS