ID   A0A9P3PFQ4_LYOSH        Unreviewed;       430 AA.
AC   A0A9P3PFQ4;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   08-NOV-2023, entry version 2.
DE   RecName: Full=Mitochondrial distribution and morphology protein 12 {ECO:0000256|HAMAP-Rule:MF_03104};
DE   AltName: Full=Mitochondrial inheritance component MDM12 {ECO:0000256|HAMAP-Rule:MF_03104};
GN   Name=MDM12 {ECO:0000256|HAMAP-Rule:MF_03104,
GN   ECO:0000313|EMBL:GLB34593.1};
GN   ORFNames=LshimejAT787_0201580 {ECO:0000313|EMBL:GLB34593.1};
OS   Lyophyllum shimeji (Hon-shimeji) (Tricholoma shimeji).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Lyophyllum.
OX   NCBI_TaxID=47721 {ECO:0000313|EMBL:GLB34593.1, ECO:0000313|Proteomes:UP001063166};
RN   [1] {ECO:0000313|EMBL:GLB34593.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AT787 {ECO:0000313|EMBL:GLB34593.1};
RA   Kobayashi Y., Shibata T., Hirakawa H., Shigenobu S., Nishiyama T.,
RA   Yamada A., Hasebe M., Kawaguchi M.;
RT   "The genome of Lyophyllum shimeji provides insight into the initial
RT   evolution of ectomycorrhizal fungal genome.";
RL   Submitted (JUL-2022) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_03104}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03104}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03104}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_03104}.
CC       Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03104};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03104};
CC       Cytoplasmic side {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_03104}.
CC   -!- SIMILARITY: Belongs to the MDM12 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03104}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GLB34593.1}.
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DR   EMBL; BRPK01000002; GLB34593.1; -; Genomic_DNA.
DR   Proteomes; UP001063166; Unassembled WGS sequence.
DR   CDD; cd21672; SMP_Mdm12; 1.
DR   HAMAP; MF_03104; Mdm12; 1.
DR   InterPro; IPR027532; Mdm12.
DR   InterPro; IPR019411; MMM1_dom.
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   Pfam; PF10296; MMM1; 1.
DR   PROSITE; PS51847; SMP; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW   Rule:MF_03104}; Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03104};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03104};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW   ECO:0000256|HAMAP-Rule:MF_03104};
KW   Transport {ECO:0000256|ARBA:ARBA00023055}.
FT   DOMAIN          1..423
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000259|PROSITE:PS51847"
FT   REGION          155..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..217
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   430 AA;  46919 MW;  1E9478092D6B5168 CRC64;
     MSIDLEWSKL DSSLSSYLVD VLNRQLANAE RPSFIGPIQV TSLDFGSTSP DVELVDLRDI
     YRDFLEDDDD DLDRDRGPVK VTEGADPDEE GFEWVPRRAA VVRDEGQGLA YHHLPPHVRY
     GYGGYGSASM YAAPAAPIDP WNLTGFADQR VPPYSGPVYR SPSPATPFHA PSLNDIDADH
     TTADMPPPPK SSPSQAHTSP SQQPPPQSPP QPQPQAPHPN LQIHLHVNWH SDLRITLTTS
     LLINYPSPSF MSLPIKLSIT GLVFTGELAV AYEGERRRVH ICILDDQDPY GPYHVGASDR
     PKRDSMTTAS GGSGGTPPEP ADDEHVGMGV SAGAGAGTPM PPPISMSMSS SQAKGKRVPA
     GQRLLPTIYI ESEIGQADKH VLKNVTRVER FIQDVIRKTV EEELVRHIVA LSTGPRKTTV
     YAVWKRTTLA
//