ID A0A0D2DGM1_9EURO Unreviewed; 443 AA.
AC A0A0D2DGM1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 ORFNames=PV07_01656 {ECO:0000313|EMBL:KIW34914.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW34914.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW34914.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW34914.1,
RC ECO:0000313|Proteomes:UP000054466};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847040; KIW34914.1; -; Genomic_DNA.
DR RefSeq; XP_016255130.1; XM_016388202.1.
DR AlphaFoldDB; A0A0D2DGM1; -.
DR STRING; 569365.A0A0D2DGM1; -.
DR GeneID; 27340850; -.
DR VEuPathDB; FungiDB:PV07_01656; -.
DR HOGENOM; CLU_026794_0_0_1; -.
DR OrthoDB; 5559at2759; -.
DR Proteomes; UP000054466; 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 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|HAMAP-Rule:MF_03104};
KW 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|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03104};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW ECO:0000256|HAMAP-Rule:MF_03104};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT DOMAIN 1..443
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 73..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 47375 MW; 42ADC6954793D2D9 CRC64;
MSVDIGWEKI TSGPDGAALA EKIRAFVHDK FQQIPLPRFI NAVHVHSFEL GSVCPEIEIK
DICDPLPDFY EDEEEDEVGA DQEVDESAIG SAQNDGVETG SHYEARESAS SSQQPRSVPQ
LSNIITGSGL AHLNASTSAK EGLSAGDEAF AGPFPRSTTP GIPGGTSNLS YFHFPGGGLS
GTQTPLAAVA SGTPFSPRPW SYDPSHNFAM MHQTPIHGAT HVKPMAQDVT GHDDPSTRPS
TANSISSPRG SESGPSSPQL PHRAQPAGEN GQGDTTLDAL TPLSASRLQS RQASDLQVVA
RVKYSGDVRM TLTAEILLDY PMPSFVGIPL KLAITGLTFD GVAIVAWVKK KMHFCFLDSE
DAATLVGESV TNNHRKKAGG TTGSGTGVPG PLQEIHVESE IGRQEDGKQV LKNVGKVEKF
VLEQVRKIFE EEFVFPSYWT FLV
//
