MDM12_CANDC
ID MDM12_CANDC Reviewed; 422 AA.
AC B9WK07;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=CD36_71040;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(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; FM992694; CAX40658.1; -; Genomic_DNA.
DR RefSeq; XP_002421324.1; XM_002421279.1.
DR AlphaFoldDB; B9WK07; -.
DR SMR; B9WK07; -.
DR STRING; 42374.XP_002421324.1; -.
DR EnsemblFungi; CAX40658; CAX40658; CD36_71040.
DR GeneID; 8049291; -.
DR KEGG; cdu:CD36_71040; -.
DR CGD; CAL0000170981; Cd36_71040.
DR VEuPathDB; FungiDB:CD36_71040; -.
DR eggNOG; ENOG502S3PB; Eukaryota.
DR HOGENOM; CLU_026794_2_0_1; -.
DR OrthoDB; 1179924at2759; -.
DR Proteomes; UP000002605; Chromosome 7.
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; IPR031468; SMP_LBD.
DR PANTHER; PTHR28204; PTHR28204; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Transport.
FT CHAIN 1..422
FT /note="Mitochondrial distribution and morphology protein
FT 12"
FT /id="PRO_0000384278"
FT DOMAIN 1..386
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03104"
FT REGION 74..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..132
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..402
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 47136 MW; A9032B7DC625302D CRC64;
MSFDINWNQL TIDDTINQSI KEFLDQQFKK ISLPSFISNL SVTDFNLGEI PPEITIRHIG
DPFEEFYEDE DNLGATNETN HNLNDERSTM GKSQENGIHK DNAYNSQNFD DDDDDDEGVD
EDDDDDEYDD HDLGTINEGI SLLNFNDSST TPSGNSFGGS IAPLPPPPLN PSRDSFHSIL
HPYGVNSIIG ATGAGSETPT NILNQNYLSS RVLPKISVKQ KQPHHDDNDI QLIVEINYKG
DMHINLLVNL LVNYPSPNFI SLPIKLHITD IVIHSIATIA YLKKSVYLSF LCDVDDAFPD
FDSNNNAQTP TSTTGGNFVD YYSNDAAINK ERIDIVKKIK IESEIGEVEN NILRNVGKVE
KFLVEQLRNI LRDEIAWPSW ICIDMNDDGD DDDDDEVEDS NVSDGDGKDN DGKHGDGPTH
EV
