MDM12_TALMQ
ID MDM12_TALMQ Reviewed; 489 AA.
AC B6QAV0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 57.
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=PMAA_074010;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995900; EEA26328.1; -; Genomic_DNA.
DR RefSeq; XP_002146875.1; XM_002146839.1.
DR AlphaFoldDB; B6QAV0; -.
DR SMR; B6QAV0; -.
DR STRING; 441960.B6QAV0; -.
DR EnsemblFungi; EEA26328; EEA26328; PMAA_074010.
DR GeneID; 7024528; -.
DR KEGG; tmf:PMAA_074010; -.
DR VEuPathDB; FungiDB:PMAA_074010; -.
DR HOGENOM; CLU_026794_0_0_1; -.
DR OrthoDB; 1179924at2759; -.
DR PhylomeDB; B6QAV0; -.
DR Proteomes; UP000001294; 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..489
FT /note="Mitochondrial distribution and morphology protein
FT 12"
FT /id="PRO_0000384301"
FT DOMAIN 1..489
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03104"
FT REGION 72..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 54232 MW; 54C210A99D1C4E92 CRC64;
MSIDLNWEAA TSGPDGEQLA ERIRCFIHDK FQQVPLPRFI RSVNVHSFEF GSIAPELEIK
DICDPFVDFY EESDSEDEDE GHEDIQSDAS SDRAAADKRG MRYRHDNNGH DEHGTNHHDH
LRTSQWVTGE IDGHHQSAQS PLRSPIGLGD HLNAQFRSTT PNILPGVTSN LGYHLMMGNL
SGTQTPLVAV AGGGTPFGTG WPDAVMHGGS QLAGQPHGRG RGREENNNNN LDTGSPSRPS
TANTNPTQLS HGQSAAGSSS NNTSNDPTVI YNDHASSTTA TAHGLHEGRE KQAPTSIIDQ
ESPPSPTPHM RERRPEDFQV ICRVKYAGDV KLSLTAEILL DYPMPSFVGL PLKLNITGIT
FDGVAVVAYI RRRAHLCFLS PEDADALLGD EEEDINHQQR QQQQQQHPYP TTNTSESINN
NNPETHPPQP RRRFGSLLQQ IRVDSEIGRK ENGKQALKNV GKVERFVLDQ VRRIFEDEFV
FPSFWTFLV
