ID   MDM12_TALSN             Reviewed;         491 AA.
AC   B8M2V6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   25-MAY-2022, entry version 53.
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=TSTA_094570;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EED22211.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; EQ962653; EED22211.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002479174.1; XM_002479129.1.
DR   AlphaFoldDB; B8M2V6; -.
DR   SMR; B8M2V6; -.
DR   STRING; 441959.B8M2V6; -.
DR   EnsemblFungi; EED22211; EED22211; TSTA_094570.
DR   GeneID; 8103785; -.
DR   eggNOG; ENOG502S1MJ; Eukaryota.
DR   HOGENOM; CLU_026794_0_0_1; -.
DR   InParanoid; B8M2V6; -.
DR   OrthoDB; 1179924at2759; -.
DR   Proteomes; UP000001745; 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..491
FT                   /note="Mitochondrial distribution and morphology protein
FT                   12"
FT                   /id="PRO_0000384314"
FT   DOMAIN          1..491
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03104"
FT   REGION          72..123
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          389..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..86
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  54300 MW;  74AEFB4E46F05F09 CRC64;
     MSIDLNWEAA TSGPDGEQLA ERIRSFIHDK FQQVPLPRFI RSVNVHSFEF GSIAPELEIK
     DICDPFVDFY EESDSSEDED GEGHDAESDT SSDRAADSTA DKRDMRYGHD DRGNNGHIPN
     HHDHLRTSQW VAGGTDGHST QSPLRSPIGL GDHLNAHFRS TTPNILPGVT SNLGYHLMMG
     NLSGTQTPLA AVAGGTPFGP GWPDAVMNQG SRMTDHTTGR TRREDHNKNE TGSPSRPSTA
     HTNPTQLSHG RSAASSSNNT SNDPTVIYND HTSSTTATTY GLHEGGDRPR DKHGHRIDQE
     EPPPSPTPHM RERRPEDFQV ICRVKYAGDV KLSLTAEILL DYPMPSFVGL PLKLNITGIT
     FDGVAVVAYI RRRAHLCFLS PEDADALLGD EDDIQHPSYS TANTTTAASG SSTDNNNNNN
     ESNDHPNHPP QPRRRFGSLL QQIRVDSEIG RKENGKQALK NVGKVERFVL DQVRRIFEDE
     FVFPSYWTFL V