MDM12_ASPTN
ID MDM12_ASPTN Reviewed; 426 AA.
AC Q0CZL5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 54.
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=ATEG_00869;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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: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=EAU39515.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476594; EAU39515.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001210955.1; XM_001210955.1.
DR AlphaFoldDB; Q0CZL5; -.
DR SMR; Q0CZL5; -.
DR STRING; 341663.Q0CZL5; -.
DR GeneID; 4355630; -.
DR eggNOG; ENOG502S3PB; Eukaryota.
DR OrthoDB; 1179924at2759; -.
DR Proteomes; UP000007963; 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..426
FT /note="Mitochondrial distribution and morphology protein
FT 12"
FT /id="PRO_0000384274"
FT DOMAIN 1..426
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03104"
FT REGION 88..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 426 AA; 47356 MW; F4D6E061F079E941 CRC64;
MSIEVDWKTA TSGPDGEALA ERIRSFIHDK FQQVALPRFI RSVQVHSFDF GTVPPDLEIK
DFCEPFADFY EEDEDDETSE VSEELVSAHG NQWHRTHSEL NEPPYRDEVT MNQPLRDPFD
EGFHPSPLRS PMEHLNPHFL PRAGTPGIPG GTSTIGYHLM SLGGLSGTQT PLAAVAGGTP
FANGWTDHNL GPGNRGHASG PAAGAMRQHR PEDIDSSNPT SRPSTSSTLP SHPSGSNRNS
GDGSHPEEEH LDDPAEPDHP FRFPKMRERR PEDFQVMCRA KYAGDVRLSL TAEILLDYPM
PSFVGLPLKL NITGVTFDGV AVVAYIRKRV NFCFLSAEDA DALIGADDQE TRDKDDHPRS
GLDPTTSPKR QGGLLREIRV ESEIGRKEDG KQVLKNVGKV ERFVLAQVRR IFEEELVFPS
FWTFLI
