ID MDM12_KLULA Reviewed; 305 AA.
AC Q6CUC3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 87.
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};
GN OrderedLocusNames=KLLA0C06028g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382123; CAH01317.1; -; Genomic_DNA.
DR RefSeq; XP_452466.1; XM_452466.1.
DR PDB; 5H54; X-ray; 3.10 A; A=1-239.
DR PDB; 5H55; X-ray; 3.50 A; A=1-305.
DR PDB; 5H5A; X-ray; 2.26 A; A/B/C/D=1-239.
DR PDB; 5H5C; X-ray; 3.31 A; A=1-239.
DR PDBsum; 5H54; -.
DR PDBsum; 5H55; -.
DR PDBsum; 5H5A; -.
DR PDBsum; 5H5C; -.
DR AlphaFoldDB; Q6CUC3; -.
DR SMR; Q6CUC3; -.
DR STRING; 284590.Q6CUC3; -.
DR PaxDb; 284590-Q6CUC3; -.
DR GeneID; 2892491; -.
DR KEGG; kla:KLLA0_C06028g; -.
DR eggNOG; ENOG502QQS2; Eukaryota.
DR HOGENOM; CLU_026794_2_0_1; -.
DR InParanoid; Q6CUC3; -.
DR OMA; AAWPSWI; -.
DR Proteomes; UP000000598; Chromosome C.
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 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Lipid transport; Lipid-binding;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transport.
FT CHAIN 1..305
FT /note="Mitochondrial distribution and morphology protein
FT 12"
FT /id="PRO_0000384288"
FT DOMAIN 1..236
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03104"
FT REGION 233..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:5H5A"
FT HELIX 14..28
FT /evidence="ECO:0007829|PDB:5H5A"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:5H5A"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:5H5A"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:5H5A"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:5H5A"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:5H5A"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5H5A"
FT STRAND 118..140
FT /evidence="ECO:0007829|PDB:5H5A"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:5H5A"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:5H5A"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5H5C"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:5H54"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:5H5A"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:5H5A"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:5H5A"
FT HELIX 202..224
FT /evidence="ECO:0007829|PDB:5H5A"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5H5A"
SQ SEQUENCE 305 AA; 34373 MW; 675E17EB366F8988 CRC64;
MSVEIDWDNI RGDLSVNQGV KDFLNSRLQE FELPSYVNNL KVTNFDLGTM PPNVILKQMD
DPLDEFYSYL LQEGDISKEA AKDKNTDVQL LVELDYKGDM SIELSADLVL NYPSPQFMIL
PVKLRISDIG MHCLCLLAYL KKQLFISFLC DVSDPLLEND KLQVDPSGPN FMGKRALERI
SLIRNIKIHT ELGQLDQGEG SVLRSVGKLE EFLVDLFRNL IRKEAAWPSW IDLDFTPEDP
EDPEEEGREN DLVADSSNDG KDIEMKSGTE ETLGAGIQES VQHVSPAVTS IDQESRVNSN
TSLEE
//
