ID K1X0N8_MARBU Unreviewed; 414 AA.
AC K1X0N8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Mitochondrial distribution and morphology protein 12 {ECO:0000256|HAMAP-Rule:MF_03104};
DE AltName: Full=Mitochondrial inheritance component MDM12 {ECO:0000256|HAMAP-Rule:MF_03104};
GN Name=MDM12 {ECO:0000256|HAMAP-Rule:MF_03104};
GN ORFNames=MBM_03535 {ECO:0000313|EMBL:EKD18542.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD18542.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD18542.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD18542.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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:0000256|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:0000256|HAMAP-Rule:MF_03104}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000256|HAMAP-
CC Rule:MF_03104}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_03104}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_03104}.
CC Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03104};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03104};
CC Cytoplasmic side {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_03104}.
CC -!- SIMILARITY: Belongs to the MDM12 family. {ECO:0000256|HAMAP-
CC Rule:MF_03104}.
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DR EMBL; JH921433; EKD18542.1; -; Genomic_DNA.
DR RefSeq; XP_007291424.1; XM_007291362.1.
DR AlphaFoldDB; K1X0N8; -.
DR STRING; 1072389.K1X0N8; -.
DR GeneID; 18759470; -.
DR KEGG; mbe:MBM_03535; -.
DR eggNOG; ENOG502S3PB; Eukaryota.
DR HOGENOM; CLU_026794_0_0_1; -.
DR InParanoid; K1X0N8; -.
DR OMA; KRAHFCF; -.
DR OrthoDB; 5559at2759; -.
DR Proteomes; UP000006753; 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:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03104};
KW Kinase {ECO:0000313|EMBL:EKD18542.1};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03104};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03104};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW ECO:0000256|HAMAP-Rule:MF_03104};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Transferase {ECO:0000313|EMBL:EKD18542.1};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT DOMAIN 1..414
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 68..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 414 AA; 46037 MW; 0CA0BAC7E2E582D4 CRC64;
MSIELNWETL TTGPDGVALA ERIRDFVHDK FQTVTLPRFI KGVKVHAFEF GSIAPELEIK
DICDPLPDFY EETEDDYGEE DEGAGQDEGW KARGSDEETS REQRRMDRLE RTNGPSQATR
FPPYIDTRLP GMRSMQNPGD IGSPFLGVST PGISGGTSNL HYFHSQLATG LSGTQTPLAA
VAGAHLPHGW PDYFNLHPNS RGHRHTASGS SLSPPPTADG QVRALREKHS VSTLATSNST
TRPQTRDGLL EESIEEEPTS PPRRFREPKA EDLQTVFRVR YSGDVKLSLT AEILLDYPMP
SFVGIPVKLN ITGLSFDGVA VLAYIRKRAH FCFLSPEDAS SAIGAEDHEV NYHPAGMKMG
GLLHEIKVES EIGQRENGKQ VLKNVGKVEK FVLEQVRRIF EDEFVYPSFW TFLV
//
