ID MMM1_ASPCL Reviewed; 494 AA. AC A1CM86; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 02-DEC-2020, entry version 61. DE RecName: Full=Maintenance of mitochondrial morphology protein 1 {ECO:0000255|HAMAP-Rule:MF_03103}; GN Name=mmm1 {ECO:0000255|HAMAP-Rule:MF_03103}; ORFNames=ACLA_096060; OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / OS NRRL 1). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=344612; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1; RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046; RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M., RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.; RT "Genomic islands in the pathogenic filamentous fungus Aspergillus RT fumigatus."; RL PLoS Genet. 4:E1000046-E1000046(2008). 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. The CC mdm12-mmm1 subcomplex functions in the major beta-barrel assembly CC pathway that is responsible for biogenesis of all outer membrane beta- CC barrel proteins, and acts in a late step after the SAM complex. The CC mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway CC after the action of the mdm12-mmm1 complex. Essential for establishing CC and maintaining the structure of mitochondria and maintenance of mtDNA CC nucleoids. {ECO:0000255|HAMAP-Rule:MF_03103}. CC -!- SUBUNIT: Homodimer. Component of the ER-mitochondria encounter CC structure (ERMES) or MDM complex, composed of mmm1, mdm10, mdm12 and CC mdm34. A mmm1 homodimer associates with one molecule of mdm12 on each CC side in a pairwise head-to-tail manner, and the SMP-LTD domains of mmm1 CC and mdm12 generate a continuous hydrophobic tunnel for phospholipid CC trafficking. {ECO:0000255|HAMAP-Rule:MF_03103}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000255|HAMAP-Rule:MF_03103}; Single-pass type I membrane protein CC {ECO:0000255|HAMAP-Rule:MF_03103}. Note=The ERMES/MDM complex localizes CC to a few discrete foci (around 10 per single cell), that represent CC mitochondria-endoplasmic reticulum junctions. These foci are often CC found next to mtDNA nucleoids. {ECO:0000255|HAMAP-Rule:MF_03103}. 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_03103}. CC -!- SIMILARITY: Belongs to the MMM1 family. {ECO:0000255|HAMAP- CC Rule:MF_03103}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DS027058; EAW08673.1; -; Genomic_DNA. DR RefSeq; XP_001270099.1; XM_001270098.1. DR SMR; A1CM86; -. DR STRING; 5057.CADACLAP00008765; -. DR EnsemblFungi; EAW08673; EAW08673; ACLA_096060. DR GeneID; 4702260; -. DR KEGG; act:ACLA_096060; -. DR EuPathDB; FungiDB:ACLA_096060; -. DR eggNOG; ENOG502QUUW; Eukaryota. DR HOGENOM; CLU_032730_1_0_1; -. DR OMA; NCRVIPV; -. DR OrthoDB; 1248004at2759; -. DR Proteomes; UP000006701; Unassembled WGS sequence. DR GO; GO:0032865; C:ERMES complex; IEA:UniProtKB-UniRule. DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; 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_03103; Mmm1; 1. DR InterPro; IPR027537; Mmm1. DR InterPro; IPR019411; MMM1_dom. DR InterPro; IPR031468; SMP_LBD. DR PANTHER; PTHR13466:SF5; PTHR13466:SF5; 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 Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..494 FT /note="Maintenance of mitochondrial morphology protein 1" FT /id="PRO_0000384212" FT TOPO_DOM 1..22 FT /note="Lumenal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103" FT TRANSMEM 23..43 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103" FT TOPO_DOM 44..494 FT /note="Cytoplasmic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103" FT DOMAIN 130..387 FT /note="SMP-LTD" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103" SQ SEQUENCE 494 AA; 53099 MW; 283DF95B427E2274 CRC64; MSSQPGDPAT LPAQSSLSFT QGFLLGQLSV VLVLAAFIKF FIFGEAPPPP SRGLSHRSAT HRRSNSIYSN SPQEAGSRSL REKPSTSNVL RPVPSSSTNT RSILRKTYYS AIPTNPAKHG RLRIHHSSHQ PESLDWFNVL IAQTIAQYRQ TAYSLKDSPT SSILNSLTAA LNNPEKKPAF IDKITVTDIS LGEEFPIFSN CRIIAVDDPN SDGGRLQALM DVDLSDDNLS IAIETQLLLN YPKPCSAILP VALSISVVRF SGTLCISLVP ASTPPLDTPS HSPSPPTADT ATSGRSKPGD KAGGNQPRSN GSTEDPAGGN PPKTSPKSNV AFSFLPDYRL DLSVRSLIGS RSRLQDVPKV AQLVEARVQA WFEERVVEPR VQVVGLPDLW PRMGRTGVRT GDDAETASNG PRSTVSADIG GSARHEELAR EPEALRFRGL LGARPPFDVA SRTSSFNVET GDLRSRSMTR QESSGDLSDQ LHIPGSLPEA VTPG //