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 23-MAY-2018, entry version 50. 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 OS 3887 / NRRL 1). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. 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., RA Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., RA Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., RA Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R., RA Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M., RA Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R., RA Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R., RA 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 CC control of mitochondrial shape and protein biogenesis, and CC function in nonvesicular lipid trafficking between the ER and CC mitochondria. The mdm12-mmm1 subcomplex functions in the major CC beta-barrel assembly pathway that is responsible for biogenesis of CC all outer membrane beta-barrel proteins, and acts in a late step CC after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further CC acts in the TOM40-specific pathway after the action of the mdm12- CC mmm1 complex. Essential for establishing and maintaining the CC structure of mitochondria and maintenance of mtDNA nucleoids. CC {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 CC and mdm34. A mmm1 homodimer associates with one molecule of mdm12 CC on each side in a pairwise head-to-tail manner, and the SMP-LTD CC domains of mmm1 and mdm12 generate a continuous hydrophobic tunnel CC for phospholipid 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 CC protein {ECO:0000255|HAMAP-Rule:MF_03103}. Note=The ERMES/MDM CC complex localizes to a few discrete foci (around 10 per single CC cell), that represent mitochondria-endoplasmic reticulum CC junctions. These foci are often found next to mtDNA nucleoids. CC {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 CC their 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; CADACLAT00008989; CADACLAP00008765; CADACLAG00008989. DR GeneID; 4702260; -. DR KEGG; act:ACLA_096060; -. DR EuPathDB; FungiDB:ACLA_096060; -. DR HOGENOM; HOG000201075; -. DR KO; K17764; -. DR OMA; ERCVEPR; -. DR OrthoDB; EOG092C2Z53; -. DR Proteomes; UP000006701; Unassembled WGS sequence. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032865; C:ERMES complex; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; 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:0007005; P:mitochondrion organization; IEA:InterPro. 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 Complete proteome; Endoplasmic reticulum; Lipid transport; KW Lipid-binding; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 494 Maintenance of mitochondrial morphology FT protein 1. FT /FTId=PRO_0000384212. FT TOPO_DOM 1 22 Lumenal. {ECO:0000255|HAMAP- FT Rule:MF_03103}. FT TRANSMEM 23 43 Helical. {ECO:0000255|HAMAP- FT Rule:MF_03103}. FT TOPO_DOM 44 494 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_03103}. FT DOMAIN 130 387 SMP-LTD. {ECO:0000255|HAMAP- FT 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 //