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 13-FEB-2019, entry version 55.
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}.
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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 HOGENOM; HOG000201075; -.
DR KO; K17764; -.
DR OMA; PILSNCR; -.
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 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
//