ID   MMM1_ARTOC              Reviewed;         471 AA.
AC   C5FRT9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=MCYG_05411;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(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. 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}.
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DR   EMBL; DS995705; EEQ32592.1; -; Genomic_DNA.
DR   RefSeq; XP_002845542.1; XM_002845496.1.
DR   AlphaFoldDB; C5FRT9; -.
DR   SMR; C5FRT9; -.
DR   STRING; 63405.XP_002845542.1; -.
DR   EnsemblFungi; EEQ32592; EEQ32592; MCYG_05411.
DR   GeneID; 9228752; -.
DR   eggNOG; ENOG502QUUW; Eukaryota.
DR   HOGENOM; CLU_032730_1_0_1; -.
DR   OMA; KWFVERC; -.
DR   OrthoDB; 1248004at2759; -.
DR   Proteomes; UP000002035; 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..471
FT                   /note="Maintenance of mitochondrial morphology protein 1"
FT                   /id="PRO_0000384237"
FT   TOPO_DOM        1..21
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   TOPO_DOM        43..471
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   DOMAIN          128..370
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   REGION          271..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   471 AA;  51703 MW;  FDBFF99769DEFD50 CRC64;
     MSSPQNTSCP PSQHSLSFTQ GLLLGQLSVV LLIGAFIKFF IFGESPSSSS RGISQRTAPR
     KRSYSVNSTL FRDAASRSLK ESASSNVLRP VPSSSTNTKS ILRKTYYNAI PTNFQKNSRH
     RLHHSTHQPE SLDWFNVLIA QLIAQYRQTA YILKDSPTSS ILDSLTETLN NVDKKPSWID
     RINVTDISIG EEFPIFSNCR VIAVEDPNSD GGRLQALMDV DLSDDNLSLA IETNLLLNYP
     KPASAVLPVA LSVSVVRFSG TLCISFVPSP GTTESSPHLP HPENQNESKP SRQDPEIPTN
     KDGVRSGIPK TSLAFSFLPD YRLDISVRSL IGSRSRLQDV PKVAQLVEAR VQSWFEDRVV
     EPRVQLVALP GIWPRMGRTG VRAQEDHDAV SIDSEDPATK ATHSGFTPVN ANRDGLQASR
     DLNMEGLRYR RGNAGDEATT DEYERLTRGD TQSVGEQLRI PGSLPGAPAV A