ID   MMM1_CANGA              Reviewed;         431 AA.
AC   Q6FVT7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Maintenance of mitochondrial morphology protein 1 {ECO:0000255|HAMAP-Rule:MF_03103};
GN   Name=MMM1 {ECO:0000255|HAMAP-Rule:MF_03103};
GN   OrderedLocusNames=CAGL0D05698g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380950; CAG58568.1; -; Genomic_DNA.
DR   RefSeq; XP_445657.1; XM_445657.1.
DR   AlphaFoldDB; Q6FVT7; -.
DR   SMR; Q6FVT7; -.
DR   STRING; 5478.XP_445657.1; -.
DR   EnsemblFungi; CAG58568; CAG58568; CAGL0D05698g.
DR   GeneID; 2886986; -.
DR   KEGG; cgr:CAGL0D05698g; -.
DR   CGD; CAL0128273; CAGL0D05698g.
DR   VEuPathDB; FungiDB:CAGL0D05698g; -.
DR   eggNOG; ENOG502QUUW; Eukaryota.
DR   HOGENOM; CLU_032730_2_0_1; -.
DR   InParanoid; Q6FVT7; -.
DR   OMA; KWFVERC; -.
DR   Proteomes; UP000002428; Chromosome D.
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:0120013; F:lipid transfer activity; IEA:EnsemblFungi.
DR   GO; GO:0015917; P:aminophospholipid transport; IEA:EnsemblFungi.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR   GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IEA:EnsemblFungi.
DR   GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IEA:EnsemblFungi.
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..431
FT                   /note="Maintenance of mitochondrial morphology protein 1"
FT                   /id="PRO_0000384223"
FT   TOPO_DOM        1..103
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   TOPO_DOM        125..431
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   DOMAIN          192..404
FT                   /note="SMP-LTD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT   REGION          412..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   431 AA;  49568 MW;  9EA6B2090C9FC2F9 CRC64;
     MVSALEVKSI KDSNETLISL DDYIRNTLPS QLHEILLEEF QNQDFSRGQD VSNSTHDQMI
     DHTLELTSDL LRNALDKQLM EVQSRTLPVR QSNQLISWSF AQGLIIGQLS VVIFLIFFVK
     FFIFTDASSK MDNPLPSKVS KSYLKNRRES SSIKDKRKGV LVKEESGETD LHGSLQLNDI
     LEKTYYNVDT HSAESLDWFN VLLAQMIQQF REEAWHKDNI LTSLDSFIQK RSSDLPDYLD
     KITITELDIG EDFPIFSNCR IQYAPNSSDK KLEAKIDIDL NDKITFGMST RLLLNYPKKC
     TAALPIDLAV SMVRFQACLT VSLITAEELE FTTGNKIDDN EKNGYYLVFS FTPEYKIDFD
     IKSLIGARSK LENIPKISNI IEYNIKKWFA ERCVEPRFQS VKLPGMWPRS KNTREEVIHK
     TEDESSKTPH S