MMM1_CANAL
ID MMM1_CANAL Reviewed; 439 AA.
AC Q59SI5; A0A1D8PL71;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 25-MAY-2022, entry version 82.
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=CAALFM_C400560CA; ORFNames=CaO19.11664, CaO19.4187;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017626; AOW28848.1; -; Genomic_DNA.
DR RefSeq; XP_712641.2; XM_707548.2.
DR AlphaFoldDB; Q59SI5; -.
DR SMR; Q59SI5; -.
DR STRING; 237561.Q59SI5; -.
DR GeneID; 3645744; -.
DR KEGG; cal:CAALFM_C400560CA; -.
DR CGD; CAL0000191719; MMM1.
DR VEuPathDB; FungiDB:C4_00560C_A; -.
DR eggNOG; ENOG502QUUW; Eukaryota.
DR HOGENOM; CLU_032730_2_0_1; -.
DR InParanoid; Q59SI5; -.
DR OrthoDB; 1248004at2759; -.
DR PRO; PR:Q59SI5; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0032865; C:ERMES complex; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
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..439
FT /note="Maintenance of mitochondrial morphology protein 1"
FT /id="PRO_0000384221"
FT TOPO_DOM 1..76
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TOPO_DOM 98..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT DOMAIN 165..395
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT REGION 125..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 439 AA; 49014 MW; 06598CBB019A1846 CRC64;
MSQDLIETTA TTTKIVEARE LGHQIHDSLL EQLKLQQEEL LQQQRDLFFQ EQQLQLQQQV
TQPVSNNGNT WSFTQGLVIG QVSVIFIIIV FVKFFVFADS SSHIPTKPGL DGATGVIVKR
NKNKKHSNGQ FANDGENEDD TSLDSNQSKI SSILEKTYYD VNNHASESLD WFNVLVAQTI
SQLRSEALLK DNIYHSLNNF LTNAKLPDFI DTINLTEIDI GDDFPIFSNC RIKYGEDLKR
LEAKIDVDLS DTLTLGIATK LLLNQPRPLT AVLPVSLTVS IVRFSGCLTV SLINTKDIDL
KNVDKTSNMN GYSKENANGD GASSSNNDED EDDGGTALMF SFSPDYRLEF IVKSLIGSRA
KLQDVPKISS LIENQLRTWF IERCVEPRFQ VVRLPSLWPR TKNTREPVTK KTTTTPSTTV
NGTSAATITT PGEYVNSNI
