MMM1_BLAGS
ID MMM1_BLAGS Reviewed; 540 AA.
AC C5JYV0; A0A179UW91;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 51.
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=BDBG_07723;
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081;
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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; GG657467; OAT12375.1; -; Genomic_DNA.
DR RefSeq; XP_002621884.1; XM_002621838.1.
DR AlphaFoldDB; C5JYV0; -.
DR SMR; C5JYV0; -.
DR STRING; 559298.C5JYV0; -.
DR EnsemblFungi; OAT12375; OAT12375; BDBG_07723.
DR GeneID; 8508790; -.
DR KEGG; bgh:BDBG_07723; -.
DR VEuPathDB; FungiDB:BDBG_07723; -.
DR HOGENOM; CLU_032730_2_0_1; -.
DR Proteomes; UP000002038; 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..540
FT /note="Maintenance of mitochondrial morphology protein 1"
FT /id="PRO_0000384210"
FT TOPO_DOM 1..25
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TOPO_DOM 47..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT DOMAIN 134..409
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT REGION 52..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 56395 MW; 576688279FC1E197 CRC64;
MAGPSNQTQP PPPVLTQPSL SFTQGLLVGQ LSVVLLIGAF IKFFIFGEAP PHPSRNGLSN
RTSSHRRSYS LNSISADSSP RTLREKPSTS NILRPVPSSS TNTRSILRKT YYSATPTNPT
SKHSRSRPHH SSHQPESLDW FNVLIAQTIA QYRQTAYILK DSPTSSILAS LSEALNNPEK
KPSFIDSIKV TDISLGEEFP IFSNCRVIAV EDPNSDGGRL QALMDVDLSD DNLSLAVETS
LLLNYPKPFS AVLPVALAVS VVRFSGTLCI SFVPGPGTSD QTMSPSPSPP KEASAENIAV
DHQSPERQSA RQRAPHQHKY TNTNTAGATA AATADDNDTH AKLPHGIPKT SLAFSFLPDY
RLDLSVRSLI GSRSRLQDVP KVAQLVEARV QAWFEERVVE PRVQVVGLPN IWPRMGRTGV
RGSQEETEAG AGGSAPADIP GTAGGDGVGV RGGGGGGGGG GGVGGSGGGS MRGTSGWGMG
YDGLRYRHNA HGDGGVGAGP GQSAGAALYG GAQGGGGGGG RGGEEQFAIP GSMPDPVVVT
