MMM1_TALMQ
ID MMM1_TALMQ Reviewed; 486 AA.
AC B6QVB2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, 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=PMAA_011910;
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(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; DS995906; EEA18919.1; -; Genomic_DNA.
DR RefSeq; XP_002153304.1; XM_002153268.1.
DR AlphaFoldDB; B6QVB2; -.
DR SMR; B6QVB2; -.
DR STRING; 441960.B6QVB2; -.
DR EnsemblFungi; EEA18919; EEA18919; PMAA_011910.
DR GeneID; 7030678; -.
DR KEGG; tmf:PMAA_011910; -.
DR VEuPathDB; FungiDB:PMAA_011910; -.
DR HOGENOM; CLU_032730_1_0_1; -.
DR OrthoDB; 1248004at2759; -.
DR PhylomeDB; B6QVB2; -.
DR Proteomes; UP000001294; 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..486
FT /note="Maintenance of mitochondrial morphology protein 1"
FT /id="PRO_0000384244"
FT TOPO_DOM 1..23
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TOPO_DOM 45..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT DOMAIN 140..389
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT REGION 52..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 52204 MW; A4F0C2671D0BF43F CRC64;
MSQHSQYDAP GVPVQPSLSF TQGFLLGQLS VVLLIGAFIK FFIFGEAPAP PSRGLASRTA
SHHRSYSINQ GDNNVSNNNT SGGSPRTLCE KPSTSNVLRP VPSSATNTRS ILRKTYYNAI
PTQFSHTKQG RHRIQHSTHQ PESLDWFNVL IAQTIAQYRQ TAYLLKDSPT SSILDSLSAA
INDPQKKPSF IDTIKVTDIS LGEEFPIFSN CRVIVVDDPN SDGGRLQALM DVDLSDDNLS
LAIETSLILN YPKPRSAVLP VALSVSVVRF SGTLCISLIP AATEQSPSSA PTPDASNLNV
RTLFQHISAE LNGTAANPTA NPEKKGVPKT NLAFSFLPDY RLDLSVRSLI GSRSRLQDVP
KVAQLVEARI HSWFEERVVE PRVQVVGLPD FWPRKGRTGV RPGEDAEAAA AVAAASASSR
GGAPEATPSV PEEAIIDDSP VRPGLRFRGP AGRYDSGSSF DELPRAGPGL GEPLDIPGSM
PGGRAQ
