ID A0A2H3T689_FUSOX Unreviewed; 418 AA.
AC A0A2H3T689;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Maintenance of mitochondrial morphology protein 1 {ECO:0000256|HAMAP-Rule:MF_03103};
GN Name=MMM1 {ECO:0000256|HAMAP-Rule:MF_03103};
GN ORFNames=FRV6_01435 {ECO:0000313|EMBL:SCO77223.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO77223.1, ECO:0000313|Proteomes:UP000219369};
RN [1] {ECO:0000313|Proteomes:UP000219369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA Guldener U.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_03103}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03103}; Single-pass type I membrane protein
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_03103}.
CC -!- SIMILARITY: Belongs to the MMM1 family. {ECO:0000256|HAMAP-
CC Rule:MF_03103}.
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DR EMBL; FMJY01000001; SCO77223.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3T689; -.
DR VEuPathDB; FungiDB:FOC1_g10010076; -.
DR VEuPathDB; FungiDB:FOC4_g10009191; -.
DR VEuPathDB; FungiDB:FOIG_08830; -.
DR VEuPathDB; FungiDB:FOMG_07278; -.
DR VEuPathDB; FungiDB:FOXG_10505; -.
DR VEuPathDB; FungiDB:FOZG_09986; -.
DR VEuPathDB; FungiDB:HZS61_002918; -.
DR OrthoDB; 1699636at2759; -.
DR Proteomes; UP000219369; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032865; C:ERMES complex; 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 CDD; cd21671; SMP_Mmm1; 1.
DR HAMAP; MF_03103; Mmm1; 1.
DR InterPro; IPR027537; Mmm1.
DR InterPro; IPR019411; MMM1_dom.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR13466:SF24; MAINTENANCE OF MITOCHONDRIAL MORPHOLOGY PROTEIN 1; 1.
DR PANTHER; PTHR13466; TEX2 PROTEIN-RELATED; 1.
DR Pfam; PF10296; MMM1; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03103};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03103, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03103};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03103}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TOPO_DOM 1..19
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 41..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT DOMAIN 117..333
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 338..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 46532 MW; 7FADD45CCADF5287 CRC64;
MEADTCPRLI EPTLSFTQGL IVGQLSVVLV LAAFIKFFIF GDPPSADVTA SLRATERRSR
TLAHKRSLLS IRSPANRGDR SQDRSLSRKK STVLRNPPTL TIGSILSKAY YNVDSHQPES
LDWFNVLIAQ TIAQFRSDAQ HDDAILDSLT KALNGDSRPD FIDEIRVTEL SLGEDFPILS
NCRIIPVDED GVSLAPGKKF DPATAARDGL RLQARMDVDL SDMLTLAVRT KLILNYPKKL
SAVLPVELAV SVIRFSGTLS ISFIPSNPSQ STPTRMIFNF LDDYRLDFEI RSLLGSRSKL
HNVPKIAQLV EARLHRWFDE RAVEPRFQEI ALPSLWPRKK NTRGPEDAST ERSESIGRSR
GNDAGRDHRE EIRGRGGDAE IRDRGVGGTV RHRRGTRSND SDDFSMPGSL PDFQVAAS
//
