ID A0A2C5Y8D5_9HYPO Unreviewed; 421 AA.
AC A0A2C5Y8D5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CDD83_2442 {ECO:0000313|EMBL:PHH84119.1};
OS Cordyceps sp. RAO-2017.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=2004951 {ECO:0000313|EMBL:PHH84119.1, ECO:0000313|Proteomes:UP000221130};
RN [1] {ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|Proteomes:UP000221130};
RA de Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHH84119.1, ECO:0000313|Proteomes:UP000221130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1346 {ECO:0000313|EMBL:PHH84119.1,
RC ECO:0000313|Proteomes:UP000221130};
RA De Bekker C., Evans H.C., Brachmann A., Hughes D.P.;
RT "Ant-infecting Ophiocordyceps genomes reveal a high diversity of potential
RT behavioral manipulation genes and a possible major role for enterotoxins.";
RL Submitted (OCT-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PHH84119.1}.
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DR EMBL; NJEV01001587; PHH84119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5Y8D5; -.
DR STRING; 2004951.A0A2C5Y8D5; -.
DR OrthoDB; 1699636at2759; -.
DR Proteomes; UP000221130; 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 Reference proteome {ECO:0000313|Proteomes:UP000221130};
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..21
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 43..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT DOMAIN 115..331
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 336..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 421 AA; 46487 MW; 9CE97889BE6EC7C0 CRC64;
MSFNTCHSGP ESACRLSFTQ GLIIGQLSVV LILAAFIKFF IFGDPLSSDA SASLRATERR
ARTLAHKQSL LSLRSPSQLK GQVLNRKKSS ILRNPPALTI GSILSKTYYN VDSHQPESLD
WFNVLVAQTI AQFRSDAQHD DAILDSLTKA LNGTSRPDFV DDIRVTELSL GDDFPIFSNC
RIIPVDEDGL TPGNGIKFDA ALAARDGTRL QARLDVDLSD MLTLAVETKL LLNYPKRQSA
ILPVALSVSV VRFSGTLSIS FIPSNPSQAT PAMMAFNFLD DYRLDFSIRS LLGSRSRLQD
VPKIAQLVEA RLHRWFDERA VEPRFQEIAL PSLWPRKKNT RGPDDAMTDG GGSVGRMRGR
EVGRDVRDEM VRGEADRREG ISSMRHRRRQ DSPDDQEIFM PGSLPGERAG VRSGALSSNG
S
//
