MMM1_UNCRE
ID MMM1_UNCRE Reviewed; 497 AA.
AC C4JP24;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 53.
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=UREG_03083;
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH476616; EEP78238.1; -; Genomic_DNA.
DR RefSeq; XP_002543567.1; XM_002543521.1.
DR AlphaFoldDB; C4JP24; -.
DR SMR; C4JP24; -.
DR STRING; 33188.XP_002543567.1; -.
DR EnsemblFungi; EEP78238; EEP78238; UREG_03083.
DR GeneID; 8439430; -.
DR KEGG; ure:UREG_03083; -.
DR VEuPathDB; FungiDB:UREG_03083; -.
DR eggNOG; ENOG502QUUW; Eukaryota.
DR HOGENOM; CLU_032730_1_0_1; -.
DR InParanoid; C4JP24; -.
DR OrthoDB; 1248004at2759; -.
DR Proteomes; UP000002058; 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..497
FT /note="Maintenance of mitochondrial morphology protein 1"
FT /id="PRO_0000384257"
FT TOPO_DOM 1..28
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TRANSMEM 29..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TOPO_DOM 56..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT DOMAIN 140..393
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT REGION 60..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 54209 MW; FAB43BF48434AC9F CRC64;
MSSVLNPSSP HSWDLCCSSS SNRSYHRPTH PIVGLLVGQL SVVLLIGAFI KFFIFGEAPP
SPSRSQTHRT SQHKRSYSIH GARDLSPRTL KEKPSSNVLR PVPSSSTNTR SILRKTYYSA
NPTNFPSKHG RHRPHHSTHQ PESLDWFNVL IAQTIAQYRQ TAYILKDSPT ASILESLATT
LNNPEKKPSF IDEITVTDIS LGEEFPIFSN CRVIAIDDPN SDGGRLQALM DVDLSDDNLS
LAIETNLVLN YPKPYSAILP VALSVSVVRF SGTLCISFVP GTTESSTNLT PTSSNIDTNL
RSNELRGKTA PQESSTTDEG SQGGATSTTG IPKTSLAFSF LPDYRLDLSV RSLIGSRSRL
QDVPKVAQLV EARVHAWFEE RVVEPRVQVV ALPGIWPRMG RTGVRGQEEQ PDVSSSDAAG
VSGAKVSMLG SRDTGAEMLH AAREVDAEGL RYRRNPPPGD KGSSSKYAQQ NQSSRERGRA
DDPFRIPGSL PDAVPIT
