MMM1_NEUCR
ID MMM1_NEUCR Reviewed; 415 AA.
AC Q9P353;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Maintenance of mitochondrial morphology protein 1 {ECO:0000255|HAMAP-Rule:MF_03103};
GN Name=mmm-1; ORFNames=NCU06193;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC STRAIN=ATCC 14692 / FGSC 262 / 74A;
RX PubMed=10982393; DOI=10.1091/mbc.11.9.2961;
RA Prokisch H., Neupert W., Westermann B.;
RT "Role of MMM1 in maintaining mitochondrial morphology in Neurospora
RT crassa.";
RL Mol. Biol. Cell 11:2961-2971(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Component of the ERMES/MDM complex, which serves as a
CC molecular tether to connect the endoplasmic reticulum (ER) and
CC mitochondria (By similarity). Components of this complex are involved
CC in the control of mitochondrial shape and protein biogenesis, and
CC function in nonvesicular lipid trafficking between the ER and
CC mitochondria (PubMed:10982393). The mdm12-mmm-1 subcomplex functions in
CC the major beta-barrel assembly pathway that is responsible for
CC biogenesis of all outer membrane beta-barrel proteins, and acts in a
CC late step after the SAM complex. The mdm10-mdm12-mmm-1 subcomplex
CC further acts in the TOM40-specific pathway after the action of the
CC mdm12-mmm-1 complex. Essential for establishing and maintaining the
CC structure of mitochondria and maintenance of mtDNA nucleoids (By
CC similarity). {ECO:0000255|HAMAP-Rule:MF_03103,
CC ECO:0000269|PubMed:10982393}.
CC -!- SUBUNIT: Homodimer. Component of the ER-mitochondria encounter
CC structure (ERMES) or MDM complex, composed of mmm-1, mdm10, mdm12 and
CC mdm34. A mmm-1 homodimer associates with one molecule of mdm12 on each
CC side in a pairwise head-to-tail manner, and the SMP-LTD domains of mmm-
CC 1 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; AF238480; AAF43713.1; -; Genomic_DNA.
DR EMBL; AF239620; AAF43714.1; -; mRNA.
DR EMBL; CM002238; EAA33769.1; -; Genomic_DNA.
DR RefSeq; XP_963005.1; XM_957912.2.
DR AlphaFoldDB; Q9P353; -.
DR SMR; Q9P353; -.
DR STRING; 5141.EFNCRP00000006009; -.
DR EnsemblFungi; EAA33769; EAA33769; NCU06193.
DR GeneID; 3879153; -.
DR KEGG; ncr:NCU06193; -.
DR VEuPathDB; FungiDB:NCU06193; -.
DR HOGENOM; CLU_032730_1_0_1; -.
DR InParanoid; Q9P353; -.
DR OMA; KWFVERC; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0032865; C:ERMES complex; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0120013; F:lipid transfer activity; IEA:EnsemblFungi.
DR GO; GO:0015917; P:aminophospholipid transport; IEA:EnsemblFungi.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IEA:EnsemblFungi.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IBA:GO_Central.
DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..415
FT /note="Maintenance of mitochondrial morphology protein 1"
FT /id="PRO_0000384239"
FT TOPO_DOM 1..18
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TOPO_DOM 40..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT DOMAIN 114..330
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT REGION 373..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 46087 MW; 20474EA6208FFAFB CRC64;
MADICPSRSE PTLSFTQGLI LGQLSVVLLL AAFIKFFIFG DPPSPEVVAS IRATDRRSRT
LAHKKSILSL RETNALQLVQ NPALNKKHVL RPGPPILTIG SILSKTYYKV DSHQPESLDW
FNVLIAQTIA QFRSDAQHDD AILSSLSKAL NGTARPDFLD EIKVTELSLG EDFPIFSNCR
IIPVDEDGLS FGTGKAFDAN MATREGARLQ ARMDVDLSDM ITLAVETKLL LNYPKRLSAV
LPVALAVSVV RFSGTLSISF IPSNPSNNEP AKMIFTFLDD YRLDFSIRSL LGSRSRLQDV
PKIAQLVESR LHRWFDERCV EPRFQEIALP NMWPRKKNTR GGDETISDVE RSMSKAKGVD
IAKDVREEAR KEIEAEAHGG ADRVPDSLRY RHRPRADEEF PGAGSMPGSM PGSMP
