MMM1_ASPFU
ID MMM1_ASPFU Reviewed; 496 AA.
AC Q4WDE0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 83.
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=AFUA_6G04420;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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 -!- SEQUENCE CAUTION:
CC Sequence=EAL85598.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAHF01000012; EAL85598.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_747636.1; XM_742543.1.
DR AlphaFoldDB; Q4WDE0; -.
DR SMR; Q4WDE0; -.
DR STRING; 746128.CADAFUBP00009124; -.
DR GeneID; 3505297; -.
DR KEGG; afm:AFUA_6G04420; -.
DR VEuPathDB; FungiDB:Afu6g04420; -.
DR eggNOG; ENOG502QUUW; Eukaryota.
DR HOGENOM; CLU_032730_1_0_1; -.
DR InParanoid; Q4WDE0; -.
DR OrthoDB; 1248004at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..496
FT /note="Maintenance of mitochondrial morphology protein 1"
FT /id="PRO_0000384214"
FT TOPO_DOM 1..22
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TOPO_DOM 44..496
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT DOMAIN 131..388
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT REGION 50..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 53664 MW; EB10261E78BD005E CRC64;
MSSQLNDPTP IPAQSSLSFT QGFLLGQLSV VLLIAAFIKF FIFGEAPPPP SRGLSHRSAT
HRRSNSIFSS AQHDGSTRTL REKPSNSNVL RPVPSSATNT RSILRKTYYT AIPTNPSSKH
GRHRIHHSSH QPESLDWFNV LIAQTIAQYR QTAYLLKDSP TSSILNSLTA ALNNPEKKPS
FIDKITVTDI SLGEEFPIFS NCRIIAVDDP NSDGGRLQAL MDVDLSDDNL SIAVETQLLL
NYPKPCSAIL PVALSISVVR FSGTLCISLV PASTPPLDTP SHSPSPPTAQ TTTAGRSKRE
DQTSGSHSHA GGSSKEPSGE NPPKTSPKSN VAFSFLPDYR LDLSVRSLIG SRSRLQDVPK
VAQLVEARVH AWFEERVVEP RVQVVGLPDL WPRMGRTGVR TGDDSETGSN VPRSSTAADA
SGSARHEDSS REPEVLRFGS LLGTRPPFDL ASRTSSFNVE TGDLRSRSMT REESNGNLSD
QFHMPGSLPG SGVATT
