MMM1_ASPTN
ID MMM1_ASPTN Reviewed; 486 AA.
AC Q0CH31;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 25-MAY-2022, entry version 61.
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=ATEG_07011;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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: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=EAU32395.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476603; EAU32395.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001209697.1; XM_001209697.1.
DR AlphaFoldDB; Q0CH31; -.
DR SMR; Q0CH31; -.
DR STRING; 341663.Q0CH31; -.
DR EnsemblFungi; EAU32395; EAU32395; ATEG_07011.
DR GeneID; 4319267; -.
DR eggNOG; ENOG502QUUW; Eukaryota.
DR OrthoDB; 1248004at2759; -.
DR Proteomes; UP000007963; 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..486
FT /note="Maintenance of mitochondrial morphology protein 1"
FT /id="PRO_0000384218"
FT TOPO_DOM 1..20
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TOPO_DOM 42..486
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT DOMAIN 128..379
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT REGION 70..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 486 AA; 52500 MW; 30653F8FEF3A3823 CRC64;
MNFQQSAIPP FSFLLSFTQG FLLGQLSVVL LIGAFIKFFI FGEAPPPPSR GLSHRASTHR
RSNSIYTIST NEAGSRSLRE KPSTSNVLRP VPSSSTNTRS ILRKTYYGAI PTNPSKHGRH
RVHHSSHQPE SLDWFNVLIA QTIAQYRQTA YLLKDEPTSS ILSSLTAALN NPEKKPSFID
KITVTDISLG EEFPIFSNCR IIAVDDPNSD GGRLQALMDV DLSDDNLSIG IETSLLLNYP
KPGSAILPVA LSISVVRFSG TLCISLVPAS TPPLHTPSPS PAPQTADGAR TQSQPENNSS
NPNQQSADAS GAPPKTSPKS NVAFSFLPDY RLDLSVRSLI GSRSRLQDVP KVAQLVEARV
HAWFEERVVE PRVQVVGLPD LWPRMGRTGV RTGEDSETGS NAASRSAISA DLGSSLRDDL
DQGPDGLRFR GPLGARPQFD SVSRSSSFNV ETGGFHGHPM TREDSRGAIS DDFHMPGSLP
DGAVGN
