MMM1_PHANO
ID MMM1_PHANO Reviewed; 500 AA.
AC Q0TYM0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=SNOG_15291;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
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DR EMBL; CH445361; EAT77224.1; -; Genomic_DNA.
DR RefSeq; XP_001805445.1; XM_001805393.1.
DR AlphaFoldDB; Q0TYM0; -.
DR SMR; Q0TYM0; -.
DR STRING; 13684.SNOT_15291; -.
DR EnsemblFungi; SNOT_15291; SNOT_15291; SNOG_15291.
DR GeneID; 5982374; -.
DR KEGG; pno:SNOG_15291; -.
DR eggNOG; ENOG502QUUW; Eukaryota.
DR HOGENOM; CLU_032730_1_0_1; -.
DR InParanoid; Q0TYM0; -.
DR OMA; KWFVERC; -.
DR OrthoDB; 1248004at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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..500
FT /note="Maintenance of mitochondrial morphology protein 1"
FT /id="PRO_0000384245"
FT TOPO_DOM 1..42
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TOPO_DOM 64..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT DOMAIN 141..375
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT REGION 283..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 55208 MW; 854AEF7BF26D3A59 CRC64;
MATQVATPLS PSYTSELIIV CHHVLQHSPT PLTPHSLSFT QGFLLGQLSI ALLIFFFIKF
FIFGEPPSAD DRSLHLNSLR RARTLAHQQS IKQLRTRSNS ISLSLRHKDS RSIIRKGEET
RGGPSIATIL AKTYYNVKGH QPESLDWFNV LIAQTIAQLR ADARQDDAIL GSLTEVLNSG
SKPDWIGEIK VNEIALGDEF PIFSNCRVMP AEDGFWYGPG TTGTEEGRLQ ARMDVDLSDV
ITIGIETTLN LNWPKPLSAV LPVALAVSIV RFSGTLALSF IPSSSPPSTS TTTPNPEHHR
SNSTTSSSTS PPHRPTTLAF TFLDDYRLDL SVRSLVGSRS RLQDVPKIAQ LIESRVHAWF
DERAVEPRFQ QIVLPSLWPR KHNTRGGATE DVEASEADLD EEVILEEEEE EEEDGGYTLP
VPPQLRHPSA ASTSLEAEGA KLREAEIRAG VRKQERPGMS RAQTSREEGV RYRPKPVSRT
SEGWSGQKGM PGALAPGTFR
