ID A0A1V6PN62_PENDC Unreviewed; 483 AA.
AC A0A1V6PN62;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Maintenance of mitochondrial morphology protein 1 {ECO:0000256|HAMAP-Rule:MF_03103};
GN Name=MMM1 {ECO:0000256|HAMAP-Rule:MF_03103};
GN ORFNames=PENDEC_c001G06095 {ECO:0000313|EMBL:OQD78394.1};
OS Penicillium decumbens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD78394.1, ECO:0000313|Proteomes:UP000191522};
RN [1] {ECO:0000313|Proteomes:UP000191522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:0000256|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:0000256|HAMAP-Rule:MF_03103}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03103}; Single-pass type I membrane protein
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_03103}.
CC -!- SIMILARITY: Belongs to the MMM1 family. {ECO:0000256|HAMAP-
CC Rule:MF_03103}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD78394.1}.
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DR EMBL; MDYL01000001; OQD78394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6PN62; -.
DR STRING; 69771.A0A1V6PN62; -.
DR OMA; WSFTQGL; -.
DR OrthoDB; 1699636at2759; -.
DR Proteomes; UP000191522; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032865; C:ERMES complex; 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 CDD; cd21671; SMP_Mmm1; 1.
DR HAMAP; MF_03103; Mmm1; 1.
DR InterPro; IPR027537; Mmm1.
DR InterPro; IPR019411; MMM1_dom.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR13466:SF24; MAINTENANCE OF MITOCHONDRIAL MORPHOLOGY PROTEIN 1; 1.
DR PANTHER; PTHR13466; TEX2 PROTEIN-RELATED; 1.
DR Pfam; PF10296; MMM1; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_03103};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03103, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000191522};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03103};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03103}; Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TOPO_DOM 1..22
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT TRANSMEM 23..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 44..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT DOMAIN 128..372
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 49..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 52095 MW; 786E0C2ADC64B64E CRC64;
MALQQHEPAS VAPQSSLSFT QGFLLGQLSV VLLIGAFIKF FIFGEAPPPP SRGLSNRTTH
RRNSSVYSSP QDGQKTLREK PSNSNVLRPV PASATNTRSI LRKTYYSSMP TNPSSKHGRH
RLHHSSHQPE SLDWFNVLIA QTIAQYRQTA YTLKDSPTSS ILSSLTAAMN DPEKKPSFIE
KITVTDISLG EEFPIFSNCR IIAVDDPISD GGRLQALLDV DLSDDNLSIA VETSMVLNYP
KPRSAILPVA LSVSVVRFSG TLCISLIPAQ TDPLHTPATS PAPPVAEAGP NSPGSLGADS
SQDQNPLKGS PKSNVAFSFL PDYRLDLSVR SLIGSRSRLQ DVPKVAQLVE ARVHAWFEER
VVEPRVQVVG LPDLWPRMGR TGVRTGEDSD AGSTAAPRSP GSVDAGGPVR FSDERDREQG
GLRFRGGLDA RLGLGAGSRS SSFNVDMGDL RSPSMTRQDS ASGFSDQLSM PGAMPERTST
PRD
//
