ID A0A2N5RZY6_9BASI Unreviewed; 588 AA.
AC A0A2N5RZY6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=PCANC_25251 {ECO:0000313|EMBL:PLW06502.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW06502.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|EMBL:PLW06502.1, ECO:0000313|Proteomes:UP000235388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW06502.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) 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: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:PLW06502.1}.
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DR EMBL; PGCJ01001311; PLW06502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5RZY6; -.
DR STRING; 200324.A0A2N5RZY6; -.
DR Proteomes; UP000235388; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000235388};
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..40
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT TOPO_DOM 62..588
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT DOMAIN 122..339
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT REGION 65..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 64400 MW; 35332DF33501D703 CRC64;
MFPVIALTHS ITTTTTSQQQ PGSSSHNSQL RPFQLTFTQG FIVGQLSILL LVVCFVRYVV
FEDPKSPQNK NPVRPQRKTY HNTTTQRRSR TNSRRLSFHD KSHGTTQSDL LSKLPYDISS
HPPETTDWLN VLLAQAIIAY RSLVHGLDDD PTDPKGNKAK EMVEEAMNFA RGEVPGIISL
DYITVTEVEF GKEYPACTNA RVRPADETGR MRIEVDIDYS DRVTLAIETK VVVNFPTARF
AVLPISLGLT LNQLSATIMA EIPPIAIPLP MNDDPSAPSP AILMSLDPDF TLSMTTTSLL
GSRAKLQDIP KIEQLILGRL RGWIVDNLVW PKVRVLKLPG LGDKGSVEDA ADGEGEYVWV
EGTMKETTST PNLKDSKPKS IVRDADEDEG PTLSPVTHDP PSGLNHSTLS PSLGIPLHPQ
YHLRSPSGSS RVAHVPLISP SDLGESASRQ RYASTRMDLR QGPPESNGYS NHPKPPGALP
GSTRSNKSFG GSPLPTASSR PEHLKGPAQQ EWFKYQRSLD TPSADSNRSA EDRGRWARAG
GMSGVPLGLG SSPQSASLGY GIRERIRDAE RLKDLRASHL DDSLAPQR
//
