ID A0A1D2VM74_9ASCO Unreviewed; 442 AA.
AC A0A1D2VM74;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=ASCRUDRAFT_137002 {ECO:0000313|EMBL:ODV62655.1};
OS Ascoidea rubescens DSM 1968.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Ascoideaceae; Ascoidea.
OX NCBI_TaxID=1344418 {ECO:0000313|EMBL:ODV62655.1, ECO:0000313|Proteomes:UP000095038};
RN [1] {ECO:0000313|Proteomes:UP000095038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1968 {ECO:0000313|Proteomes:UP000095038};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV454477; ODV62655.1; -; Genomic_DNA.
DR RefSeq; XP_020048962.1; XM_020189118.1.
DR AlphaFoldDB; A0A1D2VM74; -.
DR STRING; 1344418.A0A1D2VM74; -.
DR GeneID; 30962754; -.
DR InParanoid; A0A1D2VM74; -.
DR OrthoDB; 1699636at2759; -.
DR Proteomes; UP000095038; 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:UP000095038};
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..117
FT /note="Lumenal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT TRANSMEM 119..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 139..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03103"
FT DOMAIN 197..417
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
SQ SEQUENCE 442 AA; 49935 MW; AA6BE0C55AE46618 CRC64;
MVPDTPDTQD AQKIQLNKVV LDDNIDSTST IGSVGAQTID NNKDSDHLEE TTGLDNIEIA
ETKTLEQLSL QNNLINKLVE EKLVDLTSNF LNLQNSQFNS QVHLPKTGFN FYSFTQGLLL
GQLSVIIVLL LFIKFFIFSD SIPKKNSSQV NERSSINFLS LTNKRKQQQT NEQNSNTLSL
KIASILEKTY YDVNSHPTES LDWFNVLVAQ IISQFRDEAL LSNNLINSFD EILSDKSSSN
ALPDWLDKIK ITEIDIGDDY PIFSNCRILE KPNKNLEAKI DVDLSDTLTL GIETKLLVNK
PKFMSAVLPI ALSVSIVRFS GCLSVSLIST SDDEFLKLYN QRKSEKDKKD KTEFTGGAAL
MFFFSQDYRL EFQIKSLIGS RSKLENVPKI GYLIEEKLRG WFIERCVEPR FQLIPLPSLW
PSKQNVRVPA NSSTPTNTNN PT
//
