MMM1_ZYGRC
ID MMM1_ZYGRC Reviewed; 454 AA.
AC C5DRQ1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Maintenance of mitochondrial morphology protein 1 {ECO:0000255|HAMAP-Rule:MF_03103};
GN Name=MMM1 {ECO:0000255|HAMAP-Rule:MF_03103};
GN OrderedLocusNames=ZYRO0B10274g;
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 190-444 IN COMPLEX WITH
RP PHOSPHATIDIC ACID, SUBUNIT, AND MUTAGENESIS OF LEU-315; ARG-379; TRP-411;
RP ARG-415 AND TRP-430.
RX PubMed=29078410; DOI=10.1073/pnas.1715592114;
RA Jeong H., Park J., Jun Y., Lee C.;
RT "Crystal structures of Mmm1 and Mdm12-Mmm1 reveal mechanistic insight into
RT phospholipid trafficking at ER-mitochondria contact sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E9502-E9511(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 (By
CC similarity). Preferentially binds to glycerophospholipids such as
CC phosphatidylcholoine (PC), phosphatidic acid (PA), phosphatidylglycerol
CC (PG), and phosphatidylserine (PS), but not to phosphatidylethanolamine
CC (PE) (PubMed:29078410). The MDM12-MMM1 subcomplex functions in the
CC major beta-barrel assembly pathway that is responsible for biogenesis
CC of all outer membrane beta-barrel proteins, and acts in a late step
CC after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in
CC the TOM40-specific pathway after the action of the MDM12-MMM1 complex.
CC Essential for establishing and maintaining the structure of
CC mitochondria and maintenance of mtDNA nucleoids (By similarity).
CC {ECO:0000255|HAMAP-Rule:MF_03103, ECO:0000269|PubMed:29078410}.
CC -!- SUBUNIT: Homodimer (PubMed:29078410). Component of the ER-mitochondria
CC encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10,
CC MDM12 and MDM34 (By similarity). A MMM1 homodimer associates with one
CC molecule of MDM12 on each side in a pairwise head-to-tail manner, and
CC the SMP-LTD domains of MMM1 and MDM12 generate a continuous hydrophobic
CC tunnel for phospholipid trafficking (PubMed:29078410).
CC {ECO:0000255|HAMAP-Rule:MF_03103, ECO:0000269|PubMed:29078410}.
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; CU928174; CAR26462.1; -; Genomic_DNA.
DR RefSeq; XP_002495395.1; XM_002495350.1.
DR PDB; 5YK6; X-ray; 2.80 A; A=190-444.
DR PDB; 5YK7; X-ray; 3.80 A; A/C=190-444.
DR PDBsum; 5YK6; -.
DR PDBsum; 5YK7; -.
DR AlphaFoldDB; C5DRQ1; -.
DR SMR; C5DRQ1; -.
DR STRING; 559307.C5DRQ1; -.
DR EnsemblFungi; CAR26462; CAR26462; ZYRO0B10274g.
DR GeneID; 8202550; -.
DR KEGG; zro:ZYRO0B10274g; -.
DR HOGENOM; CLU_032730_2_0_1; -.
DR InParanoid; C5DRQ1; -.
DR Proteomes; UP000008536; Chromosome B.
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 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Lipid transport; Lipid-binding;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..454
FT /note="Maintenance of mitochondrial morphology protein 1"
FT /id="PRO_0000384262"
FT TOPO_DOM 1..117
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TOPO_DOM 139..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT DOMAIN 215..427
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT REGION 144..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 253
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:29078410"
FT BINDING 411
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:29078410"
FT BINDING 415
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:29078410"
FT BINDING 430
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:29078410"
FT BINDING 432
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:29078410"
FT BINDING 433
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:29078410"
FT MUTAGEN 315
FT /note="L->S: Impairs the interaction with MDM12."
FT /evidence="ECO:0000269|PubMed:29078410"
FT MUTAGEN 379
FT /note="R->E: No effect."
FT /evidence="ECO:0000269|PubMed:29078410"
FT MUTAGEN 411
FT /note="W->A: Completely loses the ability to bind
FT phospholipids."
FT /evidence="ECO:0000269|PubMed:29078410"
FT MUTAGEN 415
FT /note="R->E: Completely loses the ability to bind
FT phospholipids and partially impairs dimer formation."
FT /evidence="ECO:0000269|PubMed:29078410"
FT MUTAGEN 430
FT /note="W->A: Completely loses the ability to bind
FT phospholipids and partially impairs dimer formation."
FT /evidence="ECO:0000269|PubMed:29078410"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:5YK6"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:5YK6"
FT HELIX 220..235
FT /evidence="ECO:0007829|PDB:5YK6"
FT HELIX 239..253
FT /evidence="ECO:0007829|PDB:5YK6"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5YK6"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:5YK6"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:5YK6"
FT STRAND 295..303
FT /evidence="ECO:0007829|PDB:5YK6"
FT STRAND 307..317
FT /evidence="ECO:0007829|PDB:5YK6"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:5YK6"
FT STRAND 329..347
FT /evidence="ECO:0007829|PDB:5YK6"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:5YK6"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:5YK6"
FT STRAND 379..391
FT /evidence="ECO:0007829|PDB:5YK6"
FT HELIX 397..416
FT /evidence="ECO:0007829|PDB:5YK6"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:5YK6"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:5YK6"
SQ SEQUENCE 454 AA; 51378 MW; 4535ADF7D8E12C2C CRC64;
MESNYTGMDG NWALNGTVSV GNGTLISVDE FLHNALPMHL QALFQDGNSQ GPLLTMEDLE
KAIEFKRASQ ELVNDNVLAP DGLFVELLRQ QEKTLPRLIS ATSNTQGSFS SWSFAQGLIV
GQVSVVLVLI FFIKFFIFSD SSTKTNPNPA KNSSSTNSLS GLSSESRSFI SPHFFTSIMN
RKGNEQAESN DDENERSRQI DDILEKTYYN VDTHPAESLD WFNVLIGQTI QQLREEAWKK
DNIVYSLNAF IERKAQELPS YLDSIKITEL DIGHDFPIFS NCRIQYSPNS NGRKLEAKID
IDLNDRLAVG IETRLLLNYP KPLTASLPIN VTVSIIRFQA CLTVSLTKAE EFVPTSPESV
DEDDNDGYFL MFSFAPEYRM EFETQSLIGA RSKLENIPKI GSLVEYQIKK WFVERCVEPR
FQFIKLPSVW PRSKNTREGK ADVDESEPGR ETHY
