MMM1_YEAST
ID MMM1_YEAST Reviewed; 426 AA.
AC P41800; D6VXZ7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Maintenance of mitochondrial morphology protein 1 {ECO:0000255|HAMAP-Rule:MF_03103};
DE AltName: Full=Mitochondrial outer membrane protein MMM1 {ECO:0000255|HAMAP-Rule:MF_03103};
DE AltName: Full=Yeast mitochondrial escape protein 6 {ECO:0000255|HAMAP-Rule:MF_03103};
GN Name=MMM1 {ECO:0000255|HAMAP-Rule:MF_03103}; Synonyms=YME6;
GN OrderedLocusNames=YLL006W; ORFNames=L1357;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 90850 / YH8;
RX PubMed=8089172; DOI=10.1083/jcb.126.6.1375;
RA Burgess S.M., Delannoy M., Jensen R.E.;
RT "MMM1 encodes a mitochondrial outer membrane protein essential for
RT establishing and maintaining the structure of yeast mitochondria.";
RL J. Cell Biol. 126:1375-1391(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=8810043;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA Miosga T., Zimmermann F.K.;
RT "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT 43.7 kb fragment of chromosome XII including an open reading frame
RT homologous to the human cystic fibrosis transmembrane conductance regulator
RT protein CFTR.";
RL Yeast 12:693-708(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION.
RX PubMed=9628893; DOI=10.1083/jcb.141.6.1371;
RA Boldogh I.R., Vojtov N., Karmon S., Pon L.A.;
RT "Interaction between mitochondria and the actin cytoskeleton in budding
RT yeast requires two integral mitochondrial outer membrane proteins, Mmm1p
RT and Mdm10p.";
RL J. Cell Biol. 141:1371-1381(1998).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11266455; DOI=10.1083/jcb.152.2.401;
RA Hobbs A.E.A., Srinivasan M., McCaffery J.M., Jensen R.E.;
RT "Mmm1p, a mitochondrial outer membrane protein, is connected to
RT mitochondrial DNA (mtDNA) nucleoids and required for mtDNA stability.";
RL J. Cell Biol. 152:401-410(2001).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLU-215.
RX PubMed=12454062; DOI=10.1093/genetics/162.3.1147;
RA Hanekamp T., Thorsness M.K., Rebbapragada I., Fisher E.M., Seebart C.,
RA Darland M.R., Coxbill J.A., Updike D.L., Thorsness P.E.;
RT "Maintenance of mitochondrial morphology is linked to maintenance of the
RT mitochondrial genome in Saccharomyces cerevisiae.";
RL Genetics 162:1147-1156(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=12972421; DOI=10.1074/jbc.m308436200;
RA Kondo-Okamoto N., Shaw J.M., Okamoto K.;
RT "Mmm1p spans both the outer and inner mitochondrial membranes and contains
RT distinct domains for targeting and foci formation.";
RL J. Biol. Chem. 278:48997-49005(2003).
RN [9]
RP IDENTIFICATION IN THE MDM10/MDM12/MMM1 COMPLEX.
RX PubMed=13679517; DOI=10.1091/mbc.e03-04-0225;
RA Boldogh I.R., Nowakowski D.W., Yang H.-C., Chung H., Karmon S., Royes P.,
RA Pon L.A.;
RT "A protein complex containing Mdm10p, Mdm12p, and Mmm1p links mitochondrial
RT membranes and DNA to the cytoskeleton-based segregation machinery.";
RL Mol. Biol. Cell 14:4618-4627(2003).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14981098; DOI=10.1083/jcb.200308012;
RA Youngman M.J., Hobbs A.E.A., Burgess S.M., Srinivasan M., Jensen R.E.;
RT "Mmm2p, a mitochondrial outer membrane protein required for yeast
RT mitochondrial shape and maintenance of mtDNA nucleoids.";
RL J. Cell Biol. 164:677-688(2004).
RN [14]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [15]
RP FUNCTION, AND IDENTIFICATION IN MDM12/MMM1 AND MDM10/MDM12/MMM1 COMPLEXES.
RX PubMed=17410204; DOI=10.1038/sj.emboj.7601673;
RA Meisinger C., Pfannschmidt S., Rissler M., Milenkovic D., Becker T.,
RA Stojanovski D., Youngman M.J., Jensen R.E., Chacinska A., Guiard B.,
RA Pfanner N., Wiedemann N.;
RT "The morphology proteins Mdm12/Mmm1 function in the major beta-barrel
RT assembly pathway of mitochondria.";
RL EMBO J. 26:2229-2239(2007).
RN [16]
RP FUNCTION, IDENTIFICATION IN ERMES/MDM COMPLEX, SUBCELLULAR LOCATION,
RP TOPOLOGY, AND GLYCOSYLATION.
RX PubMed=19556461; DOI=10.1126/science.1175088;
RA Kornmann B., Currie E., Collins S.R., Schuldiner M., Nunnari J.,
RA Weissman J.S., Walter P.;
RT "An ER-mitochondria tethering complex revealed by a synthetic biology
RT screen.";
RL Science 325:477-481(2009).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=22250200; DOI=10.1242/jcs.085118;
RA Toulmay A., Prinz W.A.;
RT "A conserved membrane-binding domain targets proteins to organelle contact
RT sites.";
RL J. Cell Sci. 125:49-58(2012).
RN [18]
RP DISRUPTION PHENOTYPE.
RX PubMed=26370498; DOI=10.1083/jcb.201502105;
RA Lang A.B., John Peter A.T., Walter P., Kornmann B.;
RT "ER-mitochondrial junctions can be bypassed by dominant mutations in the
RT endosomal protein Vps13.";
RL J. Cell Biol. 210:883-890(2015).
RN [19]
RP DISRUPTION PHENOTYPE.
RX PubMed=27280386; DOI=10.1091/mbc.e16-02-0112;
RA Park J.S., Thorsness M.K., Policastro R., McGoldrick L.L.,
RA Hollingsworth N.M., Thorsness P.E., Neiman A.M.;
RT "Yeast Vps13 promotes mitochondrial function and is localized at membrane
RT contact sites.";
RL Mol. Biol. Cell 27:2435-2449(2016).
RN [20]
RP FUNCTION.
RX PubMed=27469264; DOI=10.1038/srep30777;
RA Kojima R., Endo T., Tamura Y.;
RT "A phospholipid transfer function of ER-mitochondria encounter structure
RT revealed in vitro.";
RL Sci. Rep. 6:30777-30777(2016).
CC -!- FUNCTION: Component of the ERMES/MDM complex, which serves as a
CC molecular tether to connect the endoplasmic reticulum and mitochondria
CC (PubMed:19556461). Components of this complex are involved in the
CC control of mitochondrial shape and protein biogenesis, and function in
CC nonvesicular lipid trafficking between the ER and mitochondria
CC (PubMed:8089172, PubMed:9628893, PubMed:27469264). The MDM12-MMM1
CC subcomplex functions in the major beta-barrel assembly pathway that is
CC responsible for biogenesis of all outer membrane beta-barrel proteins,
CC and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1
CC subcomplex further acts in the TOM40-specific pathway after the action
CC of the MDM12-MMM1 complex (PubMed:17410204). Essential for establishing
CC and maintaining the structure of mitochondria and maintenance of mtDNA
CC nucleoids (PubMed:11266455, PubMed:12454062, PubMed:14981098).
CC {ECO:0000255|HAMAP-Rule:MF_03103, ECO:0000269|PubMed:11266455,
CC ECO:0000269|PubMed:12454062, ECO:0000269|PubMed:14981098,
CC ECO:0000269|PubMed:17410204, ECO:0000269|PubMed:19556461,
CC ECO:0000269|PubMed:27469264, ECO:0000269|PubMed:8089172,
CC ECO:0000269|PubMed:9628893}.
CC -!- SUBUNIT: Homodimer (By similarity). Component of the ER-mitochondria
CC encounter structure (ERMES) or MDM complex, composed of MMM1, MDM10,
CC MDM12 and MDM34 (PubMed:13679517, PubMed:17410204, PubMed:19556461). A
CC MMM1 homodimer associates with one molecule of MDM12 on each side in a
CC pairwise head-to-tail manner, and the SMP-LTD domains of MMM1 and MDM12
CC generate a continuous hydrophobic tunnel for phospholipid trafficking
CC (By similarity). {ECO:0000250|UniProtKB:C5DRQ1, ECO:0000255|HAMAP-
CC Rule:MF_03103, ECO:0000269|PubMed:13679517,
CC ECO:0000269|PubMed:17410204, ECO:0000269|PubMed:19556461}.
CC -!- INTERACTION:
CC P41800; Q92328: MDM12; NbExp=5; IntAct=EBI-11029, EBI-10584;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03103, ECO:0000269|PubMed:11266455,
CC ECO:0000269|PubMed:12972421, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:14981098,
CC ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:19556461,
CC ECO:0000269|PubMed:22250200, ECO:0000269|PubMed:8089172}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_03103,
CC ECO:0000269|PubMed:11266455, ECO:0000269|PubMed:12972421,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:14981098, ECO:0000269|PubMed:16407407,
CC ECO:0000269|PubMed:19556461, ECO:0000269|PubMed:8089172}. Note=The
CC ERMES/MDM complex localizes to a few discrete foci (around 10 per
CC single cell), that represent mitochondria-endoplasmic reticulum
CC junctions. These foci are often found next to mtDNA nucleoids.
CC {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 -!- PTM: Glycosylated. {ECO:0000269|PubMed:19556461}.
CC -!- DISRUPTION PHENOTYPE: Loss of mitochondrial integrity
CC (PubMed:26370498). Abolishes growth on non-fermentable carbon source
CC (glycerol with ethanol) (PubMed:26370498, PubMed:27280386). Slow growth
CC on fermentable carbon source (glucose) (PubMed:26370498,
CC PubMed:27280386). Synthetic lethal with VPS13 (PubMed:26370498,
CC PubMed:27280386). {ECO:0000269|PubMed:26370498,
CC ECO:0000269|PubMed:27280386}.
CC -!- MISCELLANEOUS: Normal levels of MMM1 require MDM34.
CC -!- MISCELLANEOUS: Present with 2490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MMM1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03103}.
CC -!- CAUTION: Was originally (PubMed:12972421 and PubMed:8089172) proposed
CC to be inserted into either the outer or inner mitochondrial membrane,
CC yet more recent data indicates that it is instead inserted into the ER.
CC {ECO:0000305|PubMed:19556461}.
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DR EMBL; L32793; AAA53581.1; -; Genomic_DNA.
DR EMBL; X91488; CAA62763.1; -; Genomic_DNA.
DR EMBL; Z73111; CAA97449.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09313.1; -; Genomic_DNA.
DR PIR; S64748; S64748.
DR RefSeq; NP_013095.1; NM_001181826.1.
DR AlphaFoldDB; P41800; -.
DR SMR; P41800; -.
DR BioGRID; 31245; 645.
DR ComplexPortal; CPX-3196; ERMES complex.
DR DIP; DIP-4150N; -.
DR IntAct; P41800; 24.
DR MINT; P41800; -.
DR STRING; 4932.YLL006W; -.
DR TCDB; 9.A.58.1.1; the maintenance of mitochondrial morphology (mmm) family.
DR CarbonylDB; P41800; -.
DR iPTMnet; P41800; -.
DR MaxQB; P41800; -.
DR PaxDb; P41800; -.
DR PRIDE; P41800; -.
DR EnsemblFungi; YLL006W_mRNA; YLL006W; YLL006W.
DR GeneID; 850654; -.
DR KEGG; sce:YLL006W; -.
DR SGD; S000003929; MMM1.
DR VEuPathDB; FungiDB:YLL006W; -.
DR eggNOG; ENOG502QUUW; Eukaryota.
DR HOGENOM; CLU_032730_2_0_1; -.
DR InParanoid; P41800; -.
DR OMA; KWFVERC; -.
DR BioCyc; YEAST:G3O-32111-MON; -.
DR PRO; PR:P41800; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P41800; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0032865; C:ERMES complex; IDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0098799; C:outer mitochondrial membrane protein complex; IC:ComplexPortal.
DR GO; GO:0008289; F:lipid binding; IBA:GO_Central.
DR GO; GO:0015917; P:aminophospholipid transport; IMP:SGD.
DR GO; GO:0120009; P:intermembrane lipid transfer; IEA:GOC.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IMP:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IMP:SGD.
DR GO; GO:0055091; P:phospholipid homeostasis; IC:ComplexPortal.
DR GO; GO:0015914; P:phospholipid transport; IMP:SGD.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IMP:SGD.
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 Endoplasmic reticulum; Glycoprotein; Lipid transport; Lipid-binding;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..426
FT /note="Maintenance of mitochondrial morphology protein 1"
FT /id="PRO_0000096506"
FT TOPO_DOM 1..100
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT TOPO_DOM 122..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT DOMAIN 194..409
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03103"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 215
FT /note="E->K: In MMM1-6; impairs both mtDNA maintenance and
FT mitochondrial morpholgy."
FT /evidence="ECO:0000269|PubMed:12454062"
FT CONFLICT 200
FT /note="W -> S (in Ref. 1; AAA53581)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="S -> W (in Ref. 1; AAA53581)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="S -> A (in Ref. 1; AAA53581)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="E -> Q (in Ref. 1; AAA53581)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="S -> P (in Ref. 1; AAA53581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 48660 MW; 3610AEC2109355AF CRC64;
MTDSENESTE TDSLMTFDDY ISKELPEHLQ RLIMENLKGS TTNDLKQTSN NSEFNVSKNG
SFKGLDDAIQ ALQMQSVLHP SSLGSLATSS KFSGWSFAQG FFVGQLSIVL LFIFFLKFFI
FSDEPSKSKN PKPAASRHRS KFKEYPFISR EFLTSLVRKG AKQHYELNEE AENEHLQELA
LILEKTYYNV DVHPAESLDW FNVLVAQIIQ QFRSEAWHRD NILHSLNDFI GRKSPDLPEY
LDTIKITELD TGDDFPIFSN CRIQYSPNSG NKKLEAKIDI DLNDHLTLGV ETKLLLNYPK
PGIAALPINL VVSIVRFQAC LTVSLTNAEE FASTSNGSSS ENGMEGNSGY FLMFSFSPEY
RMEFEIKSLI GSRSKLENIP KIGSVIEYQI KKWFVERCVE PRFQFVRLPS MWPRSKNTRE
EKPTEL
