MDM34_YEAST
ID MDM34_YEAST Reviewed; 459 AA.
AC P53083; D6VTT9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Mitochondrial distribution and morphology protein 34 {ECO:0000255|HAMAP-Rule:MF_03105};
DE AltName: Full=Mitochondrial outer membrane protein MMM2 {ECO:0000255|HAMAP-Rule:MF_03105};
GN Name=MDM34 {ECO:0000255|HAMAP-Rule:MF_03105};
GN Synonyms=MMM2 {ECO:0000255|HAMAP-Rule:MF_03105}; OrderedLocusNames=YGL219C;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=11907266; DOI=10.1091/mbc.01-12-0588;
RA Dimmer K.S., Fritz S., Fuchs F., Messerschmitt M., Weinbach N., Neupert W.,
RA Westermann B.;
RT "Genetic basis of mitochondrial function and morphology in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 13:847-853(2002).
RN [5]
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 [6]
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 [7]
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 [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [9]
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 [10]
RP UBIQUITINATION.
RX PubMed=18775025; DOI=10.1111/j.1365-2443.2008.01228.x;
RA Ota K., Kito K., Okada S., Ito T.;
RT "A proteomic screen reveals the mitochondrial outer membrane protein Mdm34p
RT as an essential target of the F-box protein Mdm30p.";
RL Genes Cells 13:1075-1085(2008).
RN [11]
RP FUNCTION, IDENTIFICATION IN ERMES/MDM COMPLEX, AND SUBCELLULAR LOCATION.
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [13]
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 (ER) and
CC mitochondria (PubMed:11907266, PubMed:14981098). Components of this
CC complex are involved in the control of mitochondrial shape and protein
CC biogenesis, and function in nonvesicular lipid trafficking between the
CC ER and mitochondria (PubMed:27469264). MDM34 is required for the
CC interaction of the ER-resident membrane protein MMM1 and the outer
CC mitochondrial membrane-resident beta-barrel protein MDM10 (By
CC similarity) (PubMed:19556461). {ECO:0000255|HAMAP-Rule:MF_03105,
CC ECO:0000269|PubMed:11907266, ECO:0000269|PubMed:14981098,
CC ECO:0000269|PubMed:19556461, ECO:0000269|PubMed:27469264}.
CC -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES)
CC or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34.
CC {ECO:0000255|HAMAP-Rule:MF_03105, ECO:0000269|PubMed:19556461}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_03105, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14981098, ECO:0000269|PubMed:16407407,
CC ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:19556461}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03105,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14981098,
CC ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:16823961,
CC ECO:0000269|PubMed:19556461}. Note=The ERMES/MDM complex localizes to a
CC 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_03105}.
CC -!- DOMAIN: Lacks alpha-helical transmembrane segments, suggesting that it
CC resides in the membrane via beta-sheet conformations similar to those
CC predicted for other outer membrane proteins and porin.
CC {ECO:0000255|HAMAP-Rule:MF_03105}.
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_03105}.
CC -!- PTM: Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-
CC protein ligase complex containing the F-box protein MDM30.
CC Ubiquitination is important for mitochondrial integrity.
CC {ECO:0000255|HAMAP-Rule:MF_03105, ECO:0000269|PubMed:18775025}.
CC -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MDM34 family. {ECO:0000255|HAMAP-
CC Rule:MF_03105}.
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DR EMBL; Z72741; CAA96934.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07900.1; -; Genomic_DNA.
DR PIR; S64241; S64241.
DR RefSeq; NP_011296.1; NM_001181084.1.
DR AlphaFoldDB; P53083; -.
DR BioGRID; 33040; 506.
DR ComplexPortal; CPX-3196; ERMES complex.
DR DIP; DIP-7932N; -.
DR IntAct; P53083; 14.
DR STRING; 4932.YGL219C; -.
DR TCDB; 9.A.58.1.1; the maintenance of mitochondrial morphology (mmm) family.
DR iPTMnet; P53083; -.
DR MaxQB; P53083; -.
DR PaxDb; P53083; -.
DR PRIDE; P53083; -.
DR EnsemblFungi; YGL219C_mRNA; YGL219C; YGL219C.
DR GeneID; 852654; -.
DR KEGG; sce:YGL219C; -.
DR SGD; S000003187; MDM34.
DR VEuPathDB; FungiDB:YGL219C; -.
DR eggNOG; ENOG502QT3W; Eukaryota.
DR HOGENOM; CLU_036329_0_0_1; -.
DR InParanoid; P53083; -.
DR OMA; PGCLERQ; -.
DR BioCyc; YEAST:G3O-30693-MON; -.
DR PRO; PR:P53083; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53083; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0032865; C:ERMES complex; IPI:SGD.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0098799; C:outer mitochondrial membrane protein complex; IC:ComplexPortal.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
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; IGI:SGD.
DR HAMAP; MF_03105; Mdm34; 1.
DR InterPro; IPR027536; Mdm34.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR28185; PTHR28185; 1.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW Lipid transport; Lipid-binding; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane beta strand; Transport; Ubl conjugation.
FT CHAIN 1..459
FT /note="Mitochondrial distribution and morphology protein
FT 34"
FT /id="PRO_0000096331"
FT DOMAIN 1..190
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03105"
FT REGION 338..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 51990 MW; 222F0D0D031FC578 CRC64;
MSFRFNEAVF GDNSFNERIR EKLSTALNSP SKKKLDILKS GIKVQKVDFP TIPQLEILDL
DIITQPKSLA KGICKISCKD AMLRIQTVIE SNLLLINEQD TPSFTMPQLI NNGSFTIPIT
MTFSSIELEA ITNIFVKNPG IGISFNDVDL DFKFDCSVKI LQSTIERRLK ESMHVVFKDV
LPSLIFNTSQ NWFTNRGEST STIPGKREHH HQQTTMSRNV ILDGSDFQEL SPINMLRLSS
IVSSRSTLSL HSTVMNSLSA IPGCLERQNL YRFISRMPSL NNYYSSQSFP QPKSSTVSSK
QLVKPFYCSH NLLPKTVLDS SQYDLATITK IQSRLFDRSN SNDDNAKPRR RKIKCKKTRT
PSNLQSQGEQ AVDDSTAIET VTSTPVQTPI PELEEQSPPY LKTTVSIRDK YVIPEKISLN
LDSKKDTSKK KPFYFIGLNS QEPSNNWKWG MEDSPPPYH
