MDM10_YEAST
ID MDM10_YEAST Reviewed; 493 AA.
AC P18409; D6VPK8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 5.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Mitochondrial distribution and morphology protein 10 {ECO:0000255|HAMAP-Rule:MF_03102};
DE AltName: Full=Mitochondrial inheritance component MDM10 {ECO:0000255|HAMAP-Rule:MF_03102};
GN Name=MDM10 {ECO:0000255|HAMAP-Rule:MF_03102}; OrderedLocusNames=YAL010C;
GN ORFNames=FUN37;
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=MYY290;
RX PubMed=8089171; DOI=10.1083/jcb.126.6.1361;
RA Sogo L.F., Yaffe M.P.;
RT "Regulation of mitochondrial morphology and inheritance by Mdm10p, a
RT protein of the mitochondrial outer membrane.";
RL J. Cell Biol. 126:1361-1373(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=7941740; DOI=10.1002/yea.320100413;
RA Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
RA Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42
RT kbp SPO7-CENI-CDC15 region.";
RL Yeast 10:535-541(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 272.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
RX PubMed=2253888; DOI=10.1016/0378-1119(90)90414-m;
RA Whyte W., Koepp L.H., Lamb J., Crowley J.C., Kaback D.B.;
RT "Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae:
RT isolation, characterization and regulation of the SPO7 sporulation gene.";
RL Gene 95:65-72(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-493.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8458570; DOI=10.1139/g93-005;
RA Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B.,
RA Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32
RT kb region between the LTE1 and SPO7 genes.";
RL Genome 36:32-42(1993).
RN [7]
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 [8]
RP FUNCTION.
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 [9]
RP IDENTIFICATION IN THE MDM10/MDM12/MMM1 COMPLEX, AND SUBCELLULAR LOCATION.
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 PROBABLE BETA-BARREL TOPOLOGY.
RX PubMed=12891361; DOI=10.1038/nature01753;
RA Wiedemann N., Kozjak V., Chacinska A., Schoenfisch B., Rospert S.,
RA Ryan M.T., Pfanner N., Meisinger C.;
RT "Machinery for protein sorting and assembly in the mitochondrial outer
RT membrane.";
RL Nature 424:565-571(2003).
RN [11]
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 [12]
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 [13]
RP PROBABLE TOPOLOGY BETA-BARREL.
RX PubMed=14685243; DOI=10.1038/nature02208;
RA Paschen S.A., Waizenegger T., Stan T., Preuss M., Cyrklaff M., Hell K.,
RA Rapaport D., Neupert W.;
RT "Evolutionary conservation of biogenesis of beta-barrel membrane
RT proteins.";
RL Nature 426:862-866(2003).
RN [14]
RP FUNCTION, AND IDENTIFICATION IN SAM COMPLEX.
RX PubMed=15239954; DOI=10.1016/j.devcel.2004.06.003;
RA Meisinger C., Rissler M., Chacinska A., Szklarz L.K., Milenkovic D.,
RA Kozjak V., Schonfisch B., Lohaus C., Meyer H.E., Yaffe M.P., Guiard B.,
RA Wiedemann N., Pfanner N.;
RT "The mitochondrial morphology protein Mdm10 functions in assembly of the
RT preprotein translocase of the outer membrane.";
RL Dev. Cell 7:61-71(2004).
RN [15]
RP FUNCTION.
RX PubMed=16760475; DOI=10.1074/jbc.m602679200;
RA Meisinger C., Wiedemann N., Rissler M., Strub A., Milenkovic D.,
RA Schoenfisch B., Mueller H., Kozjak V., Pfanner N.;
RT "Mitochondrial protein sorting: differentiation of beta-barrel assembly by
RT Tom7-mediated segregation of Mdm10.";
RL J. Biol. Chem. 281:22819-22826(2006).
RN [16]
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 [17]
RP FUNCTION, AND IDENTIFICATION IN MDM10/MDM12/MMM1 AND SAM 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 [18]
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).
CC -!- FUNCTION: Component of the ERMES/MDM complex, which serves as a
CC molecular tether to connect the endoplasmic reticulum and mitochondria.
CC Components of this complex are involved in the control of mitochondrial
CC shape and protein biogenesis and may function in phospholipid exchange.
CC MDM10 is involved in the late assembly steps of the general translocase
CC of the mitochondrial outer membrane (TOM complex). Functions in the
CC TOM40-specific route of the assembly of outer membrane beta-barrel
CC proteins, including the association of TOM40 with the receptor TOM22
CC and small TOM proteins. Can associate with the SAM(core) complex as
CC well as the MDM12-MMM1 complex, both involved in late steps of the
CC major beta-barrel assembly pathway, that is responsible for biogenesis
CC of all outer membrane beta-barrel proteins. May act as a switch that
CC shuttles between both complexes and channels precursor proteins into
CC the TOM40-specific pathway. Plays a role in mitochondrial morphology
CC and in the inheritance of mitochondria. {ECO:0000255|HAMAP-
CC Rule:MF_03102, ECO:0000269|PubMed:12454062,
CC ECO:0000269|PubMed:15239954, ECO:0000269|PubMed:16760475,
CC ECO:0000269|PubMed:17410204, ECO:0000269|PubMed:19556461,
CC ECO:0000269|PubMed:8089171, ECO:0000269|PubMed:9628893}.
CC -!- SUBUNIT: Component of the ER-mitochondria encounter structure (ERMES)
CC or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34. Associates
CC with the mitochondrial outer membrane sorting assembly machinery
CC SAM(core) complex, which consists of SAM35, SAM37 and SAM50, to form a
CC SAM(holo) complex. {ECO:0000255|HAMAP-Rule:MF_03102,
CC ECO:0000269|PubMed:13679517, ECO:0000269|PubMed:15239954,
CC ECO:0000269|PubMed:17410204, ECO:0000269|PubMed:19556461}.
CC -!- INTERACTION:
CC P18409; Q92328: MDM12; NbExp=4; IntAct=EBI-10580, EBI-10584;
CC P18409; P14693: SAM35; NbExp=5; IntAct=EBI-10580, EBI-24602;
CC P18409; P53969: SAM50; NbExp=4; IntAct=EBI-10580, EBI-28646;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_03102, ECO:0000269|PubMed:13679517,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16407407,
CC ECO:0000269|PubMed:19556461, ECO:0000269|PubMed:8089171}; Multi-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03102,
CC ECO:0000269|PubMed:13679517, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:19556461,
CC ECO:0000269|PubMed:8089171}. 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.
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 -!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MDM10 family. {ECO:0000255|HAMAP-
CC Rule:MF_03102}.
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DR EMBL; X80874; CAA56842.1; -; Genomic_DNA.
DR EMBL; L22015; AAC04948.1; -; Genomic_DNA.
DR EMBL; M36073; AAA35072.2; -; Genomic_DNA.
DR EMBL; L05146; AAC04947.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06978.2; -; Genomic_DNA.
DR PIR; PS0157; PS0157.
DR RefSeq; NP_009392.2; NM_001178155.2.
DR AlphaFoldDB; P18409; -.
DR SMR; P18409; -.
DR BioGRID; 31756; 362.
DR ComplexPortal; CPX-3196; ERMES complex.
DR DIP; DIP-6697N; -.
DR IntAct; P18409; 15.
DR MINT; P18409; -.
DR STRING; 4932.YAL010C; -.
DR TCDB; 1.B.33.3.1; the outer membrane protein insertion porin (bam complex) (ompip) family.
DR TCDB; 1.B.8.6.1; the mitochondrial and plastid porin (mpp) family.
DR TCDB; 9.A.58.1.1; the maintenance of mitochondrial morphology (mmm) family.
DR MaxQB; P18409; -.
DR PaxDb; P18409; -.
DR PRIDE; P18409; -.
DR EnsemblFungi; YAL010C_mRNA; YAL010C; YAL010C.
DR GeneID; 851223; -.
DR KEGG; sce:YAL010C; -.
DR SGD; S000000008; MDM10.
DR VEuPathDB; FungiDB:YAL010C; -.
DR eggNOG; ENOG502QUN5; Eukaryota.
DR HOGENOM; CLU_026505_0_0_1; -.
DR InParanoid; P18409; -.
DR OMA; MLDFMDY; -.
DR BioCyc; YEAST:G3O-28823-MON; -.
DR PRO; PR:P18409; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P18409; protein.
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; HDA:SGD.
DR GO; GO:0098799; C:outer mitochondrial membrane protein complex; IC:ComplexPortal.
DR GO; GO:0001401; C:SAM complex; IPI:SGD.
DR GO; GO:0051654; P:establishment of mitochondrion localization; IMP:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
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; IGI:SGD.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IMP:SGD.
DR HAMAP; MF_03102; Mdm10; 1.
DR InterPro; IPR027539; Mdm10.
DR PANTHER; PTHR28035; PTHR28035; 1.
DR Pfam; PF12519; MDM10; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW Transmembrane; Transmembrane beta strand.
FT CHAIN 1..493
FT /note="Mitochondrial distribution and morphology protein
FT 10"
FT /id="PRO_0000096327"
FT CONFLICT 272
FT /note="N -> Q (in Ref. 2; no nucleotide entry, 3; AAC04948
FT and 6; AAC04947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 56237 MW; 5AE98366B5EF25E5 CRC64;
MLPYMDQVLR AFYQSTHWST QNSYEDITAT SRTLLDFRIP SAIHLQISNK STPNTFNSLD
FSTRSRINGS LSYLYSDAQQ LEKFMRNSTD IPLQDATETY RQLQPNLNFS VSSANTLSSD
NTTVDNDKKL LHDSKFVKKS LYYGRMYYPS SDLEAMIIKR LSPQTQFMLK GVSSFKESLN
VLTCYFQRDS HRNLQEWIFS TSDLLCGYRV LHNFLTTPSK FNTSLYNNSS LSLGAEFWLG
LVSLSPGCST TLRYYTHSTN TGRPLTLTLS WNPLFGHISS TYSAKTGTNS TFCAKYDFNL
YSIESNLSFG CEFWQKKHHL LETNKNNNDK LEPISDELVD INPNSRATKL LHENVPDLNS
AVNDIPSTLD IPVHKQKLLN DLTYAFSSSL RKIDEERSTI EKFDNKINSS IFTSVWKLST
SLRDKTLKLL WEGKWRGFLI SAGTELVFTR GFQESLSDDE KNDNAISISA TDTENGNIPV
FPAKFGIQFQ YST
