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Mitochondrial distribution and morphology protein 10 (Mitochondrial inheritance component MDM10)

 MDM10_YEAST             Reviewed;         493 AA.
P18409; D6VPK8;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 5.
05-DEC-2018, entry version 145.
RecName: Full=Mitochondrial distribution and morphology protein 10 {ECO:0000255|HAMAP-Rule:MF_03102};
AltName: Full=Mitochondrial inheritance component MDM10 {ECO:0000255|HAMAP-Rule:MF_03102};
Name=MDM10 {ECO:0000255|HAMAP-Rule:MF_03102};
OrderedLocusNames=YAL010C; ORFNames=FUN37;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=MYY290;
PubMed=8089171; DOI=10.1083/jcb.126.6.1361;
Sogo L.F., Yaffe M.P.;
"Regulation of mitochondrial morphology and inheritance by Mdm10p, a
protein of the mitochondrial outer membrane.";
J. Cell Biol. 126:1361-1373(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=7941740; DOI=10.1002/yea.320100413;
Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
"Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of
the 42 kbp SPO7-CENI-CDC15 region.";
Yeast 10:535-541(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
Storms R.K.;
"The nucleotide sequence of chromosome I from Saccharomyces
cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
[4]
GENOME REANNOTATION, AND SEQUENCE REVISION TO 272.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
PubMed=2253888; DOI=10.1016/0378-1119(90)90414-M;
Whyte W., Koepp L.H., Lamb J., Crowley J.C., Kaback D.B.;
"Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae:
isolation, characterization and regulation of the SPO7 sporulation
gene.";
Gene 95:65-72(1990).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-493.
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=8458570;
Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W.,
Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
"Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of
a 32 kb region between the LTE1 and SPO7 genes.";
Genome 36:32-42(1993).
[7]
FUNCTION.
PubMed=9628893; DOI=10.1083/jcb.141.6.1371;
Boldogh I.R., Vojtov N., Karmon S., Pon L.A.;
"Interaction between mitochondria and the actin cytoskeleton in
budding yeast requires two integral mitochondrial outer membrane
proteins, Mmm1p and Mdm10p.";
J. Cell Biol. 141:1371-1381(1998).
[8]
FUNCTION.
PubMed=12454062;
Hanekamp T., Thorsness M.K., Rebbapragada I., Fisher E.M., Seebart C.,
Darland M.R., Coxbill J.A., Updike D.L., Thorsness P.E.;
"Maintenance of mitochondrial morphology is linked to maintenance of
the mitochondrial genome in Saccharomyces cerevisiae.";
Genetics 162:1147-1156(2002).
[9]
IDENTIFICATION IN THE MDM10/MDM12/MMM1 COMPLEX, AND SUBCELLULAR
LOCATION.
PubMed=13679517; DOI=10.1091/mbc.E03-04-0225;
Boldogh I.R., Nowakowski D.W., Yang H.-C., Chung H., Karmon S.,
Royes P., Pon L.A.;
"A protein complex containing Mdm10p, Mdm12p, and Mmm1p links
mitochondrial membranes and DNA to the cytoskeleton-based segregation
machinery.";
Mol. Biol. Cell 14:4618-4627(2003).
[10]
PROBABLE BETA-BARREL TOPOLOGY.
PubMed=12891361; DOI=10.1038/nature01753;
Wiedemann N., Kozjak V., Chacinska A., Schoenfisch B., Rospert S.,
Ryan M.T., Pfanner N., Meisinger C.;
"Machinery for protein sorting and assembly in the mitochondrial outer
membrane.";
Nature 424:565-571(2003).
[11]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[12]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[13]
PROBABLE TOPOLOGY BETA-BARREL.
PubMed=14685243; DOI=10.1038/nature02208;
Paschen S.A., Waizenegger T., Stan T., Preuss M., Cyrklaff M.,
Hell K., Rapaport D., Neupert W.;
"Evolutionary conservation of biogenesis of beta-barrel membrane
proteins.";
Nature 426:862-866(2003).
[14]
FUNCTION, AND IDENTIFICATION IN SAM COMPLEX.
PubMed=15239954; DOI=10.1016/j.devcel.2004.06.003;
Meisinger C., Rissler M., Chacinska A., Szklarz L.K., Milenkovic D.,
Kozjak V., Schonfisch B., Lohaus C., Meyer H.E., Yaffe M.P.,
Guiard B., Wiedemann N., Pfanner N.;
"The mitochondrial morphology protein Mdm10 functions in assembly of
the preprotein translocase of the outer membrane.";
Dev. Cell 7:61-71(2004).
[15]
FUNCTION.
PubMed=16760475; DOI=10.1074/jbc.M602679200;
Meisinger C., Wiedemann N., Rissler M., Strub A., Milenkovic D.,
Schoenfisch B., Mueller H., Kozjak V., Pfanner N.;
"Mitochondrial protein sorting: differentiation of beta-barrel
assembly by Tom7-mediated segregation of Mdm10.";
J. Biol. Chem. 281:22819-22826(2006).
[16]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16407407; DOI=10.1091/mbc.E05-08-0740;
Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
"Proteomic analysis of the yeast mitochondrial outer membrane reveals
accumulation of a subclass of preproteins.";
Mol. Biol. Cell 17:1436-1450(2006).
[17]
FUNCTION, AND IDENTIFICATION IN MDM10/MDM12/MMM1 AND SAM COMPLEXES.
PubMed=17410204; DOI=10.1038/sj.emboj.7601673;
Meisinger C., Pfannschmidt S., Rissler M., Milenkovic D., Becker T.,
Stojanovski D., Youngman M.J., Jensen R.E., Chacinska A., Guiard B.,
Pfanner N., Wiedemann N.;
"The morphology proteins Mdm12/Mmm1 function in the major beta-barrel
assembly pathway of mitochondria.";
EMBO J. 26:2229-2239(2007).
[18]
FUNCTION, IDENTIFICATION IN ERMES/MDM COMPLEX, AND SUBCELLULAR
LOCATION.
PubMed=19556461; DOI=10.1126/science.1175088;
Kornmann B., Currie E., Collins S.R., Schuldiner M., Nunnari J.,
Weissman J.S., Walter P.;
"An ER-mitochondria tethering complex revealed by a synthetic biology
screen.";
Science 325:477-481(2009).
-!- FUNCTION: Component of the ERMES/MDM complex, which serves as a
molecular tether to connect the endoplasmic reticulum and
mitochondria. Components of this complex are involved in the
control of mitochondrial shape and protein biogenesis and may
function in phospholipid exchange. MDM10 is involved in the late
assembly steps of the general translocase of the mitochondrial
outer membrane (TOM complex). Functions in the TOM40-specific
route of the assembly of outer membrane beta-barrel proteins,
including the association of TOM40 with the receptor TOM22 and
small TOM proteins. Can associate with the SAM(core) complex as
well as the MDM12-MMM1 complex, both involved in late steps of the
major beta-barrel assembly pathway, that is responsible for
biogenesis of all outer membrane beta-barrel proteins. May act as
a switch that shuttles between both complexes and channels
precursor proteins into the TOM40-specific pathway. Plays a role
in mitochondrial morphology and in the inheritance of
mitochondria. {ECO:0000255|HAMAP-Rule:MF_03102,
ECO:0000269|PubMed:12454062, ECO:0000269|PubMed:15239954,
ECO:0000269|PubMed:16760475, ECO:0000269|PubMed:17410204,
ECO:0000269|PubMed:19556461, ECO:0000269|PubMed:8089171,
ECO:0000269|PubMed:9628893}.
-!- SUBUNIT: Component of the ER-mitochondria encounter structure
(ERMES) or MDM complex, composed of MMM1, MDM10, MDM12 and MDM34.
Associates with the mitochondrial outer membrane sorting assembly
machinery SAM(core) complex, which consists of SAM35, SAM37 and
SAM50, to form a SAM(holo) complex. {ECO:0000255|HAMAP-
Rule:MF_03102, ECO:0000269|PubMed:13679517,
ECO:0000269|PubMed:15239954, ECO:0000269|PubMed:17410204,
ECO:0000269|PubMed:19556461}.
-!- INTERACTION:
Q92328:MDM12; NbExp=4; IntAct=EBI-10580, EBI-10584;
P14693:SAM35; NbExp=5; IntAct=EBI-10580, EBI-24602;
P53969:SAM50; NbExp=4; IntAct=EBI-10580, EBI-28646;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000255|HAMAP-Rule:MF_03102, ECO:0000269|PubMed:13679517,
ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16407407,
ECO:0000269|PubMed:19556461, ECO:0000269|PubMed:8089171}; Multi-
pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03102,
ECO:0000269|PubMed:13679517, ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:19556461,
ECO:0000269|PubMed:8089171}. Note=The ERMES/MDM complex localizes
to a few discrete foci (around 10 per single cell), that represent
mitochondria-endoplasmic reticulum junctions. These foci are often
found next to mtDNA nucleoids.
-!- DOMAIN: Lacks alpha-helical transmembrane segments, suggesting
that it resides in the membrane via beta-sheet conformations
similar to those predicted for other outer membrane proteins and
porin.
-!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the MDM10 family. {ECO:0000255|HAMAP-
Rule:MF_03102}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X80874; CAA56842.1; -; Genomic_DNA.
EMBL; L22015; AAC04948.1; -; Genomic_DNA.
EMBL; M36073; AAA35072.2; -; Genomic_DNA.
EMBL; L05146; AAC04947.1; -; Genomic_DNA.
EMBL; BK006935; DAA06978.2; -; Genomic_DNA.
PIR; PS0157; PS0157.
RefSeq; NP_009392.2; NM_001178155.2.
BioGrid; 31756; 355.
ComplexPortal; CPX-3196; ERMES complex.
DIP; DIP-6697N; -.
IntAct; P18409; 15.
MINT; P18409; -.
STRING; 4932.YAL010C; -.
TCDB; 1.B.33.3.1; the outer membrane protein insertion porin (bam complex) (ompip) family.
TCDB; 1.B.8.6.1; the mitochondrial and plastid porin (mpp) family.
TCDB; 9.A.58.1.1; the maintenance of mitochondrial morphology (mmm) family.
MaxQB; P18409; -.
PaxDb; P18409; -.
PRIDE; P18409; -.
EnsemblFungi; YAL010C_mRNA; YAL010C_mRNA; YAL010C.
GeneID; 851223; -.
KEGG; sce:YAL010C; -.
SGD; S000000008; MDM10.
HOGENOM; HOG000177242; -.
InParanoid; P18409; -.
KO; K17774; -.
OMA; TGWNEDN; -.
OrthoDB; EOG092C2VQ2; -.
BioCyc; YEAST:G3O-28823-MONOMER; -.
PRO; PR:P18409; -.
Proteomes; UP000002311; Chromosome I.
GO; GO:0032865; C:ERMES complex; IPI:SGD.
GO; GO:0031307; C:integral component of mitochondrial outer membrane; IEA:UniProtKB-UniRule.
GO; GO:0001401; C:mitochondrial sorting and assembly machinery complex; IPI:SGD.
GO; GO:0051654; P:establishment of mitochondrion localization; IMP:SGD.
GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IMP:SGD.
GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IMP:SGD.
GO; GO:0015914; P:phospholipid transport; IGI:SGD.
GO; GO:0045040; P:protein import into mitochondrial outer membrane; IMP:SGD.
HAMAP; MF_03102; Mdm10; 1.
InterPro; IPR027539; Mdm10.
PANTHER; PTHR28035; PTHR28035; 1.
Pfam; PF12519; MDM10; 1.
1: Evidence at protein level;
Complete proteome; Membrane; Mitochondrion;
Mitochondrion outer membrane; Reference proteome; Transmembrane;
Transmembrane beta strand.
CHAIN 1 493 Mitochondrial distribution and morphology
protein 10.
/FTId=PRO_0000096327.
CONFLICT 272 272 N -> Q (in Ref. 2; no nucleotide entry,
3; AAC04948 and 6; AAC04947).
{ECO:0000305}.
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


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