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Mitochondrial distribution and morphology protein 30

 MDM30_YEAST             Reviewed;         598 AA.
Q05930; D6VZ05;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 136.
RecName: Full=Mitochondrial distribution and morphology protein 30;
Name=MDM30; OrderedLocusNames=YLR368W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
GENOME REANNOTATION.
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).
[3]
FUNCTION.
PubMed=11907266; DOI=10.1091/mbc.01-12-0588;
Dimmer K.S., Fritz S., Fuchs F., Messerschmitt M., Weinbach N.,
Neupert W., Westermann B.;
"Genetic basis of mitochondrial function and morphology in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 13:847-853(2002).
[4]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12808031; DOI=10.1091/mbc.E02-12-0831;
Fritz S., Weinbach N., Westermann B.;
"Mdm30 is an F-box protein required for maintenance of fusion-
competent mitochondria in yeast.";
Mol. Biol. Cell 14:2303-2313(2003).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=14576278; DOI=10.1073/pnas.2135385100;
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P.,
Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B.,
Rehling P., Pfanner N., Meisinger C.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[6]
INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(MDM30) COMPLEX.
PubMed=14747994; DOI=10.1002/prot.10620;
Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.;
"Functional interaction of 13 yeast SCF complexes with a set of yeast
E2 enzymes in vitro.";
Proteins 54:455-467(2004).
[7]
FUNCTION, AND INTERACTION WITH FZO1.
PubMed=16735578; DOI=10.1083/jcb.200512079;
Escobar-Henriques M., Westermann B., Langer T.;
"Regulation of mitochondrial fusion by the F-box protein Mdm30
involves proteasome-independent turnover of Fzo1.";
J. Cell Biol. 173:645-650(2006).
[8]
FUNCTION.
PubMed=18353967; DOI=10.1091/mbc.E08-02-0227;
Cohen M.M., Leboucher G.P., Livnat-Levanon N., Glickman M.H.,
Weissman A.M.;
"Ubiquitin-proteasome-dependent degradation of a mitofusin, a critical
regulator of mitochondrial fusion.";
Mol. Biol. Cell 19:2457-2464(2008).
[9]
FUNCTION, AND INTERACTION WITH FZO1.
PubMed=21385840; DOI=10.1242/jcs.073080;
Anton F., Fres J.M., Schauss A., Pinson B., Praefcke G.J., Langer T.,
Escobar-Henriques M.;
"Ugo1 and Mdm30 act sequentially during Fzo1-mediated mitochondrial
outer membrane fusion.";
J. Cell Sci. 124:1126-1135(2011).
[10]
FUNCTION, AND INTERACTION WITH FZO1.
PubMed=21502136; DOI=10.1242/jcs.079293;
Cohen M.M., Amiott E.A., Day A.R., Leboucher G.P., Pryce E.N.,
Glickman M.H., McCaffery J.M., Shaw J.M., Weissman A.M.;
"Sequential requirements for the GTPase domain of the mitofusin Fzo1
and the ubiquitin ligase SCFMdm30 in mitochondrial outer membrane
fusion.";
J. Cell Sci. 124:1403-1410(2011).
-!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-
box protein) E3 ubiquitin-protein ligase complex which mediates
the ubiquitination and subsequent proteasomal degradation of
target proteins. Probably recognizes and binds to phosphorylated
target proteins (By similarity). Recognizes FZO1 and regulates the
amount of FZO1. Regulatory factor for the mitochondrial fusion
machinery. Required for mitochondrial DNA maintenance.
{ECO:0000250, ECO:0000269|PubMed:11907266,
ECO:0000269|PubMed:12808031, ECO:0000269|PubMed:16735578,
ECO:0000269|PubMed:18353967, ECO:0000269|PubMed:21385840,
ECO:0000269|PubMed:21502136}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with SKP1. Component of the probable SCF(MDM30)
complex containing CDC53, SKP1, RBX1 and MDM30. Interacts with
SKP1 and FZO1. {ECO:0000269|PubMed:14747994,
ECO:0000269|PubMed:16735578, ECO:0000269|PubMed:21385840,
ECO:0000269|PubMed:21502136}.
-!- INTERACTION:
P46972:IMP2; NbExp=2; IntAct=EBI-31799, EBI-9231;
P52286:SKP1; NbExp=3; IntAct=EBI-31799, EBI-4090;
-!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion.
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EMBL; U19103; AAB67566.1; -; Genomic_DNA.
EMBL; BK006945; DAA09671.1; -; Genomic_DNA.
PIR; S51386; S51386.
RefSeq; NP_013472.3; NM_001182257.3.
ProteinModelPortal; Q05930; -.
BioGrid; 31628; 79.
DIP; DIP-1239N; -.
IntAct; Q05930; 13.
MINT; Q05930; -.
STRING; 4932.YLR368W; -.
PaxDb; Q05930; -.
PRIDE; Q05930; -.
EnsemblFungi; YLR368W; YLR368W; YLR368W.
GeneID; 851083; -.
KEGG; sce:YLR368W; -.
EuPathDB; FungiDB:YLR368W; -.
SGD; S000004360; MDM30.
InParanoid; Q05930; -.
KO; K15070; -.
OMA; RESICEH; -.
OrthoDB; EOG092C3XON; -.
BioCyc; YEAST:G3O-32437-MONOMER; -.
UniPathway; UPA00143; -.
PRO; PR:Q05930; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
GO; GO:0001300; P:chronological cell aging; IMP:SGD.
GO; GO:0008053; P:mitochondrial fusion; IMP:SGD.
GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:SGD.
GO; GO:0010793; P:regulation of mRNA export from nucleus; IMP:SGD.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:SGD.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
Pfam; PF00646; F-box; 1.
SMART; SM00256; FBOX; 1.
SUPFAM; SSF81383; SSF81383; 1.
PROSITE; PS50181; FBOX; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Mitochondrion; Reference proteome;
Ubl conjugation pathway.
CHAIN 1 598 Mitochondrial distribution and morphology
protein 30.
/FTId=PRO_0000119969.
DOMAIN 13 59 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
SEQUENCE 598 AA; 70528 MW; CECDC2E2C7EDBB06 CRC64;
MTKRRNLFMV GSSFTIDHLP PEIWLCISKL VGTSDLHNLC LINRRLYLTI TSDEIWKRRC
YDRWINRESL DILTGNDYDS IPVSQWYSYY LRRAKWENKI FCLLWGLTEE TNPQHFREKY
LHILQFRHYK LATFLHRIIK QGYIPDKRPL DLITYANYLL KNVRHKYVFP LFYPTNAAEL
KNLNNMASRD AEMIYLRLSA IDTSFDDLLD AREFILNGIC SDLLQKYKKI EEFLKLRPVT
RVSKLISIST DYLDCFTQPH DSVGQTNDRA TGRELHREDF MLLRVYSREG RGYKTIILAI
IQAITKRYNV DSYLARDHLV VSEPDFPDGR AFVTVNEDFQ PYIFDKEDLL SVWSNNFHNA
ENFESTVLPA LLEPISIQHL LTEFFRELLR CKPRPFEGYP NRAHGLRDMF PYGKVEVPRD
VTMYFAFIYD LFDGMFESGM TSLRGQMLRD LLNYVNANNF GDLNIIIGQN ALKEPNDCWS
NKRDYVLLDD NNKIGYFYTD IETEDTLCAL NQYEVDGKVF ITTIDILGDI RVRLAEGLTP
FQGDNDKLWE SFSSVVPRTD WGLFFKGYDK ERRRMQLNPY IEEKLSNLAN DEQPLHNL


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