MDM30_YEAST
ID MDM30_YEAST Reviewed; 598 AA.
AC Q05930; D6VZ05;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Mitochondrial distribution and morphology protein 30;
GN Name=MDM30; OrderedLocusNames=YLR368W;
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12808031; DOI=10.1091/mbc.e02-12-0831;
RA Fritz S., Weinbach N., Westermann B.;
RT "Mdm30 is an F-box protein required for maintenance of fusion-competent
RT mitochondria in yeast.";
RL Mol. Biol. Cell 14:2303-2313(2003).
RN [5]
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 [6]
RP INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(MDM30) COMPLEX.
RX PubMed=14747994; DOI=10.1002/prot.10620;
RA Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.;
RT "Functional interaction of 13 yeast SCF complexes with a set of yeast E2
RT enzymes in vitro.";
RL Proteins 54:455-467(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH FZO1.
RX PubMed=16735578; DOI=10.1083/jcb.200512079;
RA Escobar-Henriques M., Westermann B., Langer T.;
RT "Regulation of mitochondrial fusion by the F-box protein Mdm30 involves
RT proteasome-independent turnover of Fzo1.";
RL J. Cell Biol. 173:645-650(2006).
RN [8]
RP FUNCTION.
RX PubMed=18353967; DOI=10.1091/mbc.e08-02-0227;
RA Cohen M.M., Leboucher G.P., Livnat-Levanon N., Glickman M.H.,
RA Weissman A.M.;
RT "Ubiquitin-proteasome-dependent degradation of a mitofusin, a critical
RT regulator of mitochondrial fusion.";
RL Mol. Biol. Cell 19:2457-2464(2008).
RN [9]
RP FUNCTION, AND INTERACTION WITH FZO1.
RX PubMed=21385840; DOI=10.1242/jcs.073080;
RA Anton F., Fres J.M., Schauss A., Pinson B., Praefcke G.J., Langer T.,
RA Escobar-Henriques M.;
RT "Ugo1 and Mdm30 act sequentially during Fzo1-mediated mitochondrial outer
RT membrane fusion.";
RL J. Cell Sci. 124:1126-1135(2011).
RN [10]
RP FUNCTION, AND INTERACTION WITH FZO1.
RX PubMed=21502136; DOI=10.1242/jcs.079293;
RA Cohen M.M., Amiott E.A., Day A.R., Leboucher G.P., Pryce E.N.,
RA Glickman M.H., McCaffery J.M., Shaw J.M., Weissman A.M.;
RT "Sequential requirements for the GTPase domain of the mitofusin Fzo1 and
RT the ubiquitin ligase SCFMdm30 in mitochondrial outer membrane fusion.";
RL J. Cell Sci. 124:1403-1410(2011).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Probably recognizes and binds to phosphorylated target
CC proteins (By similarity). Recognizes FZO1 and regulates the amount of
CC FZO1. Regulatory factor for the mitochondrial fusion machinery.
CC Required for mitochondrial DNA maintenance. {ECO:0000250,
CC ECO:0000269|PubMed:11907266, ECO:0000269|PubMed:12808031,
CC ECO:0000269|PubMed:16735578, ECO:0000269|PubMed:18353967,
CC ECO:0000269|PubMed:21385840, ECO:0000269|PubMed:21502136}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with SKP1. Component of the probable SCF(MDM30)
CC complex containing CDC53, SKP1, RBX1 and MDM30. Interacts with SKP1 and
CC FZO1. {ECO:0000269|PubMed:14747994, ECO:0000269|PubMed:16735578,
CC ECO:0000269|PubMed:21385840, ECO:0000269|PubMed:21502136}.
CC -!- INTERACTION:
CC Q05930; P46972: IMP2; NbExp=2; IntAct=EBI-31799, EBI-9231;
CC Q05930; P52286: SKP1; NbExp=5; IntAct=EBI-31799, EBI-4090;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion.
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DR EMBL; U19103; AAB67566.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09671.1; -; Genomic_DNA.
DR PIR; S51386; S51386.
DR RefSeq; NP_013472.3; NM_001182257.3.
DR AlphaFoldDB; Q05930; -.
DR BioGRID; 31628; 93.
DR ComplexPortal; CPX-3242; SCF-Mdm30 ubiquitin ligase complex.
DR DIP; DIP-1239N; -.
DR IntAct; Q05930; 13.
DR MINT; Q05930; -.
DR STRING; 4932.YLR368W; -.
DR PaxDb; Q05930; -.
DR PRIDE; Q05930; -.
DR EnsemblFungi; YLR368W_mRNA; YLR368W; YLR368W.
DR GeneID; 851083; -.
DR KEGG; sce:YLR368W; -.
DR SGD; S000004360; MDM30.
DR VEuPathDB; FungiDB:YLR368W; -.
DR eggNOG; ENOG502QU21; Eukaryota.
DR HOGENOM; CLU_477498_0_0_1; -.
DR InParanoid; Q05930; -.
DR OMA; CHLEDIM; -.
DR BioCyc; YEAST:G3O-32437-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q05930; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05930; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:SGD.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; IMP:SGD.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Mitochondrion; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..598
FT /note="Mitochondrial distribution and morphology protein
FT 30"
FT /id="PRO_0000119969"
FT DOMAIN 13..59
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
SQ 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
