UGO1_YEAST
ID UGO1_YEAST Reviewed; 502 AA.
AC Q03327; D6VT94;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Mitochondrial fusion and transport protein UGO1;
GN Name=UGO1 {ECO:0000312|SGD:S000002878}; OrderedLocusNames=YDR470C;
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] {ECO:0000305, ECO:0000312|EMBL:AAB64924.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c {ECO:0000312|EMBL:AAB64924.2};
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2] {ECO:0000305}
RP SEQUENCE REVISION TO 114.
RX PubMed=10930523; DOI=10.1016/s0005-2736(00)00222-4;
RA Belenkiy R., Haefele A., Eisen M.B., Wohlrab H.;
RT "The yeast mitochondrial transport proteins: new sequences and consensus
RT residues, lack of direct relation between consensus residues and
RT transmembrane helices, expression patterns of the transport protein genes,
RT and protein-protein interactions with other proteins.";
RL Biochim. Biophys. Acta 1467:207-218(2000).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 114.
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11257114; DOI=10.1083/jcb.152.6.1123;
RA Sesaki H., Jensen R.E.;
RT "UGO1 encodes an outer membrane protein required for mitochondrial
RT fusion.";
RL J. Cell Biol. 152:1123-1134(2001).
RN [5] {ECO:0000305}
RP INTERACTION WITH FZO1 AND MGM1.
RX PubMed=12566426; DOI=10.1083/jcb.200209015;
RA Wong E.D., Wagner J.A., Scott S.V., Okreglak V., Holewinske T.J.,
RA Cassidy-Stone A., Nunnari J.;
RT "The intramitochondrial dynamin-related GTPase, Mgm1p, is a component of a
RT protein complex that mediates mitochondrial fusion.";
RL J. Cell Biol. 160:303-311(2003).
RN [6] {ECO:0000305}
RP INTERACTION WITH FZO1 AND MGM1.
RX PubMed=12808034; DOI=10.1091/mbc.e02-12-0788;
RA Sesaki H., Southard S.M., Yaffe M.P., Jensen R.E.;
RT "Mgm1p, a dynamin-related GTPase, is essential for fusion of the
RT mitochondrial outer membrane.";
RL Mol. Biol. Cell 14:2342-2356(2003).
RN [7] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [8] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH FZO1 AND MGM1.
RX PubMed=15087460; DOI=10.1074/jbc.m401363200;
RA Sesaki H., Jensen R.E.;
RT "Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion.";
RL J. Biol. Chem. 279:28298-28303(2004).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for mitochondrial fusion as well as normal
CC mitochondrial morphology by bridging the essential interaction between
CC FZO1 and MGM1. May coordinate fusion of inner and outer membranes
CC during mitochondrial fusion. {ECO:0000269|PubMed:11257114,
CC ECO:0000269|PubMed:15087460}.
CC -!- SUBUNIT: Interacts with FZO1 through its cytoplasmic domain and with
CC MGM1 through its mitochondrial intermembrane space domain.
CC {ECO:0000269|PubMed:12566426, ECO:0000269|PubMed:12808034,
CC ECO:0000269|PubMed:15087460}.
CC -!- INTERACTION:
CC Q03327; P38297: FZO1; NbExp=2; IntAct=EBI-32955, EBI-20900;
CC Q03327; P32266: MGM1; NbExp=2; IntAct=EBI-32955, EBI-10865;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:11257114, ECO:0000269|PubMed:14576278}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:11257114,
CC ECO:0000269|PubMed:14576278}.
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DR EMBL; U33050; AAB64924.2; -; Genomic_DNA.
DR EMBL; BK006938; DAA12304.2; -; Genomic_DNA.
DR PIR; S69637; S69637.
DR RefSeq; NP_010758.3; NM_001180778.2.
DR AlphaFoldDB; Q03327; -.
DR BioGRID; 32523; 88.
DR ComplexPortal; CPX-161; FZO1-MGM1-UGO1 complex.
DR IntAct; Q03327; 5.
DR MINT; Q03327; -.
DR STRING; 4932.YDR470C; -.
DR TCDB; 1.N.6.1.1; the mitochondrial inner/outer membrane fusion (mmf) family.
DR iPTMnet; Q03327; -.
DR MaxQB; Q03327; -.
DR PaxDb; Q03327; -.
DR PRIDE; Q03327; -.
DR EnsemblFungi; YDR470C_mRNA; YDR470C; YDR470C.
DR GeneID; 852081; -.
DR KEGG; sce:YDR470C; -.
DR SGD; S000002878; UGO1.
DR VEuPathDB; FungiDB:YDR470C; -.
DR eggNOG; ENOG502RQI2; Eukaryota.
DR HOGENOM; CLU_029376_0_0_1; -.
DR InParanoid; Q03327; -.
DR OMA; ELWRGWR; -.
DR BioCyc; YEAST:G3O-29997-MON; -.
DR PRO; PR:Q03327; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03327; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0015234; F:thiamine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:SGD.
DR GO; GO:1990627; P:mitochondrial inner membrane fusion; IMP:ComplexPortal.
DR GO; GO:1990626; P:mitochondrial outer membrane fusion; IMP:ComplexPortal.
DR GO; GO:0030974; P:thiamine pyrophosphate transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR SUPFAM; SSF103506; SSF103506; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Repeat; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..502
FT /note="Mitochondrial fusion and transport protein UGO1"
FT /id="PRO_0000270985"
FT TOPO_DOM 1..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..502
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REPEAT 288..383
FT /note="Solcar"
FT /evidence="ECO:0000255"
FT REGION 1..294
FT /note="Binds FZO1"
FT /evidence="ECO:0000269|PubMed:15087460"
FT REGION 312..502
FT /note="Binds MGM1"
FT /evidence="ECO:0000269|PubMed:15087460"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CONFLICT 114
FT /note="E -> G (in Ref. 1; AAB64924 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 57543 MW; 6417C4730DACD8F6 CRC64;
MNNNNVTEAT SRAQIRPYYD PDSFNAGYSA VFKPDEGVVD PHGYTIASKL NVINSSPTTK
RMANALFKSS PMKKLSNSVN DGLSLEGSNG EITGLNNFEW AELVNIQKWR KIFEQLLDMF
FRKYFQLLIQ QPFDVARLLI QVGEFKIFKT TVDTNKPQAP IILRDEEGDG AAREGEEDAY
DEEEIDFFPI ERKIAEANST APIMAEETDH SHHEPTDISL TIAPQSLHTI DVINALFDQE
GIRGLWKANN TTFIYNFLSL SIDTWFTGLL SSFLGVPDPY FMEVINSPDI SKSFILALGA
GVFTSIILLP VDLIRTRLIV TSFKKKKNVK TDGKNMVTNT RSLRQLIRCW SWRKNGVSIP
LDMWSLTILQ SINNSFFNKL FDLVIYNQFH IEKYSQTVMY NTMKFFSKSL ELFIKLPLEN
LLRRCQLNYL LNDQRLSFKV DSTELIVKPK KYNGIWDVIR NNSNTNRGQL WNGWKVGVIS
LICGYGLQMM NKVDINMEQE KF
