FZO1_YEAST
ID FZO1_YEAST Reviewed; 855 AA.
AC P38297; D6VQH3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Mitofusin FZO1;
DE EC=3.6.5.- {ECO:0000269|PubMed:19812251};
DE AltName: Full=Transmembrane GTPase FZO1;
GN Name=FZO1; OrderedLocusNames=YBR179C; ORFNames=YBR1241;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9685359; DOI=10.1074/jbc.273.32.20150;
RA Rapaport D., Brunner M., Neupert W., Westermann B.;
RT "Fzo1p is a mitochondrial outer membrane protein essential for the
RT biogenesis of functional mitochondria in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:20150-20155(1998).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-200; SER-201;
RP THR-221 AND LYS-371.
RX PubMed=9786948; DOI=10.1083/jcb.143.2.359;
RA Hermann G.J., Thatcher J.W., Mills J.P., Hales K.G., Fuller M.T.,
RA Nunnari J., Shaw J.M.;
RT "Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p.";
RL J. Cell Biol. 143:359-373(1998).
RN [5]
RP FUNCTION.
RX PubMed=10562274; DOI=10.1083/jcb.147.4.699;
RA Sesaki H., Jensen R.E.;
RT "Division versus fusion: Dnm1p and Fzo1p antagonistically regulate
RT mitochondrial shape.";
RL J. Cell Biol. 147:699-706(1999).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11266460; DOI=10.1083/jcb.152.4.683;
RA Fritz S., Rapaport D., Klanner E., Neupert W., Westermann B.;
RT "Connection of the mitochondrial outer and inner membranes by Fzo1 is
RT critical for organellar fusion.";
RL J. Cell Biol. 152:683-692(2001).
RN [7]
RP INTERACTION WITH MGM1 AND UGO1.
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 [8]
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 [9]
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 [10]
RP INTERACTION WITH UGO1 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 [11]
RP FUNCTION.
RX PubMed=15297626; DOI=10.1126/science.1100612;
RA Meeusen S., McCaffery J.M., Nunnari J.;
RT "Mitochondrial fusion intermediates revealed in vitro.";
RL Science 305:1747-1752(2004).
RN [12]
RP FUNCTION, AND PROTEIN DEGRADATION.
RX PubMed=15760898; DOI=10.1074/jbc.m500807200;
RA Neutzner A., Youle R.J.;
RT "Instability of the mitofusin Fzo1 regulates mitochondrial morphology
RT during the mating response of the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:18598-18603(2005).
RN [13]
RP FUNCTION, DOMAIN, SUBUNIT, AND MUTAGENESIS OF VAL-172; LYS-200; SER-201;
RP THR-221; TYR-490; LEU-501; LEU-504; LEU-518; LYS-538; TYR-769; LEU-773 AND
RP LEU-819.
RX PubMed=16624808; DOI=10.1074/jbc.m601847200;
RA Griffin E.E., Chan D.C.;
RT "Domain interactions within Fzo1 oligomers are essential for mitochondrial
RT fusion.";
RL J. Biol. Chem. 281:16599-16606(2006).
RN [14]
RP INTERACTION WITH MDM30.
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 [15]
RP UBIQUITINATION BY MDM30.
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 [16]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, UBIQUITINATION, AND MUTAGENESIS OF
RP VAL-196 AND VAL-327.
RX PubMed=19812251; DOI=10.1091/mbc.e09-07-0622;
RA Amiott E.A., Cohen M.M., Saint-Georges Y., Weissman A.M., Shaw J.M.;
RT "A mutation associated with CMT2A neuropathy causes defects in Fzo1 GTP
RT hydrolysis, ubiquitylation, and protein turnover.";
RL Mol. Biol. Cell 20:5026-5035(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [18]
RP FUNCTION.
RX PubMed=20550520; DOI=10.1111/j.1474-9726.2010.00587.x;
RA Palermo V., Falcone C., Calvani M., Mazzoni C.;
RT "Acetyl-L-carnitine protects yeast cells from apoptosis and aging and
RT inhibits mitochondrial fission.";
RL Aging Cell 9:570-579(2010).
RN [19]
RP FUNCTION.
RX PubMed=20505073; DOI=10.1091/mbc.e10-02-0096;
RA Hammermeister M., Schodel K., Westermann B.;
RT "Mdm36 is a mitochondrial fission-promoting protein in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 21:2443-2452(2010).
RN [20]
RP SUBUNIT, FUNCTION, MUTAGENESIS OF ASP-195; ASN-197; LYS-200; SER-201;
RP THR-221 AND ASP-320, INTERACTION WITH MDM30, AND UBIQUITINATION.
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 [21]
RP FUNCTION, MUTAGENESIS OF LYS-200; SER-201 AND THR-221, INTERACTION WITH
RP MDM30, AND UBIQUITINATION BY MDM30.
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).
RN [22]
RP FUNCTION.
RX PubMed=22353369; DOI=10.1016/j.mito.2012.02.001;
RA Fernandez-Cid A., Riera A., Herrero P., Moreno F.;
RT "Glucose levels regulate the nucleo-mitochondrial distribution of Mig2.";
RL Mitochondrion 12:370-380(2012).
RN [23]
RP FUNCTION, UBIQUITINATION AT LYS-398 AND LYS-464, INTERACTION WITH UBP2 AND
RP UBP12, DEUBIQUITINATION BY UBP2 AND UBP12, AND MUTAGENESIS OF LYS-398 AND
RP LYS-464.
RX PubMed=23317502; DOI=10.1016/j.molcel.2012.12.003;
RA Anton F., Dittmar G., Langer T., Escobar-Henriques M.;
RT "Two deubiquitylases act on mitofusin and regulate mitochondrial fusion
RT along independent pathways.";
RL Mol. Cell 49:487-498(2013).
RN [24]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27253069; DOI=10.7554/elife.14618;
RA Brandt T., Cavellini L., Kuehlbrandt W., Cohen M.M.;
RT "A mitofusin-dependent docking ring complex triggers mitochondrial fusion
RT in vitro.";
RL Elife 5:E14618-E14618(2016).
RN [25]
RP INTERACTION WITH DOA1, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=27044889; DOI=10.1083/jcb.201510098;
RA Wu X., Li L., Jiang H.;
RT "Doa1 targets ubiquitinated substrates for mitochondria-associated
RT degradation.";
RL J. Cell Biol. 213:49-63(2016).
RN [26]
RP TOPOLOGY, AND MUTAGENESIS OF LYS-200; ASP-313; ASP-335; LYS-464; TYR-490;
RP ASP-523; HIS-780; GLU-818 AND LEU-819.
RX PubMed=28860650; DOI=10.1038/s41598-017-10687-2;
RA De Vecchis D., Cavellini L., Baaden M., Henin J., Cohen M.M., Taly A.;
RT "A membrane-inserted structural model of the yeast mitofusin Fzo1.";
RL Sci. Rep. 7:10217-10217(2017).
CC -!- FUNCTION: Essential transmembrane GTPase, which mediates mitochondrial
CC fusion (PubMed:9685359, PubMed:9786948, PubMed:10562274,
CC PubMed:11266460, PubMed:15297626, PubMed:15760898, PubMed:16624808,
CC PubMed:19812251, PubMed:21385840, PubMed:21502136, PubMed:23317502,
CC PubMed:27253069). Fusion proceeds through several steps; first
CC mitochondria are tethered together, then brought into close contact,
CC followed by the formation of a docking ring around contact areas, and
CC finally membrane fusion (PubMed:27253069). Fusion of mitochondria
CC occurs in many cell types and constitutes an important step in
CC mitochondrial morphology, which is balanced between fusion and fission,
CC mediated by FZO1 and DNM1, respectively (PubMed:10562274). Functions
CC antagonistically with DNM1 (PubMed:10562274). Probably acts by forming
CC membrane contact sites that mediate mitochondrial membrane fusion
CC (PubMed:27253069). Mitochondrial docking and fusion requires GTP
CC hydrolysis (PubMed:15297626, PubMed:19812251, PubMed:27253069).
CC Mitochondrial fusion promotes also increased lifespan.
CC {ECO:0000269|PubMed:10562274, ECO:0000269|PubMed:11266460,
CC ECO:0000269|PubMed:15297626, ECO:0000269|PubMed:15760898,
CC ECO:0000269|PubMed:19812251, ECO:0000269|PubMed:20505073,
CC ECO:0000269|PubMed:20550520, ECO:0000269|PubMed:21385840,
CC ECO:0000269|PubMed:22353369, ECO:0000269|PubMed:27253069,
CC ECO:0000269|PubMed:9685359, ECO:0000269|PubMed:9786948}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:19812251};
CC -!- SUBUNIT: Homodimer (PubMed:16624808, PubMed:21385840, PubMed:19812251).
CC Dimerization depends on GTP binding (PubMed:16624808, PubMed:21385840,
CC PubMed:19812251). Component of a large multiprotein complex of 800 kDa
CC (PubMed:9685359). Binds the cytoplasmic domain of UGO1 which binds MGM1
CC through its intermembrane space domain (PubMed:15087460,
CC PubMed:12808034). Interacts with MDM30 (PubMed:21385840,
CC PubMed:21502136, PubMed:16735578). Interacts with UBP2 and UBP12
CC (PubMed:23317502). Interacts (when ubiquitinated) with DOA1; the
CC interaction recruits FZO1 to CDC48 and promotes FZO1 proteasomal
CC degradation (PubMed:27044889). {ECO:0000269|PubMed:12808034,
CC ECO:0000269|PubMed:15087460, ECO:0000269|PubMed:16624808,
CC ECO:0000269|PubMed:16735578, ECO:0000269|PubMed:19812251,
CC ECO:0000269|PubMed:21385840, ECO:0000269|PubMed:21502136,
CC ECO:0000269|PubMed:23317502, ECO:0000269|PubMed:27044889,
CC ECO:0000269|PubMed:9685359}.
CC -!- INTERACTION:
CC P38297; P32266: MGM1; NbExp=2; IntAct=EBI-20900, EBI-10865;
CC P38297; Q03327: UGO1; NbExp=2; IntAct=EBI-20900, EBI-32955;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:11266460, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:27044889, ECO:0000269|PubMed:27253069,
CC ECO:0000269|PubMed:9685359, ECO:0000269|PubMed:9786948}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11266460,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9685359,
CC ECO:0000269|PubMed:9786948}. Note=Detected at the periphery of
CC mitochondrial contact sites that form before mitochondrial fusion.
CC {ECO:0000269|PubMed:27253069}.
CC -!- DOMAIN: The GTPase domain may regulate the interaction with UGO1 since
CC FZO1 lacking the GTPase domain binds 5-fold higher amount of UGO1 than
CC full-length FZO1. The coiled-coil heptad repeat domains HRN, HR1 and
CC HR2 are required for the oligomerization and function in mitochondrial
CC fusion. {ECO:0000269|PubMed:16624808}.
CC -!- PTM: Ubiquitinated at Lys-398 and Lys-464 (PubMed:19812251,
CC PubMed:23317502, PubMed:27044889). MDM30 and UGO1 are involved in
CC ubiquitination (PubMed:18353967, PubMed:21385840, PubMed:21502136).
CC Deubiquitinated by UBP2 and UBP12 (PubMed:23317502). UBP2 and UBP12
CC recognize distinct ubiquitin chains on FZO1 that have opposing effects
CC on mitochondrial fusion (PubMed:23317502). UBP2 removes ubiquitin
CC chains that initiate proteolysis of FZO1 and inhibit fusion
CC (PubMed:23317502). UBP12 recognizes ubiquitin chains that stabilize
CC FZO1 and promote mitochondrial fusion. UBP12 deubiquitylates FZO1 only
CC after oligomerization (PubMed:23317502). {ECO:0000269|PubMed:18353967,
CC ECO:0000269|PubMed:19812251, ECO:0000269|PubMed:21385840,
CC ECO:0000269|PubMed:21502136, ECO:0000269|PubMed:23317502,
CC ECO:0000269|PubMed:27044889}.
CC -!- MISCELLANEOUS: Present with 1000 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.
CC {ECO:0000305}.
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DR EMBL; Z36048; CAA85140.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07293.1; -; Genomic_DNA.
DR PIR; S46050; S46050.
DR RefSeq; NP_009738.1; NM_001178527.1.
DR AlphaFoldDB; P38297; -.
DR BioGRID; 32877; 150.
DR ComplexPortal; CPX-161; FZO1-MGM1-UGO1 complex.
DR DIP; DIP-5581N; -.
DR IntAct; P38297; 4.
DR MINT; P38297; -.
DR STRING; 4932.YBR179C; -.
DR TCDB; 1.N.6.1.1; the mitochondrial inner/outer membrane fusion (mmf) family.
DR iPTMnet; P38297; -.
DR MaxQB; P38297; -.
DR PaxDb; P38297; -.
DR PRIDE; P38297; -.
DR TopDownProteomics; P38297; -.
DR EnsemblFungi; YBR179C_mRNA; YBR179C; YBR179C.
DR GeneID; 852477; -.
DR KEGG; sce:YBR179C; -.
DR SGD; S000000383; FZO1.
DR VEuPathDB; FungiDB:YBR179C; -.
DR eggNOG; KOG0448; Eukaryota.
DR GeneTree; ENSGT00390000013727; -.
DR HOGENOM; CLU_011752_0_0_1; -.
DR InParanoid; P38297; -.
DR OMA; AHEKAYI; -.
DR BioCyc; YEAST:G3O-29123-MON; -.
DR Reactome; R-SCE-9013419; RHOT2 GTPase cycle.
DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P38297; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38297; protein.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027094; Mitofusin_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10465; PTHR10465; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; GTP-binding; Hydrolase; Isopeptide bond; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..855
FT /note="Mitofusin FZO1"
FT /id="PRO_0000127682"
FT TOPO_DOM 1..705
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11266460"
FT TRANSMEM 706..726
FT /note="Helical; Name=1"
FT /evidence="ECO:0000305|PubMed:28860650"
FT TOPO_DOM 727..736
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:11266460"
FT TRANSMEM 737..757
FT /note="Helical; Name=2"
FT /evidence="ECO:0000305|PubMed:28860650"
FT TOPO_DOM 758..855
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:11266460"
FT DOMAIN 184..467
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..190
FT /note="HRN"
FT /evidence="ECO:0000305|PubMed:28860650"
FT REGION 413..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..547
FT /note="HR1"
FT /evidence="ECO:0000305|PubMed:28860650"
FT REGION 630..843
FT /note="Required for interaction with UGO1"
FT REGION 769..831
FT /note="HR2"
FT /evidence="ECO:0000305|PubMed:28860650"
FT COILED 798..825
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197..202
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT BINDING 370..373
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT BINDING 408
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IWA4"
FT CROSSLNK 398
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23317502"
FT CROSSLNK 464
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23317502"
FT MUTAGEN 172
FT /note="V->P: Abolishes fusion function."
FT /evidence="ECO:0000269|PubMed:16624808"
FT MUTAGEN 195
FT /note="D->A: Abolishes fusion function."
FT /evidence="ECO:0000269|PubMed:21385840"
FT MUTAGEN 196
FT /note="V->M: Leads to an unusual intermediate mitochondrial
FT morphology described as disorganized tubules in which
FT mitochondria are tubular, distorted, less branched, and
FT poorly distributed throughout the cell."
FT /evidence="ECO:0000269|PubMed:19812251"
FT MUTAGEN 197
FT /note="N->A: Abolishes fusion function."
FT /evidence="ECO:0000269|PubMed:21385840"
FT MUTAGEN 200
FT /note="K->A: Abolishes fusion function, MDM30-binding and
FT MDM30-dependent ubiquitination. No effect on localization
FT or interaction with UGO1."
FT /evidence="ECO:0000269|PubMed:16624808,
FT ECO:0000269|PubMed:21385840, ECO:0000269|PubMed:21502136,
FT ECO:0000269|PubMed:28860650, ECO:0000269|PubMed:9786948"
FT MUTAGEN 200
FT /note="K->D: Abolishes respiratory growth."
FT /evidence="ECO:0000269|PubMed:28860650"
FT MUTAGEN 200
FT /note="K->R: No effect."
FT /evidence="ECO:0000269|PubMed:28860650"
FT MUTAGEN 201
FT /note="S->N: Abolishes fusion function, MDM30-binding and
FT MDM30-dependent ubiquitination, but not localization to
FT mitochondrial outer membrane."
FT /evidence="ECO:0000269|PubMed:16624808,
FT ECO:0000269|PubMed:21385840, ECO:0000269|PubMed:21502136,
FT ECO:0000269|PubMed:9786948"
FT MUTAGEN 221
FT /note="T->A: Abolishes fusion function, MDM30-binding and
FT MDM30-dependent ubiquitination, but not localization to
FT mitochondrial outer membrane."
FT /evidence="ECO:0000269|PubMed:16624808,
FT ECO:0000269|PubMed:21385840, ECO:0000269|PubMed:21502136,
FT ECO:0000269|PubMed:9786948"
FT MUTAGEN 313
FT /note="D->K: Abolishes respiratory growth."
FT /evidence="ECO:0000269|PubMed:28860650"
FT MUTAGEN 320
FT /note="D->A: Loss of mitochondrial fusion."
FT /evidence="ECO:0000269|PubMed:21385840"
FT MUTAGEN 327
FT /note="V->T: Impairs GTP Hydrolysis and abolishes fusion
FT function."
FT /evidence="ECO:0000269|PubMed:19812251"
FT MUTAGEN 335
FT /note="D->K: Abolishes respiratory growth. Restores
FT respiratory growth; when associated with D-464."
FT /evidence="ECO:0000269|PubMed:28860650"
FT MUTAGEN 371
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:9786948"
FT MUTAGEN 398
FT /note="K->R: Leads to accelerated proteolysis."
FT /evidence="ECO:0000269|PubMed:23317502"
FT MUTAGEN 464
FT /note="K->D: Abolishes respiratory growth. Restores
FT respiratory growth; when associated with K-335."
FT /evidence="ECO:0000269|PubMed:28860650"
FT MUTAGEN 464
FT /note="K->R: Abolishes fusion function."
FT /evidence="ECO:0000269|PubMed:23317502"
FT MUTAGEN 490
FT /note="Y->A,K: No effect."
FT /evidence="ECO:0000269|PubMed:28860650"
FT MUTAGEN 490
FT /note="Y->P: Abolishes fusion function."
FT /evidence="ECO:0000269|PubMed:16624808"
FT MUTAGEN 501
FT /note="L->A: Abolishes fusion function; when associated
FT with Ala-504."
FT /evidence="ECO:0000269|PubMed:16624808"
FT MUTAGEN 504
FT /note="L->A: Abolishes fusion function; when associated
FT with Ala-501."
FT /evidence="ECO:0000269|PubMed:16624808"
FT MUTAGEN 518
FT /note="L->P: Abolishes fusion function."
FT /evidence="ECO:0000269|PubMed:16624808"
FT MUTAGEN 523
FT /note="D->H: Abolishes respiratory growth. Restores
FT respiratory growth; when associated with D-780."
FT /evidence="ECO:0000269|PubMed:28860650"
FT MUTAGEN 538
FT /note="K->P: Abolishes fusion function."
FT /evidence="ECO:0000269|PubMed:16624808"
FT MUTAGEN 769
FT /note="Y->P: Abolishes fusion function."
FT /evidence="ECO:0000269|PubMed:16624808"
FT MUTAGEN 773
FT /note="L->P: Abolishes fusion function."
FT /evidence="ECO:0000269|PubMed:16624808"
FT MUTAGEN 780
FT /note="H->D: No effect. Restores respiratory growth; when
FT associated with H-523."
FT /evidence="ECO:0000269|PubMed:28860650"
FT MUTAGEN 818
FT /note="E->A,R: No effect."
FT /evidence="ECO:0000269|PubMed:28860650"
FT MUTAGEN 818
FT /note="E->P: Abolishes respiratory growth."
FT /evidence="ECO:0000269|PubMed:28860650"
FT MUTAGEN 819
FT /note="L->A: No effect."
FT /evidence="ECO:0000269|PubMed:28860650"
FT MUTAGEN 819
FT /note="L->P,E: Abolishes fusion function."
FT /evidence="ECO:0000269|PubMed:16624808,
FT ECO:0000269|PubMed:28860650"
SQ SEQUENCE 855 AA; 97808 MW; D796DA455E2AE28B CRC64;
MSEGKQQFKD SNKPHKDSTD QDDDAATIVP QTLTYSRNEG HFLGSNFHGV TDDRTTLFDG
EEGRREDDLL PSLRSSNSKA HLISSQLSQW NYNNNRVLLK RSILKTQAFM DQLQEENNIR
PIFIAANDER EKLHVLQLNI KLDGQYNTKE KNGFNIEKKA LSKLFHSQIV SVTNHLNALK
KRVDDVSSKV FITGDVNTGK SALCNSLLKQ RLLPEDQLPC TNVFSEILEA RENDGIEEVH
AIPLNIAPTL KEAIDMYSIQ NPKTYEIHTL KELPDLVPQN GKYALLKIYI KDDKRPASTS
LLRNGTVDIS LIDSPGLNMD SLQTAEVMSR QEEIDLVIFV VNAENQLTLS AKEFISLASR
EKKLMFFVVK KFDKIRDKQR CKELILKQIR DLSPETYKRA ADFVHFVSKN GDELPHYHNE
NDNEDHGDRK PDDDPYSSSD PDPDFDSLED SLRNFVLKKR SLSKLLPAKT YLSKLLSDII
MISKSNMKMY SEEEIKINEQ LETLRPEILS ARAKCNDLTT SVDQMAEQTI TMTYNNTKEA
LLNALDVPLH EYPKYQGLGQ IYDFIFSTEA FIANQIDESI GSSELFAKQK TDLLVKKIYE
IGKNELGDDF MCERVFRSEL MFRKRKHLIG KRLKVSLSIT DLFAPTWKGF LSYLSWQKPV
TAPLPDIEGQ TNEGQIGLMK YLGLKNYPLT QYWSRPSLLF TSKIPTLTLY FLGSTKVVGN
IILNGIKLSS WSSLKKLSVP VIVVGSLLGL TYLIHDLPRA LPMNLSIKYK RKLQELDYIH
LNAQRTSNEV RDVLRVPTRE ILRSCEIIMD KKQITKKELE NKKESNLLSI KFFQSLYEGT
VAQKLMVEEI NLDID
