DNM1_YEAST
ID DNM1_YEAST Reviewed; 757 AA.
AC P54861; D6VY02;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Dynamin-related protein DNM1;
DE EC=3.6.5.5;
GN Name=DNM1; OrderedLocusNames=YLL001W; ORFNames=L1381;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7622557; DOI=10.1083/jcb.130.3.553;
RA Gammie A.E., Kurihara L.J., Vallee R.B., Rose M.D.;
RT "DNM1, a dynamin-related gene, participates in endosomal trafficking in
RT yeast.";
RL J. Cell Biol. 130:553-566(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX PubMed=8810043;
RX DOI=10.1002/(sici)1097-0061(19960615)12:7<693::aid-yea956>3.0.co;2-g;
RA Miosga T., Zimmermann F.K.;
RT "Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on a
RT 43.7 kb fragment of chromosome XII including an open reading frame
RT homologous to the human cystic fibrosis transmembrane conductance regulator
RT protein CFTR.";
RL Yeast 12:693-708(1996).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10559943; DOI=10.1038/13014;
RA Bleazard W., McCaffery J.M., King E.J., Bale S., Mozdy A., Tieu Q.,
RA Nunnari J., Shaw J.M.;
RT "The dynamin-related GTPase Dnm1 regulates mitochondrial fission in
RT yeast.";
RL Nat. Cell Biol. 1:298-304(1999).
RN [6]
RP INTERACTION WITH MDV1, AND SUBCELLULAR LOCATION.
RX PubMed=11038182; DOI=10.1083/jcb.151.2.353;
RA Tieu Q., Nunnari J.;
RT "Mdv1p is a WD repeat protein that interacts with the dynamin-related
RT GTPase, Dnm1p, to trigger mitochondrial division.";
RL J. Cell Biol. 151:353-366(2000).
RN [7]
RP MUTAGENESIS OF LYS-705.
RX PubMed=11553714; DOI=10.1091/mbc.12.9.2756;
RA Fukushima N.H., Brisch E., Keegan B.R., Bleazard W., Shaw J.M.;
RT "The GTPase effector domain sequence of the Dnm1p GTPase regulates self-
RT assembly and controls a rate-limiting step in mitochondrial fission.";
RL Mol. Biol. Cell 12:2756-2766(2001).
RN [8]
RP INTERACTION WITH FIS1 AND MDV1.
RX PubMed=14517324; DOI=10.1091/mbc.e03-02-0092;
RA Cerveny K.L., Jensen R.E.;
RT "The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division
RT of mitochondria.";
RL Mol. Biol. Cell 14:4126-4139(2003).
RN [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND IDENTIFICATION BY
RP 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 [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23530241; DOI=10.1073/pnas.1300855110;
RA Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.;
RT "Interchangeable adaptors regulate mitochondrial dynamin assembly for
RT membrane scission.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013).
CC -!- FUNCTION: Microtubule-associated force-producing protein that
CC participates mitochondrial fission. Fission of mitochondria occurs in
CC many cell types and constitutes an important step in mitochondria
CC morphology, which is balanced between fusion and fission. Functions
CC antagonistically with FZO1. {ECO:0000269|PubMed:10559943,
CC ECO:0000269|PubMed:23530241}.
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; EC=3.6.5.5;
CC -!- SUBUNIT: Interacts with FIS1 and MDV1. {ECO:0000269|PubMed:11038182,
CC ECO:0000269|PubMed:14517324}.
CC -!- INTERACTION:
CC P54861; P54861: DNM1; NbExp=4; IntAct=EBI-6002, EBI-6002;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:10559943, ECO:0000269|PubMed:11038182,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23530241}; Peripheral
CC membrane protein {ECO:0000269|PubMed:10559943,
CC ECO:0000269|PubMed:11038182, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:23530241}; Cytoplasmic side
CC {ECO:0000269|PubMed:10559943, ECO:0000269|PubMed:11038182,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23530241}.
CC Note=Cytoplasm, localizes to the cytoplasmic outer membrane of
CC mitochondria.
CC -!- DOMAIN: The GTPase domain modulates a rate-limiting step in
CC mitochondrial membrane fission.
CC -!- MISCELLANEOUS: Present with 9600 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. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; L40588; AAA99998.1; -; Genomic_DNA.
DR EMBL; X91488; CAA62769.1; -; Genomic_DNA.
DR EMBL; Z73106; CAA97444.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09318.1; -; Genomic_DNA.
DR PIR; S64742; S64742.
DR RefSeq; NP_013100.1; NM_001181821.1.
DR AlphaFoldDB; P54861; -.
DR SMR; P54861; -.
DR BioGRID; 31273; 217.
DR DIP; DIP-1908N; -.
DR IntAct; P54861; 27.
DR MINT; P54861; -.
DR STRING; 4932.YLL001W; -.
DR iPTMnet; P54861; -.
DR MaxQB; P54861; -.
DR PaxDb; P54861; -.
DR PRIDE; P54861; -.
DR EnsemblFungi; YLL001W_mRNA; YLL001W; YLL001W.
DR GeneID; 850686; -.
DR KEGG; sce:YLL001W; -.
DR SGD; S000003924; DNM1.
DR VEuPathDB; FungiDB:YLL001W; -.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000172538; -.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; P54861; -.
DR OMA; IMATQFQ; -.
DR BioCyc; YEAST:G3O-32106-MON; -.
DR BRENDA; 3.6.5.5; 984.
DR Reactome; R-SCE-169911; Regulation of Apoptosis.
DR Reactome; R-SCE-196025; Formation of annular gap junctions.
DR PRO; PR:P54861; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P54861; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IDA:SGD.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0015886; P:heme transport; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0061024; P:membrane organization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000266; P:mitochondrial fission; IDA:UniProtKB.
DR GO; GO:0000001; P:mitochondrion inheritance; IGI:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
DR GO; GO:0016559; P:peroxisome fission; IGI:SGD.
DR GO; GO:0007031; P:peroxisome organization; IMP:SGD.
DR GO; GO:0051260; P:protein homooligomerization; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016050; P:vesicle organization; IDA:ParkinsonsUK-UCL.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 2.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..757
FT /note="Dynamin-related protein DNM1"
FT /id="PRO_0000206586"
FT DOMAIN 25..333
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 670..757
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 35..42
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 61..63
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 175..178
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 244..247
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 274..277
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 557..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35..42
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 175..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 244..247
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 705
FT /note="K->A: Induces an increase of mitochondrial fission."
FT /evidence="ECO:0000269|PubMed:11553714"
FT CONFLICT 124
FT /note="H -> ISPD (in Ref. 1; AAA99998)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 84972 MW; EBEF8793C5951770 CRC64;
MASLEDLIPT VNKLQDVMYD SGIDTLDLPI LAVVGSQSSG KSSILETLVG RDFLPRGTGI
VTRRPLVLQL NNISPNSPLI EEDDNSVNPH DEVTKISGFE AGTKPLEYRG KERNHADEWG
EFLHIPGKRF YDFDDIKREI ENETARIAGK DKGISKIPIN LKVFSPHVLN LTLVDLPGIT
KVPIGEQPPD IEKQIKNLIL DYIATPNCLI LAVSPANVDL VNSESLKLAR EVDPQGKRTI
GVITKLDLMD SGTNALDILS GKMYPLKLGF VGVVNRSQQD IQLNKTVEES LDKEEDYFRK
HPVYRTISTK CGTRYLAKLL NQTLLSHIRD KLPDIKTKLN TLISQTEQEL ARYGGVGATT
NESRASLVLQ LMNKFSTNFI SSIDGTSSDI NTKELCGGAR IYYIYNNVFG NSLKSIDPTS
NLSVLDVRTA IRNSTGPRPT LFVPELAFDL LVKPQIKLLL EPSQRCVELV YEELMKICHK
CGSAELARYP KLKSMLIEVI SELLRERLQP TRSYVESLID IHRAYINTNH PNFLSATEAM
DDIMKTRRKR NQELLKSKLS QQENGQTNGI NGTSSISSNI DQDSAKNSDY DDDGIDAESK
QTKDKFLNYF FGKDKKGQPV FDASDKKRSI AGDGNIEDFR NLQISDFSLG DIDDLENAEP
PLTEREELEC ELIKRLIVSY FDIIREMIED QVPKAVMCLL VNYCKDSVQN RLVTKLYKET
LFEELLVEDQ TLAQDRELCV KSLGVYKKAA TLISNIL
