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Dynamin-related protein DNM1 (EC 3.6.5.5)

 DNM1_YEAST              Reviewed;         757 AA.
P54861; D6VY02;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
12-SEP-2018, entry version 161.
RecName: Full=Dynamin-related protein DNM1;
EC=3.6.5.5;
Name=DNM1; OrderedLocusNames=YLL001W; ORFNames=L1381;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7622557; DOI=10.1083/jcb.130.3.553;
Gammie A.E., Kurihara L.J., Vallee R.B., Rose M.D.;
"DNM1, a dynamin-related gene, participates in endosomal trafficking
in yeast.";
J. Cell Biol. 130:553-566(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 90840 / EAY235 / FY23;
PubMed=8810043;
DOI=10.1002/(SICI)1097-0061(19960615)12:7<693::AID-YEA956>3.0.CO;2-G;
Miosga T., Zimmermann F.K.;
"Sequence analysis of the CEN12 region of Saccharomyces cerevisiae on
a 43.7 kb fragment of chromosome XII including an open reading frame
homologous to the human cystic fibrosis transmembrane conductance
regulator protein CFTR.";
Yeast 12:693-708(1996).
[3]
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).
[4]
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).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10559943; DOI=10.1038/13014;
Bleazard W., McCaffery J.M., King E.J., Bale S., Mozdy A., Tieu Q.,
Nunnari J., Shaw J.M.;
"The dynamin-related GTPase Dnm1 regulates mitochondrial fission in
yeast.";
Nat. Cell Biol. 1:298-304(1999).
[6]
INTERACTION WITH MDV1, AND SUBCELLULAR LOCATION.
PubMed=11038182; DOI=10.1083/jcb.151.2.353;
Tieu Q., Nunnari J.;
"Mdv1p is a WD repeat protein that interacts with the dynamin-related
GTPase, Dnm1p, to trigger mitochondrial division.";
J. Cell Biol. 151:353-366(2000).
[7]
MUTAGENESIS OF LYS-705.
PubMed=11553714; DOI=10.1091/mbc.12.9.2756;
Fukushima N.H., Brisch E., Keegan B.R., Bleazard W., Shaw J.M.;
"The GTPase effector domain sequence of the Dnm1p GTPase regulates
self-assembly and controls a rate-limiting step in mitochondrial
fission.";
Mol. Biol. Cell 12:2756-2766(2001).
[8]
INTERACTION WITH FIS1 AND MDV1.
PubMed=14517324; DOI=10.1091/mbc.E03-02-0092;
Cerveny K.L., Jensen R.E.;
"The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate
division of mitochondria.";
Mol. Biol. Cell 14:4126-4139(2003).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23530241; DOI=10.1073/pnas.1300855110;
Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A.,
Shaw J.M.;
"Interchangeable adaptors regulate mitochondrial dynamin assembly for
membrane scission.";
Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013).
-!- FUNCTION: Microtubule-associated force-producing protein that
participates mitochondrial fission. Fission of mitochondria occurs
in many cell types and constitutes an important step in
mitochondria morphology, which is balanced between fusion and
fission. Functions antagonistically with FZO1.
{ECO:0000269|PubMed:10559943, ECO:0000269|PubMed:23530241}.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
-!- SUBUNIT: Interacts with FIS1 and MDV1.
{ECO:0000269|PubMed:11038182, ECO:0000269|PubMed:14517324}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-6002, EBI-6002;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000269|PubMed:10559943, ECO:0000269|PubMed:11038182,
ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23530241};
Peripheral membrane protein {ECO:0000269|PubMed:10559943,
ECO:0000269|PubMed:11038182, ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:23530241}; Cytoplasmic side
{ECO:0000269|PubMed:10559943, ECO:0000269|PubMed:11038182,
ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23530241}.
Note=Cytoplasm, localizes to the cytoplasmic outer membrane of
mitochondria.
-!- DOMAIN: The GTPase domain modulates a rate-limiting step in
mitochondrial membrane fission.
-!- MISCELLANEOUS: Present with 9600 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
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EMBL; L40588; AAA99998.1; -; Genomic_DNA.
EMBL; X91488; CAA62769.1; -; Genomic_DNA.
EMBL; Z73106; CAA97444.1; -; Genomic_DNA.
EMBL; BK006945; DAA09318.1; -; Genomic_DNA.
PIR; S64742; S64742.
RefSeq; NP_013100.1; NM_001181821.1.
ProteinModelPortal; P54861; -.
SMR; P54861; -.
BioGrid; 31273; 211.
DIP; DIP-1908N; -.
IntAct; P54861; 27.
MINT; P54861; -.
STRING; 4932.YLL001W; -.
iPTMnet; P54861; -.
MaxQB; P54861; -.
PaxDb; P54861; -.
PRIDE; P54861; -.
EnsemblFungi; YLL001W; YLL001W; YLL001W.
GeneID; 850686; -.
KEGG; sce:YLL001W; -.
EuPathDB; FungiDB:YLL001W; -.
SGD; S000003924; DNM1.
GeneTree; ENSGT00760000119213; -.
HOGENOM; HOG000161068; -.
InParanoid; P54861; -.
KO; K17065; -.
OMA; HHIPNRR; -.
OrthoDB; EOG092C16PN; -.
BioCyc; YEAST:G3O-32106-MONOMER; -.
Reactome; R-SCE-1169408; ISG15 antiviral mechanism.
Reactome; R-SCE-75153; Apoptotic execution phase.
PRO; PR:P54861; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IDA:SGD.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IDA:SGD.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IDA:SGD.
GO; GO:0001300; P:chronological cell aging; IMP:SGD.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; IBA:GO_Central.
GO; GO:0016236; P:macroautophagy; IMP:SGD.
GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
GO; GO:0061024; P:membrane organization; IDA:ParkinsonsUK-UCL.
GO; GO:0000266; P:mitochondrial fission; IDA:UniProtKB.
GO; GO:0000001; P:mitochondrion inheritance; IGI:SGD.
GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
GO; GO:0016559; P:peroxisome fission; IGI:SGD.
GO; GO:0007031; P:peroxisome organization; IMP:SGD.
GO; GO:0051260; P:protein homooligomerization; IDA:SGD.
GO; GO:0016050; P:vesicle organization; IDA:ParkinsonsUK-UCL.
CDD; cd08771; DLP_1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000375; Dynamin_central.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR019762; Dynamin_GTPase_CS.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR003130; GED.
InterPro; IPR020850; GED_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR011993; PH-like_dom_sf.
PANTHER; PTHR11566; PTHR11566; 1.
Pfam; PF01031; Dynamin_M; 1.
Pfam; PF00350; Dynamin_N; 1.
Pfam; PF02212; GED; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SMART; SM00302; GED; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
1: Evidence at protein level;
Complete proteome; GTP-binding; Hydrolase; Membrane; Mitochondrion;
Mitochondrion outer membrane; Motor protein; Nucleotide-binding;
Phosphoprotein; Reference proteome.
CHAIN 1 757 Dynamin-related protein DNM1.
/FTId=PRO_0000206586.
DOMAIN 25 333 Dynamin-type G. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
DOMAIN 670 757 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 35 42 GTP. {ECO:0000255}.
NP_BIND 175 179 GTP. {ECO:0000255}.
NP_BIND 244 247 GTP. {ECO:0000255}.
REGION 35 42 G1 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 61 63 G2 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 175 178 G3 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 244 247 G4 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
REGION 274 277 G5 motif. {ECO:0000255|PROSITE-
ProRule:PRU01055}.
MOD_RES 629 629 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MUTAGEN 705 705 K->A: Induces an increase of
mitochondrial fission.
{ECO:0000269|PubMed:11553714}.
CONFLICT 124 124 H -> ISPD (in Ref. 1; AAA99998).
{ECO:0000305}.
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


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