DNM1_SCHPO
ID DNM1_SCHPO Reviewed; 781 AA.
AC Q09748;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Dynamin-related protein dnm1;
DE EC=3.6.5.5;
GN Name=dnm1; ORFNames=SPBC12C2.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION.
RX PubMed=18088324; DOI=10.1111/j.1600-0854.2007.00685.x;
RA Jourdain I., Sontam D., Johnson C., Dillies C., Hyams J.S.;
RT "Dynamin-dependent biogenesis, cell cycle regulation and mitochondrial
RT association of peroxisomes in fission yeast.";
RL Traffic 9:353-365(2008).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19373772; DOI=10.1002/cm.20351;
RA Jourdain I., Gachet Y., Hyams J.S.;
RT "The dynamin related protein Dnm1 fragments mitochondria in a microtubule-
RT dependent manner during the fission yeast cell cycle.";
RL Cell Motil. Cytoskeleton 66:509-523(2009).
CC -!- FUNCTION: Microtubule-associated force-producing protein that mediates
CC mitochondrial fission during interphasic growth and at cell division.
CC Fission of mitochondria occurs in many cell types and constitutes an
CC important step in mitochondria morphology, which is balanced between
CC fusion and fission. With vps1, acts redundantly in peroxisome
CC biogenesis, which is under cell cycle control.
CC {ECO:0000269|PubMed:18088324, ECO:0000269|PubMed:19373772}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:19373772}. Mitochondrion outer membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Localizes at sites of mitochondrial
CC constriction.
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; CU329671; CAA90821.1; -; Genomic_DNA.
DR PIR; T39373; T39373.
DR RefSeq; NP_596014.1; NM_001021922.2.
DR AlphaFoldDB; Q09748; -.
DR SMR; Q09748; -.
DR BioGRID; 276694; 24.
DR STRING; 4896.SPBC12C2.08.1; -.
DR MaxQB; Q09748; -.
DR PaxDb; Q09748; -.
DR EnsemblFungi; SPBC12C2.08.1; SPBC12C2.08.1:pep; SPBC12C2.08.
DR GeneID; 2540159; -.
DR KEGG; spo:SPBC12C2.08; -.
DR PomBase; SPBC12C2.08; dnm1.
DR VEuPathDB; FungiDB:SPBC12C2.08; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; Q09748; -.
DR OMA; IMATQFQ; -.
DR PhylomeDB; Q09748; -.
DR Reactome; R-SPO-169911; Regulation of Apoptosis.
DR Reactome; R-SPO-196025; Formation of annular gap junctions.
DR Reactome; R-SPO-437239; Recycling pathway of L1.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q09748; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
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; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IDA:PomBase.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:1990606; F:membrane scission GTPase motor activity; TAS:PomBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0034643; P:establishment of mitochondrion localization, microtubule-mediated; IGI:PomBase.
DR GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
DR GO; GO:0090149; P:mitochondrial membrane fission; IMP:PomBase.
DR GO; GO:0000001; P:mitochondrion inheritance; IMP:PomBase.
DR GO; GO:0016559; P:peroxisome fission; IBA:GO_Central.
DR GO; GO:0007031; P:peroxisome organization; IGI:PomBase.
DR GO; GO:0140572; P:vacuole fission; IMP:PomBase.
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; 1.
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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Motor protein; Nucleotide-binding;
KW Peroxisome biogenesis; Reference proteome.
FT CHAIN 1..781
FT /note="Dynamin-related protein dnm1"
FT /id="PRO_0000206589"
FT DOMAIN 23..328
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 694..781
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 33..40
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 59..61
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 76..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..173
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 239..242
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 269..272
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 170..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 239..242
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 781 AA; 87009 MW; 9431E088F92C27D6 CRC64;
MEQLIPLVNQ LQDLVYNTIG SDFLDLPSIV VVGSQSCGKS SVLENIVGKD FLPRGTGIVT
RRPLILQLIN LKRKTKNNHD EESTSDNNSE ETSAAGETGS LEGIEEDSDE IEDYAEFLHI
PDTKFTDMNK VRAEIENETL RVAGANKGIN KLPINLKIYS TRVLNLTLID LPGLTKIPVG
DQPTDIEAQT RSLIMEYISR PNSIILAVSP ANFDIVNSEG LKLARSVDPK GKRTIGVLTK
LDLMDQGTNA MDILSGRVYP LKLGFVATVN RSQSDIVSHK SMRDALQSER SFFEHHPAYR
TIKDRCGTPY LAKTLSNLLV SHIRERLPDI KARLSTLISQ TQQQLNNYGD FKLSDQSQRG
IILLQAMNRF ANTFIASIDG NSSNIPTKEL SGGARLYSIF NNVFTTALNS IDPLQNLSTV
DIRTAILNST GSRATLFLSE MAFDILVKPQ LNLLAAPCHQ CVELVYEELM KICHYSGDSD
ISHFPKLQTA LVETVSDLLR ENLTPTYSFV ESLIAIQSAY INTNHPDFLG VQGAMAVVLS
RKEQNRLMLS QENDEPISSA LDTVKPDGIE LYSSDPDTSV KSITNKATNE ITTLKSDDSA
KMQPLDVLAS KRYNNAFSTE TAERKTFLSY VFGANNATRK AMSIDKSSSY PLNDSLSGGD
TNHKNNHPLK MTDLSNEVET MALEDMSERE EVEVDLIKEL ITSYFNLTRK IIIDQVPKVI
MHLLVNASKD AIQNRLVSKL YREDFFDTLL IEDENVKSER EKCERLLSVY NQANKIISTV
F
