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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
 
 
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