DYNA_DICDI
ID DYNA_DICDI Reviewed; 853 AA.
AC Q94464; Q54YU0;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Dynamin-A;
GN Name=dymA; ORFNames=DDB_G0277849;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=9880338; DOI=10.1091/mbc.10.1.225;
RA Wienke D.C., Knetsch M.L., Neuhaus E.M., Reedy M.C., Manstein D.J.;
RT "Disruption of a dynamin homologue affects endocytosis, organelle
RT morphology, and cytokinesis in Dictyostelium discoideum.";
RL Mol. Biol. Cell 10:225-243(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16782229; DOI=10.1016/j.ejcb.2006.05.008;
RA Koch K.V., Reinders Y., Ho T.-H., Sickmann A., Graef R.;
RT "Identification and isolation of Dictyostelium microtubule-associated
RT protein interactors by tandem affinity purification.";
RL Eur. J. Cell Biol. 85:1079-1090(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-316.
RX PubMed=11689422; DOI=10.1093/emboj/20.21.5813;
RA Niemann H.H., Knetsch M.L., Scherer A., Manstein D.J., Kull F.J.;
RT "Crystal structure of a dynamin GTPase domain in both nucleotide-free and
RT GDP-bound forms.";
RL EMBO J. 20:5813-5821(2001).
CC -!- FUNCTION: Function in membrane trafficking processes along the endo-
CC lysosomal pathway. {ECO:0000269|PubMed:9880338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9880338}.
CC Note=Found in association with endosomal and postlysosomal vacuoles.
CC -!- DEVELOPMENTAL STAGE: Present during all stages of development.
CC {ECO:0000269|PubMed:9880338}.
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; X99669; CAA67983.1; -; mRNA.
DR EMBL; AAFI02000023; EAL68097.1; -; Genomic_DNA.
DR RefSeq; XP_642112.1; XM_637020.1.
DR PDB; 1JWY; X-ray; 2.30 A; B=2-316.
DR PDB; 1JX2; X-ray; 2.30 A; B=2-316.
DR PDBsum; 1JWY; -.
DR PDBsum; 1JX2; -.
DR AlphaFoldDB; Q94464; -.
DR SMR; Q94464; -.
DR STRING; 44689.DDB0216177; -.
DR PaxDb; Q94464; -.
DR PRIDE; Q94464; -.
DR EnsemblProtists; EAL68097; EAL68097; DDB_G0277849.
DR GeneID; 8621323; -.
DR KEGG; ddi:DDB_G0277849; -.
DR dictyBase; DDB_G0277849; dymA.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_0_1; -.
DR InParanoid; Q94464; -.
DR OMA; IMATQFQ; -.
DR PhylomeDB; Q94464; -.
DR Reactome; R-DDI-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DDI-169911; Regulation of Apoptosis.
DR Reactome; R-DDI-196025; Formation of annular gap junctions.
DR Reactome; R-DDI-75153; Apoptotic execution phase.
DR Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR EvolutionaryTrace; Q94464; -.
DR PRO; PR:Q94464; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0032154; C:cleavage furrow; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0097204; C:phagocytic cup base; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0003925; F:G protein activity; IDA:dictyBase.
DR GO; GO:0005525; F:GTP binding; IDA:dictyBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:dictyBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IDA:dictyBase.
DR GO; GO:0005522; F:profilin binding; IPI:dictyBase.
DR GO; GO:0007015; P:actin filament organization; IMP:dictyBase.
DR GO; GO:0007032; P:endosome organization; IMP:dictyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:dictyBase.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:dictyBase.
DR GO; GO:0061952; P:midbody abscission; IMP:dictyBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:dictyBase.
DR GO; GO:0006997; P:nucleus organization; IMP:dictyBase.
DR GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0090383; P:phagosome acidification; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; IMP:dictyBase.
DR GO; GO:1905345; P:protein localization to cleavage furrow; IMP:dictyBase.
DR GO; GO:1900756; P:protein processing in phagocytic vesicle; IMP:dictyBase.
DR GO; GO:0044656; P:regulation of post-lysosomal vacuole size; IMP:dictyBase.
DR GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; GTP-binding; Hydrolase; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..853
FT /note="Dynamin-A"
FT /id="PRO_0000312856"
FT DOMAIN 22..296
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 762..853
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 32..39
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 58..60
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 138..141
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 207..210
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 237..240
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 523..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 207..213
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT BINDING 238..241
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O00429"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:1JWY"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1JWY"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:1JWY"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1JWY"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:1JWY"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:1JWY"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1JX2"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:1JWY"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:1JWY"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1JWY"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:1JWY"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:1JWY"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1JWY"
FT HELIX 276..305
FT /evidence="ECO:0007829|PDB:1JWY"
SQ SEQUENCE 853 AA; 96106 MW; 5812FF0B90CB97BC CRC64;
MDQLIPVINK LQDVFNTLGS DPLDLPQIVV VGSQSSGKSS VLENIVGRDF LPRGSGIVTR
RPLILQLTHL PIADDGSQTQ EWGEFLHKPN DMFYDFSEIR EEIIRDTDRM TGKNKGISAQ
PINLKIYSPH VVNLTLVDLP GITKVPVGDQ PTDIEQQIRR MVMAYIKKQN AIIVAVTPAN
TDLANSDALQ LAKEVDPEGK RTIGVITKLD LMDKGTDAME VLTGRVIPLT LGFIGVINRS
QEDIIAKKSI RESLKSEILY FKNHPIYKSI ANRSGTAYLS KTLNKLLMFH IRDTLPDLKV
KVSKMLSDVQ GELSTYGDPL YDTKNSQGAL LLQIITIFSS NFKDAIDGKL TDLSNNELYG
GARISYIFNE IYSHCVNNID PLEGISLNDI RTTMRNATGP RAALFIPEIS FELLVKKQVV
RLEEPSAQCV EYVYDELQRI VSQLEAKELS RFINLKARVI EVVNNLLQKH KVPTKTMIEH
LIKIETAFIN TSHPDFVGGE GIFESLYKKQ QLQQQNHLQQ LQDQYQQQQQ QQQQQQQQNG
INNNQKGDNG NMNVNQQNMN QQNMNQQNQS TNPFLQQQQQ GQNKYPGGPP AQQQPNQQPN
QLNKGPQNMP PNQSKPSSIP QNGPNNNNNN NNNNNRQDHQ QGSFFSSFFR ASPDPSLGQY
GGANNSNNSN NPTSPINSSS NSGNNYNTFG GQQSSSSSSQ QLQQSSQSQY KTSYNNNNNS
SSNNSSYNRY QDDFYGRGDK LNQVPSIIKA PDDLTSKEKF ETELIRELLI SYFNIVKKNV
KDSVPKSIMH FLVNQSKEHI QNELVAALYK EELFDELLEE SPQISSKRKS CKAMIEILRK
ANEIINEIRD FRN
