DLPA_DICDI
ID DLPA_DICDI Reviewed; 880 AA.
AC Q55F94; B0G0Y6; C7FZW1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Dynamin-like protein A;
DE EC=3.6.5.5;
GN Name=dlpA; Synonyms=slb233; ORFNames=DDB_G0268592;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=12796308; DOI=10.1128/ec.2.3.627-637.2003;
RA Maeda M., Sakamoto H., Iranfar N., Fuller D., Maruo T., Ogihara S.,
RA Morio T., Urushihara H., Tanaka Y., Loomis W.F.;
RT "Changing patterns of gene expression in Dictyostelium prestalk cell
RT subtypes recognized by in situ hybridization with genes from microarray
RT analyses.";
RL Eukaryot. Cell 2:627-637(2003).
RN [3]
RP INDUCTION.
RX PubMed=15470642; DOI=10.1387/ijdb.041862ns;
RA Shimada N., Maeda M., Urushihara H., Kawata T.;
RT "Identification of new modes of Dd-STATa regulation of gene expression in
RT Dictyostelium by in situ hybridisation.";
RL Int. J. Dev. Biol. 48:679-682(2004).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18809930; DOI=10.1073/pnas.0802412105;
RA Miyagishima S.Y., Kuwayama H., Urushihara H., Nakanishi H.;
RT "Evolutionary linkage between eukaryotic cytokinesis and chloroplast
RT division by dynamin proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15202-15207(2008).
CC -!- FUNCTION: Involved in cytokinesis. May hydrolyze GTP.
CC {ECO:0000269|PubMed:18809930}.
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:0000305}. Cleavage furrow
CC {ECO:0000269|PubMed:18809930}. Note=During cytokinesis, found in the
CC cleavage furrow.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q55F94-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q55F94-2; Sequence=VSP_037020;
CC Name=3;
CC IsoId=Q55F94-3; Sequence=VSP_037019;
CC -!- DEVELOPMENTAL STAGE: Expression begins during cell cycle progression,
CC between 12 and 24 hours after germination. Reach a maximum around mid-
CC log phase and disappear during the stationary phase. Expressed in the
CC central funnel of cells of migrating slugs and at the top of rising
CC culminants. Not expressed until the slug stage.
CC {ECO:0000269|PubMed:12796308, ECO:0000269|PubMed:18809930}.
CC -!- INDUCTION: Induced by STATa. {ECO:0000269|PubMed:15470642}.
CC -!- DISRUPTION PHENOTYPE: Produced cells are larger and a large amount of
CC them contains more than 2 nuclei. {ECO:0000269|PubMed:18809930}.
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; AAFI02000003; EAL73749.1; -; Genomic_DNA.
DR EMBL; AAFI02000003; EDR41124.1; -; Genomic_DNA.
DR EMBL; AAFI02000003; EEU04162.1; -; Genomic_DNA.
DR RefSeq; XP_001732949.1; XM_001732897.1.
DR RefSeq; XP_002649212.1; XM_002649166.1.
DR RefSeq; XP_647639.1; XM_642547.1.
DR AlphaFoldDB; Q55F94; -.
DR SMR; Q55F94; -.
DR STRING; 44689.DDB0233887; -.
DR PaxDb; Q55F94; -.
DR PRIDE; Q55F94; -.
DR EnsemblProtists; EAL73749; EAL73749; DDB_G0268592.
DR EnsemblProtists; EDR41124; EDR41124; DDB_G0268592.
DR EnsemblProtists; EEU04162; EEU04162; DDB_G0268592.
DR GeneID; 8616454; -.
DR KEGG; ddi:DDB_G0268592; -.
DR dictyBase; DDB_G0268592; dlpA.
DR eggNOG; KOG0446; Eukaryota.
DR InParanoid; Q55F94; -.
DR OMA; TRTIYWE; -.
DR PhylomeDB; Q55F94; -.
DR BRENDA; 3.6.5.5; 1939.
DR PRO; PR:Q55F94; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0032154; C:cleavage furrow; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IDA:dictyBase.
DR GO; GO:0001891; C:phagocytic cup; IDA:dictyBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IGI:dictyBase.
DR GO; GO:0061952; P:midbody abscission; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IMP:dictyBase.
DR GO; GO:0006997; P:nucleus organization; IMP:dictyBase.
DR GO; GO:1905345; P:protein localization to cleavage furrow; 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; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW GTP-binding; Hydrolase; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..880
FT /note="Dynamin-like protein A"
FT /id="PRO_0000371337"
FT DOMAIN 191..478
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..208
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 227..240
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 315..318
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 380..383
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 413..416
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 532..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 69..152
FT /evidence="ECO:0000255"
FT COILED 479..509
FT /evidence="ECO:0000255"
FT COILED 824..861
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 201..208
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 315..319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 380..383
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..19
FT /note="MSVFKKKDKSDDKKKKHDE -> MISCTNHHRTIYQNNLNNSINNSNNTVDN
FT KKI (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_037019"
FT VAR_SEQ 19
FT /note="E -> EVDNKKI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_037020"
SQ SEQUENCE 880 AA; 100009 MW; 055ACA2D0D209512 CRC64;
MSVFKKKDKS DDKKKKHDEE TPQGTFQPAS QSTSNTNLNS LASSVNNGAS VGSTNGSTPN
NSNGSTPTYN HNNSAEELEK QKKEEDEKRK KSELEAAAAV VAKKKEDEEK QRKEQVELER
KRRDEEIRRT NAAAANAANK ELNEQVEISS LEQMGKLDPS STIHDMFSFF PNEVYNSYEK
LQYFSRDLNT AVSHPEIVFV GPRSSGKSSL IEAFIGRALN IVGGGNIVGV GGSNANGCSK
RVLYLQFTNN IDFEVPKVTI KKDNTIKEFD HDIIVSIEQL NENLAKRNQL TNDYIEEPIY
VSIESRTTLN LTLIDSPGLL FDQSQAESNK IESIVSSLLR PSHRLIIAVE SCSQDWKSMS
MGQYLKKIDP ELSRSTFVFT KFHHTVRGFS STRDINKYLS GTVPDIKGFF VTLPNHQVRA
SYSEANRFQE KIYQAHKRDM HALEQLQYDK RYERTIGVAP LRRYILNIVW KSYQDTIPRI
LKHLRSKRQT AEATLNELQK QSSSLDSTKL RSIASNYTVT FLQITEKLLS GTSEGNPSAN
GQTLDEEKSQ QGDCGEWVDA YKEAIYIDPE EWNIPYWSSK LYGGQQLERL MAEFKAVCDN
SKISEVKMDD IATASGINKL NNIPNYAWAA SDLTSLISRD TFVPLIEQLC ERAMYIMKRL
TDIADKVIDS RRKSRCIGSS PFGGNGLNNI NSGGNNGINI NDRLSNTDMD SLDQYPFFTH
HVKNLYYDFV HRAAKGCKEK CMDEFYSSRT IYWELTEHPD SSLPSIRNDH HETKTAVCQL
ATKLFDSIRQ RITKNVLLKL YNFFLVPMQT DLWNEIQAQI TCLSNEQLEQ LFEVQATREQ
LKQEEKKQQQ ILEKYSQIDE QFLKAASLFC RPLSNPTPSA
