DYN1_CAEEL
ID DYN1_CAEEL Reviewed; 830 AA.
AC P39055; Q93176; Q95QY9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Dynamin;
DE EC=3.6.5.5;
GN Name=dyn-1; ORFNames=C02C6.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF PRO-70.
RC STRAIN=Bristol N2;
RX PubMed=9294229; DOI=10.1073/pnas.94.19.10438;
RA Clark S.G., Shurland D.L., Meyerowitz E.M., Bargmann C.I.,
RA van der Bliek A.M.;
RT "A dynamin GTPase mutation causes a rapid and reversible temperature-
RT inducible locomotion defect in C. elegans.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:10438-10443(1997).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA van der Bliek A.M.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS A AND B).
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION, INTERACTION WITH VPS-34 AND RAB-5, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-70.
RX PubMed=18425118; DOI=10.1038/ncb1718;
RA Kinchen J.M., Doukoumetzidis K., Almendinger J., Stergiou L.,
RA Tosello-Trampont A., Sifri C.D., Hengartner M.O., Ravichandran K.S.;
RT "A pathway for phagosome maturation during engulfment of apoptotic cells.";
RL Nat. Cell Biol. 10:556-566(2008).
RN [5]
RP FUNCTION, INTERACTION WITH TAX-6, AND MUTAGENESIS OF PRO-70.
RX PubMed=20803083; DOI=10.1007/s10059-010-0116-x;
RA Song H.O., Lee J., Ji Y.J., Dwivedi M., Cho J.H., Park B.J., Ahnn J.;
RT "Calcineurin regulates coelomocyte endocytosis via DYN-1 and CUP-4 in
RT Caenorhabditis elegans.";
RL Mol. Cells 30:255-262(2010).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-204.
RX PubMed=21490059; DOI=10.1242/dev.060012;
RA Neukomm L.J., Nicot A.S., Kinchen J.M., Almendinger J., Pinto S.M.,
RA Zeng S., Doukoumetzidis K., Tronchere H., Payrastre B., Laporte J.F.,
RA Hengartner M.O.;
RT "The phosphoinositide phosphatase MTM-1 regulates apoptotic cell corpse
RT clearance through CED-5-CED-12 in C. elegans.";
RL Development 138:2003-2014(2011).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLY-204.
RX PubMed=22272187; DOI=10.1371/journal.pbio.1001245;
RA Lu N., Shen Q., Mahoney T.R., Neukomm L.J., Wang Y., Zhou Z.;
RT "Two PI 3-kinases and one PI 3-phosphatase together establish the cyclic
RT waves of phagosomal PtdIns(3)P critical for the degradation of apoptotic
RT cells.";
RL PLoS Biol. 10:E1001245-E1001245(2012).
CC -!- FUNCTION: Microtubule-associated force-producing protein involved in
CC producing microtubule bundles and able to bind and hydrolyze GTP. Most
CC probably involved in vesicular trafficking processes, in particular
CC endocytosis (By similarity). Required for coelomocyte endocytosis
CC (PubMed:20803083). Involved in apoptotic cell phagocytosis
CC (PubMed:21490059). Required for recruitment of phosphatidylinositol 3-
CC kinase piki-1 to phagosomes (PubMed:22272187). May play a role in rab-5
CC recruitment to cell-corpses-containing phagosomes but not to endosomes
CC (PubMed:18425118). Required for embryonic and larval development
CC (PubMed:9294229, PubMed:21490059, PubMed:20803083).
CC {ECO:0000250|UniProtKB:P39052, ECO:0000269|PubMed:18425118,
CC ECO:0000269|PubMed:20803083, ECO:0000269|PubMed:21490059,
CC ECO:0000269|PubMed:22272187}.
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 -!- SUBUNIT: May be a component of a complex composed of rab-5 (in GDP-
CC bound form), dyn-1 and vps-34 (PubMed:18425118). Interacts with tax-6
CC (PubMed:20803083). {ECO:0000269|PubMed:20803083,
CC ECO:0000305|PubMed:18425118}.
CC -!- INTERACTION:
CC P39055; P34258: B0303.7; NbExp=4; IntAct=EBI-317945, EBI-322705;
CC P39055; Q7K7J0: gei-18; NbExp=3; IntAct=EBI-317945, EBI-2315822;
CC P39055; Q8I4E2: lst-4; NbExp=4; IntAct=EBI-317945, EBI-4325777;
CC P39055; Q9N2Z7: wwp-1; NbExp=3; IntAct=EBI-317945, EBI-317369;
CC P39055; G5ECK4: Y37A1B.17; NbExp=4; IntAct=EBI-317945, EBI-6533538;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39052}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18425118}. Cytoplasmic
CC vesicle, phagosome membrane {ECO:0000269|PubMed:18425118}; Peripheral
CC membrane protein {ECO:0000269|PubMed:18425118}. Note=Microtubule-
CC associated (By similarity). Transiently associates with cell corpses
CC containing early phagosomes where it colocalizes with vps-34 and rab-5
CC (PubMed:18425118). {ECO:0000250|UniProtKB:P39052,
CC ECO:0000269|PubMed:18425118}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P39055-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P39055-2; Sequence=VSP_001329;
CC -!- TISSUE SPECIFICITY: Expressed in motor neurons in the head and in
CC ventral nerve cord and, to a lesser extent, in sensory neurons in the
CC nerve ring and the tail and interneurons. Expressed in pharyngeal-
CC intestinal valve, intestinal-rectal valve and in intestinal cells.
CC {ECO:0000269|PubMed:9294229}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes abnormal
CC accumulation of apoptotic cell corpses in early phagosomes in gonads.
CC {ECO:0000269|PubMed:18425118}.
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; L29031; AAB72228.2; -; mRNA.
DR EMBL; Z79596; CAB01857.1; -; Genomic_DNA.
DR EMBL; Z79596; CAC42251.1; -; Genomic_DNA.
DR PIR; T18860; T18860.
DR RefSeq; NP_001024331.1; NM_001029160.2.
DR RefSeq; NP_001024332.1; NM_001029161.2. [P39055-2]
DR AlphaFoldDB; P39055; -.
DR SMR; P39055; -.
DR BioGRID; 46538; 37.
DR IntAct; P39055; 19.
DR MINT; P39055; -.
DR STRING; 6239.C02C6.1b; -.
DR EPD; P39055; -.
DR PaxDb; P39055; -.
DR PeptideAtlas; P39055; -.
DR PRIDE; P39055; -.
DR EnsemblMetazoa; C02C6.1a.1; C02C6.1a.1; WBGene00001130. [P39055-1]
DR EnsemblMetazoa; C02C6.1b.1; C02C6.1b.1; WBGene00001130. [P39055-2]
DR GeneID; 181644; -.
DR KEGG; cel:CELE_C02C6.1; -.
DR UCSC; C02C6.1b; c. elegans. [P39055-1]
DR CTD; 181644; -.
DR WormBase; C02C6.1a; CE07833; WBGene00001130; dyn-1. [P39055-1]
DR WormBase; C02C6.1b; CE07832; WBGene00001130; dyn-1. [P39055-2]
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000166903; -.
DR HOGENOM; CLU_008964_1_0_1; -.
DR InParanoid; P39055; -.
DR OMA; MQMVQTF; -.
DR OrthoDB; 264244at2759; -.
DR PhylomeDB; P39055; -.
DR BRENDA; 3.6.5.5; 1045.
DR Reactome; R-CEL-190873; Gap junction degradation.
DR Reactome; R-CEL-196025; Formation of annular gap junctions.
DR Reactome; R-CEL-203641; NOSTRIN mediated eNOS trafficking.
DR Reactome; R-CEL-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-CEL-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-CEL-437239; Recycling pathway of L1.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P39055; -.
DR PRO; PR:P39055; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001130; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0045177; C:apical part of cell; IDA:WormBase.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
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:WormBase.
DR GO; GO:1990075; C:periciliary membrane compartment; IDA:WormBase.
DR GO; GO:0001891; C:phagocytic cup; IDA:WormBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:WormBase.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0048786; C:presynaptic active zone; IDA:WormBase.
DR GO; GO:0031143; C:pseudopodium; IDA:WormBase.
DR GO; GO:0005876; C:spindle microtubule; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:WormBase.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0006897; P:endocytosis; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0090386; P:phagosome maturation involved in apoptotic cell clearance; IMP:WormBase.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IGI:WormBase.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:WormBase.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027741; DNM1.
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 InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR PANTHER; PTHR11566:SF32; PTHR11566:SF32; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SMART; SM00233; PH; 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.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Endocytosis; GTP-binding; Hydrolase; Membrane; Microtubule; Motor protein;
KW Nucleotide-binding; Phagocytosis; Reference proteome.
FT CHAIN 1..830
FT /note="Dynamin"
FT /id="PRO_0000206575"
FT DOMAIN 30..296
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 519..624
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 653..744
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 40..47
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 66..68
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 743..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..805
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..830
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40..48
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 VAR_SEQ 817..830
FT /note="PGPGGPPPNMAPPR -> VPTPSNGAPEIPARPQVPKRPF (in isoform
FT b)"
FT /evidence="ECO:0000305"
FT /id="VSP_001329"
FT MUTAGEN 70
FT /note="P->S: In dy51; temperature sensitive mutant which at
FT the restrictive temperature of 25 degrees Celsius displays
FT uncoordinated movements, reduced pharyngeal pumping rate,
FT prolonged defecation cycle, an egg-laying defect and
FT embryonic lethality of the progeny. Accumulates of
FT apoptotic cell corpses in abnormally enlarged early
FT phagosomes prior to rab-5 recruitment. Decreases rab-5
FT recruitment to phagosomes. Impaired coelomocyte
FT endocytosis."
FT /evidence="ECO:0000269|PubMed:18425118,
FT ECO:0000269|PubMed:20803083, ECO:0000269|PubMed:9294229"
FT MUTAGEN 204
FT /note="G->E: In n4039; loss of apoptotic cell engulfment.
FT Embryos fail to hatch. Loss of piki-1 recruitment to the
FT nascent phagosome during apoptotic cell corpse engulfment."
FT /evidence="ECO:0000269|PubMed:21490059,
FT ECO:0000269|PubMed:22272187"
FT CONFLICT 734
FT /note="R -> P (in Ref. 1; AAB72228)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 830 AA; 93407 MW; FF681250E51AB8A5 CRC64;
MSWQNQGMQA LIPVINRVQD AFSQLGTSVS FELPQIAVVG GQSAGKSSVL ENFVGKDFLP
RGSGIVTRRP LILQLIQDRN EYAEFLHKKG HRFVDFDAVR KEIEDETDRV TGQNKGISPH
PINLRVFSPN VLNLTLIDLP GLTKVPVGDQ PADIEQQIRD MILTFINRET CLILAVTPAN
SDLATSDALK LAKEVDPQGL RTIGVLTKLD LMDEGTDARE ILENKLFTLR RGYVGVVNRG
QKDIVGRKDI RAALDAERKF FISHPSYRHM ADRLGTSYLQ HTLNQQLTNH IRDTLPTLRD
SLQKKMFAME KDVAEYKNYQ PNDPGRKTKA LLQMVTQFNA DIERSIEGSS AKLVSTNELS
GGARINRLFH ERFPFEIVKM EIDEKEMRKE IQYAIRNIHG IRVGLFTPDM AFEAIAKKQI
TRLKEPSLKC VDLVVNELAN VIRQCADTMA RYPRLRDELE RIVVSHMRER EQIAKQQIGL
IVDYELAYMN TNHEDFIGFS NAEAKASQGQ SAKKNLGNQV IRKGWLSLSN VSFVRGSKDN
WFVLMSDSLS WYKDDEEKEK KYMLPLDGVK LKDIEGGFMS RNHKFALFYP DGKNIYKDYK
QLELGCTNLD EIDAWKASFL RAGVYPEKQK AQEDESQQEM EDTSIDPQLE RQVETIRNLV
DSYMRIITKT IKDLVPKAVM HLIVNQTGEF MKDELLAHLY QCGDTDALME ESQIEAQKRE
EMLRMYHACK EALRIISEVN MSTLGDQPPP LPMSDYRPHP SGPSPVPRPA PAPPGGRQAP
MPPRGGPGAP PPPGMRPPPG APGGGGGMYP PLIPTRPGPG GPPPNMAPPR
