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 27-MAR-2024, entry version 189. 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; G5ECK4: dnbp-1; NbExp=4; IntAct=EBI-317945, EBI-6533538; 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 39. DR IntAct; P39055; 19. DR MINT; P39055; -. DR STRING; 6239.C02C6.1b.1; -. DR EPD; P39055; -. DR PaxDb; 6239-C02C6-1b; -. DR PeptideAtlas; 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 AGR; WB:WBGene00001130; -. 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; 1052588at2759; -. 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-3928665; EPH-ephrin mediated repulsion of cells. 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 cell types or 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: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:0070266; P:necroptotic process; IGI:WormBase. DR GO; GO:0090386; P:phagosome maturation involved in apoptotic cell clearance; IMP:WormBase. DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:WormBase. DR CDD; cd08771; DLP_1; 1. DR CDD; cd01256; PH_dynamin; 1. DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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 InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR PANTHER; PTHR11566; DYNAMIN; 1. DR PANTHER; PTHR11566:SF212; DYNAMIN; 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; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50729; PH domain-like; 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 //