ID Q18965_CAEEL Unreviewed; 964 AA.
AC Q18965;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 3.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=Dynamin-like 120 kDa protein, mitochondrial {ECO:0000256|ARBA:ARBA00018307};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN Name=eat-3 {ECO:0000313|EMBL:CAA87771.3,
GN ECO:0000313|WormBase:D2013.5};
GN ORFNames=CELE_D2013.5 {ECO:0000313|EMBL:CAA87771.3}, D2013.5
GN {ECO:0000313|WormBase:D2013.5};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA87771.3, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA87771.3, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA87771.3,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 Evidence={ECO:0000256|ARBA:ARBA00001837};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004325}.
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DR EMBL; BX284602; CAA87771.3; -; Genomic_DNA.
DR RefSeq; NP_495986.3; NM_063585.7.
DR AlphaFoldDB; Q18965; -.
DR SMR; Q18965; -.
DR STRING; 6239.D2013.5.1; -.
DR EPD; Q18965; -.
DR PaxDb; 6239-D2013-5; -.
DR PeptideAtlas; Q18965; -.
DR EnsemblMetazoa; D2013.5.1; D2013.5.1; WBGene00001134.
DR GeneID; 174476; -.
DR KEGG; cel:CELE_D2013.5; -.
DR UCSC; D2013.5; c. elegans.
DR AGR; WB:WBGene00001134; -.
DR WormBase; D2013.5; CE42493; WBGene00001134; eat-3.
DR eggNOG; KOG0447; Eukaryota.
DR GeneTree; ENSGT00550000074851; -.
DR HOGENOM; CLU_012302_0_0_1; -.
DR InParanoid; Q18965; -.
DR OMA; ESQTDAF; -.
DR OrthoDB; 48011at2759; -.
DR PhylomeDB; Q18965; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001134; Expressed in adult organism and 4 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:WormBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:WormBase.
DR GO; GO:0035264; P:multicellular organism growth; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0000303; P:response to superoxide; IMP:WormBase.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR045817; OPA1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF67; DYNAMIN-LIKE 120 KDA PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF19434; OPA1_C; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 1: Evidence at protein level;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Proteomics identification {ECO:0007829|EPD:Q18965,
KW ECO:0007829|PeptideAtlas:Q18965};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 284..560
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT COILED 199..251
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 964 AA; 110254 MW; B79A7CD572C80B0C CRC64;
MRIATRRRFI SNNLHKFSRI SASTSATLAA YSNGNQHQNR QFGTNALFSK KGGLLQKRQT
VINLQSERAF IGIAASAARH LLKLRYFIAT GVIGGSVAAR TWYEEWKSNL PDLSLPEWFD
SNGSWNEFSQ KMKGIKDGFG ADGQNKWAEW MAKFEQFKQQ KEDQNGNSGG GGGGEGNVPV
KEPVILASLM SAFSSKKDEP EEKKDNVSAE ERIQKLQEEM LKTQSQYQRE LERLEKENKV
LKQRLLLSDD KAAIRLKRLK RSLIDMYSEV LDLLNEYDSS YNTSDNLPRV VVVGDQSAGK
TSVLEMVAQA RIFPRGSGEM MTRAPVKVTL SEGPYHVAQF RDSSREFDLT KETDLQQLRN
ETEVRMRNSV RDGKTVSNEV ISLTVKGPNL PRMVLVDLPG VISTVTADMA RETKDDIIRM
SKAHMENPNA IILCIQDGSV DAERSNVTDL VSSIDPSGKR TILVLTKVDM AEKNLANPDR
IKKILEGKLF PMKALGYFGV VTGRGNSSDS IDEIRKYEEN FFSTSQLLRD GVLKPSQMTT
RNMSLAVSDC FWRMVRDSIE SQTDAFRAAK FNLEAEWKNH FLRIRQLNRD ELYDKARGEI
LDEIVNLSLI GVEEWEKLLQ DKLWSGISSH VFDQILMPAY ASSSSGSFNT TVDIKLKHFA
DKQLAQKSIE TGWDTLKEVF FRQINQDART KKDHDPVFDA LKEAVIEEAM LTHGWDDKAM
DYLRVIQLNA MEDRAVQDKR SWDAACNFLH KAASERLAAV KKQLTDDRGP GWASKWLMWK
TPTADNHYSC VIQDELYSIL GADPEHKQAL TDDDITVIRR NIETKGVLEV PTESIRKQWK
LVFKKHFLER IINSSKDCLS MYQMYRQGMI EGQDIDCQTI VLFYRIQKMV NLTCNALRQQ
ITNTEHRRLE KEIKEVLDDW SQEPDIKKKY LTGRRVDLAE EIQQVRRIQE KLEEFMAQLQ
REKI
//