UniProt: Q18965

Database: UniProt
Entry: Q18965_CAEEL

LinkDB:  Q18965_CAEEL 
Original site:  Q18965_CAEEL

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Ontology (16)   
   GO (16)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   WORMBASE (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (33)   

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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
//

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