UBC18_CAEEL
ID UBC18_CAEEL Reviewed; 153 AA.
AC Q21633;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 ubc-18 {ECO:0000305};
DE EC=2.3.2.23 {ECO:0000269|PubMed:19553937};
GN Name=ubc-18 {ECO:0000312|WormBase:R01H2.6};
GN ORFNames=R01H2.6 {ECO:0000312|WormBase:R01H2.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-10.
RX PubMed=12783801; DOI=10.1242/dev.00561;
RA Fay D.S., Large E., Han M., Darland M.;
RT "lin-35/Rb and ubc-18, an E2 ubiquitin-conjugating enzyme, function
RT redundantly to control pharyngeal morphogenesis in C. elegans.";
RL Development 130:3319-3330(2003).
RN [3] {ECO:0000305}
RP INTERACTION WITH ARI-1.1.
RX PubMed=16457801; DOI=10.1016/j.ydbio.2005.11.045;
RA Qiu X., Fay D.S.;
RT "ARI-1, an RBR family ubiquitin-ligase, functions with UBC-18 to regulate
RT pharyngeal development in C. elegans.";
RL Dev. Biol. 291:239-252(2006).
RN [4] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH WWP-1, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-10.
RX PubMed=19553937; DOI=10.1038/nature08130;
RA Carrano A.C., Liu Z., Dillin A., Hunter T.;
RT "A conserved ubiquitination pathway determines longevity in response to
RT diet restriction.";
RL Nature 460:396-399(2009).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19521497; DOI=10.1371/journal.pgen.1000510;
RA Mani K., Fay D.S.;
RT "A mechanistic basis for the coordinated regulation of pharyngeal
RT morphogenesis in Caenorhabditis elegans by LIN-35/Rb and UBC-18-ARI-1.";
RL PLoS Genet. 5:E1000510-E1000510(2009).
CC -!- FUNCTION: Ubiquitin-conjugating enzyme E2 (PubMed:19553937). Accepts
CC ubiquitin from the E1 complex and catalyzes its covalent attachment to
CC other proteins (PubMed:19553937). Required for diet restriction-
CC mediated lifespan extension, probably acting as part of a complex with
CC ubiquitin-protein ligase wwp-1 (PubMed:19553937). Acts redundantly with
CC lin-35/Rb in the regulation of pharyngeal morphogenesis during
CC embryonic development by negatively regulating the expression of
CC proteins such as sup-35 (PubMed:12783801, PubMed:19521497).
CC {ECO:0000269|PubMed:12783801, ECO:0000269|PubMed:19521497,
CC ECO:0000269|PubMed:19553937}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000269|PubMed:19553937};
CC -!- SUBUNIT: Interacts with E3 ubiquitin-protein ligase wwp-1
CC (PubMed:19553937). Interacts with RBR-type E3 ubiquitin transferase
CC ari-1.1 (PubMed:16457801). {ECO:0000269|PubMed:16457801,
CC ECO:0000269|PubMed:19553937}.
CC -!- INTERACTION:
CC Q21633; Q9N2Z7: wwp-1; NbExp=3; IntAct=EBI-325980, EBI-317369;
CC -!- TISSUE SPECIFICITY: Expressed in neurons localized in the head and tail
CC of adults. {ECO:0000269|PubMed:19553937}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown very slightly reduces
CC viability and brood size; phenotype is exacerbated on a mutant
CC background which enhances the overall efficacy of RNAi
CC (PubMed:12783801). Increases sensitivity to paraquat and reduces
CC lifespan at 25 degrees Celsius, but not at 20 degrees Celsius
CC (PubMed:19553937). Abolishes lifespan extension completely on an eat-2
CC mutant background (PubMed:19553937). Substantially increases embryonic
CC expression of sup-35 (PubMed:19521497). {ECO:0000269|PubMed:12783801,
CC ECO:0000269|PubMed:19521497, ECO:0000269|PubMed:19553937}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; BX284603; CCD69287.1; -; Genomic_DNA.
DR PIR; T16646; T16646.
DR RefSeq; NP_498541.1; NM_066140.4.
DR AlphaFoldDB; Q21633; -.
DR SMR; Q21633; -.
DR DIP; DIP-26820N; -.
DR IntAct; Q21633; 6.
DR STRING; 6239.R01H2.6; -.
DR EPD; Q21633; -.
DR PaxDb; Q21633; -.
DR PeptideAtlas; Q21633; -.
DR EnsemblMetazoa; R01H2.6.1; R01H2.6.1; WBGene00006713.
DR GeneID; 175985; -.
DR KEGG; cel:CELE_R01H2.6; -.
DR UCSC; R01H2.6; c. elegans.
DR CTD; 175985; -.
DR WormBase; R01H2.6; CE25067; WBGene00006713; ubc-18.
DR eggNOG; KOG0422; Eukaryota.
DR GeneTree; ENSGT00940000165322; -.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; Q21633; -.
DR OMA; EHTKKHA; -.
DR OrthoDB; 1420213at2759; -.
DR PhylomeDB; Q21633; -.
DR BRENDA; 2.3.2.23; 1045.
DR Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
DR Reactome; R-CEL-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q21633; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006713; Expressed in embryo and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:WormBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:WormBase.
DR GO; GO:0009887; P:animal organ morphogenesis; IGI:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:WormBase.
DR GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; IMP:WormBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:WormBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:WormBase.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..153
FT /note="Ubiquitin-conjugating enzyme E2 ubc-18"
FT /id="PRO_0000452645"
FT DOMAIN 2..149
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 86
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MUTAGEN 10
FT /note="E->K: In ku354; drastically reduces wwp-1-dependent
FT ubiquitin ligase activity. Marked reduction in brood size.
FT On a lin-35 mutant background, 4% of larvae display a Pun
FT (pharyngeal unattached) phenotype, whereby the pharynx
FT fails to elongate and form an attachment to the anterior
FT alimentary opening or buccal cavity. Increases to 40% Pun
FT phenotype animals on a lin-35 mutant background combined
FT with RNAi-mediated knockdown."
FT /evidence="ECO:0000269|PubMed:12783801,
FT ECO:0000269|PubMed:19553937"
SQ SEQUENCE 153 AA; 17653 MW; 8F47141C578F4271 CRC64;
MSATRRLQKE LGDLKNCGVK AYENVECEET NLLKWTVLLI PDKEPYNKGA FKVGITFPVD
YPFKPPKVAF ETKIYHPNVD EEGKFCLPIV TAENWKPATK TEQVMMALLS LINEPEPSHP
IRADVAEEFQ KDHKKFMKTA EEHTRKHAEK RPE
