UBE2W_CAEEL
ID UBE2W_CAEEL Reviewed; 152 AA.
AC Q9XWF6;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 W {ECO:0000305};
DE EC=2.3.2.23 {ECO:0000250|UniProtKB:Q96B02};
DE AltName: Full=E2 ubiquitin-conjugating enzyme W {ECO:0000305};
DE AltName: Full=N-terminal E2 ubiquitin-conjugating enzyme {ECO:0000305};
DE EC=2.3.2.25 {ECO:0000250|UniProtKB:Q96B02};
DE AltName: Full=N-terminus-conjugating E2 {ECO:0000305};
DE AltName: Full=Ubiquitin carrier protein W {ECO:0000305};
DE AltName: Full=Ubiquitin-conjugating enzyme 16 {ECO:0000312|WormBase:Y54E5B.4};
DE AltName: Full=Ubiquitin-protein ligase W {ECO:0000305};
GN Name=ubc-16 {ECO:0000312|WormBase:Y54E5B.4};
GN ORFNames=Y54E5B.4 {ECO:0000312|WormBase:Y54E5B.4};
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, AND DISRUPTION PHENOTYPE.
RX PubMed=31153831; DOI=10.1016/j.ydbio.2019.05.015;
RA Molina P., Lim Y., Boyd L.;
RT "Ubiquitination is required for the initial removal of paternal organelles
RT in C. elegans.";
RL Dev. Biol. 453:168-179(2019).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins (By similarity). Together with
CC ubc-18, required for the ubiquitination of membranous organelles, and
CC the removal of paternal mitochondria from early embryos
CC (PubMed:31153831). {ECO:0000250|UniProtKB:Q96B02,
CC ECO:0000269|PubMed:31153831}.
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:0000250|UniProtKB:Q96B02};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating
CC enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein].;
CC EC=2.3.2.25; Evidence={ECO:0000250|UniProtKB:Q96B02};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown does not alter the
CC ubiquitination of membranous organelles (MOs) or the number of MOs
CC (PubMed:31153831). Double RNAi-mediated knockdown together with ubc-18
CC reduces the ubiquitination of MOs (PubMed:31153831). Double knockdown
CC also reduces the number of lgg-1-positive autophagosome vesicles in
CC embryos (PubMed:31153831). {ECO:0000269|PubMed:31153831}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; BX284601; CAA21716.1; -; Genomic_DNA.
DR PIR; T27167; T27167.
DR RefSeq; NP_493587.1; NM_061186.4.
DR AlphaFoldDB; Q9XWF6; -.
DR SMR; Q9XWF6; -.
DR STRING; 6239.Y54E5B.4; -.
DR EPD; Q9XWF6; -.
DR PaxDb; Q9XWF6; -.
DR PeptideAtlas; Q9XWF6; -.
DR EnsemblMetazoa; Y54E5B.4.1; Y54E5B.4.1; WBGene00006711.
DR GeneID; 173354; -.
DR KEGG; cel:CELE_Y54E5B.4; -.
DR UCSC; Y54E5B.4; c. elegans.
DR CTD; 173354; -.
DR WormBase; Y54E5B.4; CE19228; WBGene00006711; ubc-16.
DR eggNOG; KOG0427; Eukaryota.
DR GeneTree; ENSGT00940000156908; -.
DR HOGENOM; CLU_030988_15_1_1; -.
DR InParanoid; Q9XWF6; -.
DR OMA; YNTQRPR; -.
DR OrthoDB; 1522577at2759; -.
DR PhylomeDB; Q9XWF6; -.
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 UniPathway; UPA00143; -.
DR PRO; PR:Q9XWF6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006711; Expressed in embryo and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IGI:UniProtKB.
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 3: Inferred from homology;
KW Ligase; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..152
FT /note="Ubiquitin-conjugating enzyme E2 W"
FT /id="PRO_0000448278"
FT DOMAIN 4..152
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 92
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT CROSSLNK 1
FT /note="Peptide (Met-Gly) (interchain with G-Cter in
FT ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q96B02"
SQ SEQUENCE 152 AA; 16936 MW; 228649EE08FF8C05 CRC64;
MSDAATRRLM KELAQLKSEA PEGLLVDNTS TSNDLKQWKI GVVGAEGTLY AGEVFMLQFT
FGPQYPFNSP EVMFVGETIP AHPHIYSNGH ICLSILSDDW TPALSVQSVC LSILSMLSSS
KEKKHPIDDA IYVRTCSKNP SKTRWWFHDD SV
