UB2V1_CAEEL
ID UB2V1_CAEEL Reviewed; 139 AA.
AC O45495;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 1 {ECO:0000312|WormBase:F39B2.2};
GN Name=uev-1 {ECO:0000312|WormBase:F39B2.2};
GN ORFNames=F39B2.2 {ECO:0000312|WormBase:F39B2.2};
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]
RP FUNCTION, AND INTERACTION WITH UBC-13.
RX PubMed=15530417; DOI=10.1016/j.bbrc.2004.10.047;
RA Gudgen M., Chandrasekaran A., Frazier T., Boyd L.;
RT "Interactions within the ubiquitin pathway of Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 325:479-486(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17663792; DOI=10.1186/1471-2121-8-32;
RA Howard R.A., Sharma P., Hajjar C., Caldwell K.A., Caldwell G.A.,
RA du Breuil R., Moore R., Boyd L.;
RT "Ubiquitin conjugating enzymes participate in polyglutamine protein
RT aggregation.";
RL BMC Cell Biol. 8:32-32(2007).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH UBC-13, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP PHE-8.
RX PubMed=21179194; DOI=10.1371/journal.pone.0014291;
RA Kramer L.B., Shim J., Previtera M.L., Isack N.R., Lee M.C., Firestein B.L.,
RA Rongo C.;
RT "UEV-1 is an ubiquitin-conjugating enzyme variant that regulates glutamate
RT receptor trafficking in C. elegans neurons.";
RL PLoS ONE 5:E14291-E14291(2010).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=22494772; DOI=10.1186/1471-2121-13-10;
RA Skibinski G.A., Boyd L.;
RT "Ubiquitination is involved in secondary growth, not initial formation of
RT polyglutamine protein aggregates in C. elegans.";
RL BMC Cell Biol. 13:10-10(2012).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24595290; DOI=10.1242/dev.103044;
RA Sato M., Konuma R., Sato K., Tomura K., Sato K.;
RT "Fertilization-induced K63-linked ubiquitylation mediates clearance of
RT maternal membrane proteins.";
RL Development 141:1324-1331(2014).
CC -!- FUNCTION: Involved in protein ubiquitination, but has no ubiquitin
CC ligase activity on its own (PubMed:15530417). The uev-1-ubc-13
CC heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin
CC chains that are linked through Lys-63 (PubMed:15530417,
CC PubMed:24595290). Involved in sorting Lys-63-linked polyubiquitinated
CC maternal membrane proteins for degradation by targeting to
CC multivesicular bodies (PubMed:24595290). Required for glr-1-containing
CC glutamate receptor trafficking in neurons (PubMed:21179194). May have a
CC role in synaptic transmission at motorneurons (PubMed:21179194). May be
CC involved in the ubiquitination and growth of intracellular
CC polyglutamine protein aggregates (PubMed:17663792, PubMed:22494772).
CC {ECO:0000269|PubMed:15530417, ECO:0000269|PubMed:17663792,
CC ECO:0000269|PubMed:21179194, ECO:0000269|PubMed:22494772,
CC ECO:0000269|PubMed:24595290}.
CC -!- SUBUNIT: Heterodimer with ubc-13. {ECO:0000269|PubMed:15530417,
CC ECO:0000269|PubMed:21179194}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21179194}.
CC Nucleus {ECO:0000269|PubMed:21179194}. Cell projection, dendrite
CC {ECO:0000269|PubMed:21179194}. Perikaryon
CC {ECO:0000269|PubMed:21179194}.
CC -!- TISSUE SPECIFICITY: Expressed in the pharynx, body wall muscle cells,
CC vulval epithelia, distal tip cell, intestine, tail, head neurons and
CC ventral cord motorneurons. {ECO:0000269|PubMed:21179194}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryo to adulthood.
CC {ECO:0000269|PubMed:21179194}.
CC -!- DISRUPTION PHENOTYPE: Temperature sensitive with partial embryonic
CC lethality at 25 degrees Celsius (PubMed:24595290). Inhibited
CC degradation of maternal membrane proteins, cav-1, chs-1 and rme-2, and
CC ubiquitination of cav-1 with accumulation of these proteins on the
CC maternal plasma membrane and endosome-like vesicles in later-stage
CC embryos (PubMed:24595290). Locomotion defect with animals displaying
CC increased body flexing (PubMed:21179194). Mis-localized glr-1-
CC containing glutamate receptor with increased glr-1 accumulation in the
CC ventral nerve cord (PubMed:21179194). Reduced and irregular snb-1
CC accumulation at neuromuscular junctions (PubMed:21179194). RNAi-
CC mediated knockdown prevents localization of ubiquitin and proteasomes
CC to polyglutamine protein aggregates (PubMed:17663792). Reduced size of
CC polyglutamine protein aggregates (PubMed:17663792). Inhibited
CC degradation of the maternal membrane protein, cav-1 in embryos
CC (PubMed:24595290). {ECO:0000269|PubMed:17663792,
CC ECO:0000269|PubMed:21179194, ECO:0000269|PubMed:24595290}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- CAUTION: Has no ubiquitin ligase activity on its own; may require
CC ubiquitin-conjugating enzyme, ubc-13. {ECO:0000269|PubMed:15530417}.
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DR EMBL; BX284601; CAB07383.1; -; Genomic_DNA.
DR PIR; T21984; T21984.
DR RefSeq; NP_493578.1; NM_061177.5.
DR AlphaFoldDB; O45495; -.
DR SMR; O45495; -.
DR ComplexPortal; CPX-4625; ubc-13-uev-1 ubiquitin-conjugating enzyme E2 complex.
DR IntAct; O45495; 8.
DR MINT; O45495; -.
DR STRING; 6239.F39B2.2.1; -.
DR EPD; O45495; -.
DR PaxDb; O45495; -.
DR PeptideAtlas; O45495; -.
DR EnsemblMetazoa; F39B2.2.1; F39B2.2.1; WBGene00006730.
DR GeneID; 173347; -.
DR KEGG; cel:CELE_F39B2.2; -.
DR UCSC; F39B2.2.1; c. elegans.
DR CTD; 173347; -.
DR WormBase; F39B2.2; CE16008; WBGene00006730; uev-1.
DR eggNOG; KOG0896; Eukaryota.
DR GeneTree; ENSGT00740000115534; -.
DR HOGENOM; CLU_063065_3_0_1; -.
DR InParanoid; O45495; -.
DR OMA; NLPCVDQ; -.
DR OrthoDB; 1507995at2759; -.
DR PhylomeDB; O45495; -.
DR Reactome; R-CEL-9020702; Interleukin-1 signaling.
DR Reactome; R-CEL-9646399; Aggrephagy.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:O45495; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006730; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0035370; C:UBC13-UEV1A complex; IPI:ComplexPortal.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:WormBase.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IC:ComplexPortal.
DR GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; IC:ComplexPortal.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0090325; P:regulation of locomotion involved in locomotory behavior; IMP:WormBase.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:WormBase.
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 Cell projection; Cytoplasm; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..139
FT /note="Ubiquitin-conjugating enzyme E2 variant 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434946"
FT DOMAIN 5..139
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MUTAGEN 8
FT /note="F->A: Does not bind to ubc-13."
FT /evidence="ECO:0000269|PubMed:21179194"
SQ SEQUENCE 139 AA; 15921 MW; 1D2F86FFAE6CC1F0 CRC64;
MVDVPRNFRL LEELEEGQKG KGDGNISWGL EDDSDMTLTR WTASIIGPPR TPYESRIYNL
QIQCGGNYPR EPPTVRFTTK VHMVGVNQSN GVIDKRNLTT LRNWSNSYMI KTVLEDIRKN
MMMAKENLKL QQPAEGAMF
