UB2V3_CAEEL
ID UB2V3_CAEEL Reviewed; 368 AA.
AC P91853;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 3 {ECO:0000312|WormBase:F26H9.7};
GN Name=uev-3 {ECO:0000312|WormBase:F26H9.7};
GN ORFNames=F26H9.7 {ECO:0000312|WormBase:F26H9.7};
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|EMBL:CAB04202.2, ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAB04202.2,
RC 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, INTERACTION WITH PMK-3, AND TISSUE SPECIFICITY.
RX PubMed=20592265; DOI=10.1534/genetics.110.117341;
RA Trujillo G., Nakata K., Yan D., Maruyama I.N., Jin Y.;
RT "A ubiquitin E2 variant protein acts in axon termination and synaptogenesis
RT in Caenorhabditis elegans.";
RL Genetics 186:135-145(2010).
RN [3] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26657059; DOI=10.1371/journal.pgen.1005733;
RA van der Vaart A., Rademakers S., Jansen G.;
RT "DLK-1/p38 MAP Kinase signaling controls cilium length by regulating RAB-5
RT mediated endocytosis in Caenorhabditis elegans.";
RL PLoS Genet. 11:E1005733-E1005733(2015).
CC -!- FUNCTION: Possible negative regulator of polyubiquitination (By
CC similarity). May modulate the activity of the p38 MAP kinase pnk-3
CC (PubMed:20592265). May have a role in axon termination and synaptic
CC transmission at motor and mechanosensory neurons (PubMed:20592265).
CC Plays a role in intraflagellar transport in cilia and cilium length
CC regulation (PubMed:26657059). {ECO:0000250|UniProtKB:Q8IX04,
CC ECO:0000269|PubMed:20592265, ECO:0000269|PubMed:26657059}.
CC -!- SUBUNIT: May interact with pmk-3. {ECO:0000269|PubMed:20592265}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26657059}. Cytoplasm
CC {ECO:0000269|PubMed:26657059}. Cell projection, dendrite
CC {ECO:0000269|PubMed:26657059}. Cell projection, axon
CC {ECO:0000269|PubMed:26657059}. Cell projection, cilium
CC {ECO:0000269|PubMed:26657059}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:20592265}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- CAUTION: Lacks the active site cysteine required for interaction with
CC ubiquitin. {ECO:0000305}.
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DR EMBL; BX284601; CAB04202.2; -; Genomic_DNA.
DR RefSeq; NP_492482.2; NM_060081.2.
DR AlphaFoldDB; P91853; -.
DR SMR; P91853; -.
DR STRING; 6239.F26H9.7; -.
DR EPD; P91853; -.
DR PaxDb; P91853; -.
DR EnsemblMetazoa; F26H9.7a.1; F26H9.7a.1; WBGene00006732.
DR UCSC; F26H9.7; c. elegans.
DR WormBase; F26H9.7; CE42102; WBGene00006732; uev-3.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_835680_0_0_1; -.
DR InParanoid; P91853; -.
DR OMA; LARENWE; -.
DR OrthoDB; 1541187at2759; -.
DR Reactome; R-CEL-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR SignaLink; P91853; -.
DR PRO; PR:P91853; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006732; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; P91853; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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..368
FT /note="Ubiquitin-conjugating enzyme E2 variant 3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436503"
FT DOMAIN 181..336
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 42784 MW; E054F3A8E536FCA9 CRC64;
MSDQPGTSRP PLRAEPTPTK SKCFSNQLNS KETATRRRAR PIAIPSDETP RNEVTFLRPS
EVPQRKPLPE YREPQPRKTV PKNVPLEDLH NYHREECLNV SIPHFINTED LIKESQRVNG
LISFRSTNFV DPSVILKEIK KKEEETVTLM DNDKNSIIDI VGDGINYEKL KKVEKSLCQI
DIITEFMNRS RHLQGKKVNG CIMRIDETKQ LLFHVIIDGP VGSIYEGGTF FADINIQPYQ
NHSLIPRVCF HTFIFHPNLG KYGNWDMRGI QWERRSNLEV LYNFIVEGMR NVKYDIERRN
LAQLEDMSQP NISRLAKEDW PKFERTAREF VMKMAGGTIN GRKTIFAETK KRRRQDFLDE
DIDVIGIS
