UBC25_CAEEL
ID UBC25_CAEEL Reviewed; 387 AA.
AC Q93571; Q86M58;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 25 {ECO:0000303|PubMed:12763049};
DE EC=2.3.2.23 {ECO:0000255};
DE AltName: Full=E2 ubiquitin-conjugating enzyme 25;
GN Name=ubc-25 {ECO:0000312|WormBase:F25H2.8};
GN ORFNames=F25H2.8 {ECO:0000312|WormBase:F25H2.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:CAB02096.2};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=12763049; DOI=10.1016/s0006-291x(03)00824-6;
RA Schulze E., Altmann M.E., Adham I.M., Schulze B., Frode S., Engel W.;
RT "The maintenance of neuromuscular function requires UBC-25 in
RT Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 305:691-699(2003).
RN [2]
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).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins (Potential). Required for the maintenance of neuromuscular
CC function (PubMed:12763049). {ECO:0000255|PROSITE-ProRule:PRU00388,
CC ECO:0000269|PubMed:12763049}.
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:0000255|PROSITE-ProRule:PRU00388};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12763049}. Nucleus
CC {ECO:0000269|PubMed:12763049}.
CC -!- TISSUE SPECIFICITY: In the embryo, expressed in precursor neuron and
CC muscle cells and in other cells such as hypodermal cells. After
CC hatching of L1 larvae and in all subsequent stages, strongest
CC expression in pharyngeal muscle and anal muscle cells. In L4 larvae and
CC adolescent hermaphrodites, also expressed in the vulval muscles.
CC Expression also detected in all four nerve cords and in neurons with
CC weaker levels in all body wall muscles. {ECO:0000269|PubMed:12763049}.
CC -!- DEVELOPMENTAL STAGE: Expression begins during gastrulation and
CC continues during all subsequent stages. {ECO:0000269|PubMed:12763049}.
CC -!- DISRUPTION PHENOTYPE: In males and hermaphrodites, late-onset paralysis
CC of muscular functions required for locomotion and defecation. In
CC addition, hermaphrodites show a progressive egg-laying defect,
CC resulting in intrauterine hatching and premature death. Vulva
CC protrusion is often observed with occasional rupture resulting in the
CC projection of internal organs. {ECO:0000269|PubMed:12763049}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AF537093; AAO85552.1; -; mRNA.
DR EMBL; Z79754; CAB02096.2; -; Genomic_DNA.
DR PIR; T21349; T21349.
DR RefSeq; NP_492764.2; NM_060363.3.
DR AlphaFoldDB; Q93571; -.
DR SMR; Q93571; -.
DR STRING; 6239.F25H2.8; -.
DR EPD; Q93571; -.
DR PaxDb; Q93571; -.
DR PeptideAtlas; Q93571; -.
DR EnsemblMetazoa; F25H2.8.1; F25H2.8.1; WBGene00006720.
DR GeneID; 172941; -.
DR KEGG; cel:CELE_F25H2.8; -.
DR UCSC; F25H2.8.1; c. elegans.
DR CTD; 172941; -.
DR WormBase; F25H2.8; CE34543; WBGene00006720; ubc-25.
DR eggNOG; KOG0897; Eukaryota.
DR GeneTree; ENSGT00940000170329; -.
DR HOGENOM; CLU_053863_0_0_1; -.
DR InParanoid; Q93571; -.
DR OMA; NIQENYP; -.
DR OrthoDB; 1214134at2759; -.
DR PhylomeDB; Q93571; -.
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:Q93571; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006720; Expressed in embryo and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..387
FT /note="Ubiquitin-conjugating enzyme E2 25"
FT /evidence="ECO:0000305"
FT /id="PRO_0000431420"
FT DOMAIN 214..380
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 117..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..164
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT CONFLICT 196
FT /note="V -> A (in Ref. 1; AAO85552)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="T -> S (in Ref. 1; AAO85552)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 44061 MW; BA09933EEB7BAF1D CRC64;
MACLRKLKED IQVLEKLFPK NHNRFQILSA SVDELSMKFI NAENKGIIVT ANIQENYPRQ
PPIWFSESDD VPVIGMSLQR LTETEESTNI LHQVHRLVSD LCSFYNLQMP CELPQIAPPV
RDDIDEGRGS DISDTTSEPI DDDMAGDGEV DDDDEEEEDD EDADGDIEIV EMAEEDPTSQ
HDVGVSKEGL DMLDKVSKIN RQQHLDGKVQ GSITATDRLM KEIRDIHRSE HFKNGIYTFE
LEKEENLYQW WIKLHKVDED SPLFEDMKKL KKDHNQDHLL FSFTFNEKFP CDPPFVRVVA
PHINQGFVLG GGAICMELLT KQGWSSAYSI ESCILQIAAT LVKGRARISF DAKHTSTYSM
ARAQQSFKSL QQIHAKSGWY TPPKTEG
