ID   UBCD4_DROME             Reviewed;         199 AA.
AC   P52486; P91633;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   09-NOV-2004, sequence version 2.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-22 kDa;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 4;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=Ubc4 {ECO:0000312|FlyBase:FBgn0015321}; Synonyms=UbcD4;
GN   ORFNames=CG8284 {ECO:0000312|FlyBase:FBgn0015321};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RPN10, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Canton-S, and Oregon-R;
RX   PubMed=11862484; DOI=10.1007/s00438-001-0623-8;
RA   Canning M., Kirby R., Finnegan D.;
RT   "UbcD4, a ubiquitin-conjugating enzyme in Drosophila melanogaster expressed
RT   in pole cells.";
RL   Mol. Genet. Genomics 266:907-913(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. {ECO:0000255|PROSITE-ProRule:PRU00388,
CC       ECO:0000269|PubMed:11862484}.
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, ECO:0000255|PROSITE-
CC         ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with Rpn10. {ECO:0000269|PubMed:11862484}.
CC   -!- INTERACTION:
CC       P52486; Q9VMY2: Dmel\CG14044; NbExp=4; IntAct=EBI-224571, EBI-185616;
CC       P52486; P55035: Rpn10; NbExp=2; IntAct=EBI-224571, EBI-146479;
CC   -!- TISSUE SPECIFICITY: During gastrulation, expression is highest in the
CC       invaginating posterior midgut primordium (PMG), high expression is also
CC       observed in the cephalic furrow and ventral ectodermal neurogenic
CC       region. In stage 10-11 embryos, expression is high in the pole cells
CC       present in the pocket formed by the PMG. During germ band retraction,
CC       expression appears to reinitiate in many tissues, especially the gut
CC       and nervous system. After dorsal closure, expression is detectable at
CC       low levels throughout the embryo. {ECO:0000269|PubMed:11862484}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Embryonic expression is highest at 0-8 hours.
CC       {ECO:0000269|PubMed:11862484}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; X92838; CAA63424.1; -; mRNA.
DR   EMBL; Y11349; CAA72184.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF50222.1; -; Genomic_DNA.
DR   EMBL; AY060381; AAL25420.1; -; mRNA.
DR   PIR; T08465; T08465.
DR   RefSeq; NP_001287013.1; NM_001300084.1.
DR   RefSeq; NP_001287014.1; NM_001300085.1.
DR   RefSeq; NP_524010.2; NM_079286.3.
DR   AlphaFoldDB; P52486; -.
DR   SMR; P52486; -.
DR   BioGRID; 64522; 12.
DR   DIP; DIP-20847N; -.
DR   IntAct; P52486; 10.
DR   STRING; 7227.FBpp0311673; -.
DR   PaxDb; 7227-FBpp0076124; -.
DR   DNASU; 39133; -.
DR   EnsemblMetazoa; FBtr0076395; FBpp0076124; FBgn0015321.
DR   EnsemblMetazoa; FBtr0345603; FBpp0311672; FBgn0015321.
DR   EnsemblMetazoa; FBtr0345604; FBpp0311673; FBgn0015321.
DR   GeneID; 39133; -.
DR   KEGG; dme:Dmel_CG8284; -.
DR   AGR; FB:FBgn0015321; -.
DR   CTD; 39133; -.
DR   FlyBase; FBgn0015321; Ubc4.
DR   VEuPathDB; VectorBase:FBgn0015321; -.
DR   eggNOG; KOG0418; Eukaryota.
DR   HOGENOM; CLU_030988_13_1_1; -.
DR   InParanoid; P52486; -.
DR   OMA; TGYFKGP; -.
DR   OrthoDB; 102270at2759; -.
DR   PhylomeDB; P52486; -.
DR   Reactome; R-DME-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 39133; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; eff; fly.
DR   GenomeRNAi; 39133; -.
DR   PRO; PR:P52486; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0015321; Expressed in egg cell and 23 other cell types or tissues.
DR   ExpressionAtlas; P52486; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0070628; F:proteasome binding; IPI:FlyBase.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:FlyBase.
DR   GO; GO:0061059; P:positive regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:FlyBase.
DR   CDD; cd14391; UBA_II_E2_UBCD4; 1.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR042614; UBCD4_UBA.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067:SF347; E2 UBIQUITIN-CONJUGATING ENZYME; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; P52486; DM.
PE   1: Evidence at protein level;
KW   ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..199
FT                   /note="Ubiquitin-conjugating enzyme E2-22 kDa"
FT                   /id="PRO_0000082522"
FT   DOMAIN          4..154
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   DOMAIN          161..199
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   ACT_SITE        92
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   CONFLICT        34..36
FT                   /note="DSW -> GQL (in Ref. 1; CAA63424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        73
FT                   /note="V -> A (in Ref. 1; CAA63424)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   199 AA;  22510 MW;  2875F9478632C630 CRC64;
     MANMAVSRIK REFKEVMRSE EIVQCSIKIE LVNDSWTELR GEIAGPPDTP YEGGKFVLEI
     KVPETYPFNP PKVRFITRIW HPNISSVTGA ICLDILKDNW AAAMTLRTVL LSLQALLAAA
     EPDDPQDAVV AYQFKDKYDL FLLTAKHWTN AYAGGPHTFP DCDSKIQRLR DMGIDEHEAR
     AVLSKENWNL EKATEGLFS
//