ID   UBCD1_DROME             Reviewed;         147 AA.
AC   P25867; Q9VFG6;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   27-MAR-2024, entry version 202.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2-17 kDa;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme D1;
DE   AltName: Full=Protein effete;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=eff; Synonyms=UbcD1; ORFNames=CG7425;
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].
RC   STRAIN=Oregon-P2;
RX   PubMed=1310935; DOI=10.1002/j.1460-2075.1992.tb05059.x;
RA   Treier M., Seufert W., Jentsch S.;
RT   "Drosophila UbcD1 encodes a highly conserved ubiquitin-conjugating enzyme
RT   involved in selective protein degradation.";
RL   EMBO J. 11:367-372(1992).
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=Head;
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).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-11, AND FUNCTION.
RX   PubMed=9106658; DOI=10.1101/gad.11.7.863;
RA   Cenci G., Rawson R.B., Belloni G., Castrillon D.H., Tudor M., Petrucci R.,
RA   Goldberg M.L., Wasserman S.A., Gatti M.;
RT   "UbcD1, a Drosophila ubiquitin-conjugating enzyme required for proper
RT   telomere behavior.";
RL   Genes Dev. 11:863-875(1997).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Mediates the selective degradation of short-lived and
CC       abnormal proteins. Required for proper telomere behavior during cell
CC       divisions and possibly for ubiquitination of proteins involved in
CC       postmeiotic stages of spermatogenesis. Deletion mutations are lethal in
CC       homozygotes. {ECO:0000255|PROSITE-ProRule:PRU00388,
CC       ECO:0000269|PubMed:9106658}.
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   -!- INTERACTION:
CC       P25867; A1Z9I6: anon-EST:GressD1; NbExp=3; IntAct=EBI-196394, EBI-91747;
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; X62575; CAA44453.1; -; mRNA.
DR   EMBL; AE014297; AAF55093.1; -; Genomic_DNA.
DR   EMBL; AY060304; AAL25343.1; -; mRNA.
DR   EMBL; U68298; AAB39622.1; -; mRNA.
DR   PIR; S19157; S19157.
DR   RefSeq; NP_001262578.1; NM_001275649.1.
DR   RefSeq; NP_001262579.1; NM_001275650.1.
DR   RefSeq; NP_731941.1; NM_169601.2.
DR   AlphaFoldDB; P25867; -.
DR   SMR; P25867; -.
DR   BioGRID; 66859; 38.
DR   DIP; DIP-18953N; -.
DR   IntAct; P25867; 11.
DR   STRING; 7227.FBpp0082477; -.
DR   PaxDb; 7227-FBpp0082477; -.
DR   DNASU; 41785; -.
DR   EnsemblMetazoa; FBtr0083018; FBpp0082477; FBgn0011217.
DR   EnsemblMetazoa; FBtr0310554; FBpp0302691; FBgn0011217.
DR   EnsemblMetazoa; FBtr0336876; FBpp0307824; FBgn0011217.
DR   GeneID; 41785; -.
DR   KEGG; dme:Dmel_CG7425; -.
DR   AGR; FB:FBgn0011217; -.
DR   CTD; 41785; -.
DR   FlyBase; FBgn0011217; eff.
DR   VEuPathDB; VectorBase:FBgn0011217; -.
DR   eggNOG; KOG0417; Eukaryota.
DR   GeneTree; ENSGT00940000155109; -.
DR   HOGENOM; CLU_030988_13_3_1; -.
DR   InParanoid; P25867; -.
DR   OMA; PNIASMY; -.
DR   OrthoDB; 5478564at2759; -.
DR   PhylomeDB; P25867; -.
DR   Reactome; R-DME-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-DME-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-DME-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-DME-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-DME-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-DME-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-DME-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-DME-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-DME-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-DME-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR   Reactome; R-DME-176412; Phosphorylation of the APC/C.
DR   Reactome; R-DME-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-DME-201451; Signaling by BMP.
DR   Reactome; R-DME-202424; Downstream TCR signaling.
DR   Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR   Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
DR   Reactome; R-DME-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-DME-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-DME-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-DME-5357905; Regulation of TNFR1 signaling.
DR   Reactome; R-DME-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-DME-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-DME-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-DME-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-DME-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-DME-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-DME-8951664; Neddylation.
DR   Reactome; R-DME-9033241; Peroxisomal protein import.
DR   Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; P25867; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 41785; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; eff; fly.
DR   GenomeRNAi; 41785; -.
DR   PRO; PR:P25867; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0011217; Expressed in mouthpart and 29 other cell types or tissues.
DR   ExpressionAtlas; P25867; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:FlyBase.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:FlyBase.
DR   GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
DR   GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR   GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IMP:FlyBase.
DR   GO; GO:0048132; P:female germ-line stem cell asymmetric division; IMP:FlyBase.
DR   GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR   GO; GO:0007140; P:male meiotic nuclear division; IMP:FlyBase.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:FlyBase.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR   GO; GO:0016322; P:neuron remodeling; IDA:FlyBase.
DR   GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR   GO; GO:0097039; P:protein linear polyubiquitination; IDA:FlyBase.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:FlyBase.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR   GO; GO:0031647; P:regulation of protein stability; IMP:FlyBase.
DR   GO; GO:0045676; P:regulation of R7 cell differentiation; IGI:FlyBase.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24068:SF74; UBIQUITIN-CONJUGATING ENZYME E2-17 KDA; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; P25867; DM.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Meiosis; Nucleotide-binding;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..147
FT                   /note="Ubiquitin-conjugating enzyme E2-17 kDa"
FT                   /id="PRO_0000082519"
FT   DOMAIN          1..147
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        85
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   147 AA;  16678 MW;  82E0CE24F925E2EE CRC64;
     MALKRINKEL QDLGRDPPAQ CSAGPVGDDL FHWQATIMGP PDSPYQGGVF FLTIHFPTDY
     PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV
     PEIARIYKTD REKYNELARE WTRKYAM
//