UBC3_ARATH
ID UBC3_ARATH Reviewed; 150 AA.
AC P42746; Q4TZ06; Q8H1P1; Q94AD2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 3;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 3;
DE AltName: Full=Ubiquitin carrier protein 3;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 3;
DE AltName: Full=Ubiquitin-protein ligase 3;
GN Name=UBC3; OrderedLocusNames=At5g62540; ORFNames=K19B1.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia; TISSUE=Green leaf;
RX PubMed=8155884; DOI=10.1007/bf00023561;
RA Sullivan M.L., Carpenter T.B., Vierstra R.D.;
RT "Homologues of wheat ubiquitin-conjugating enzymes -- TaUBC1 and TaUBC4 are
RT encoded by small multigene families in Arabidopsis thaliana.";
RL Plant Mol. Biol. 24:651-661(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=16339806; DOI=10.1104/pp.105.067983;
RA Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W.,
RA Callis J.;
RT "Genome analysis and functional characterization of the E2 and RING-type E3
RT ligase ubiquitination enzymes of Arabidopsis.";
RL Plant Physiol. 139:1597-1611(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=8790283; DOI=10.1007/bf00042223;
RA Thoma S., Sullivan M.L., Vierstra R.D.;
RT "Members of two gene families encoding ubiquitin-conjugating enzymes,
RT AtUBC1-3 and AtUBC4-6, from Arabidopsis thaliana are differentially
RT expressed.";
RL Plant Mol. Biol. 31:493-505(1996).
CC -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. {ECO:0000269|PubMed:16339806}.
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 -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Lower levels
CC found in leaves. {ECO:0000269|PubMed:8790283}.
CC -!- INDUCTION: Up-regulated by syringolin, a cell death-inducing chemical,
CC but not induced by heat shock. {ECO:0000269|PubMed:16339806,
CC ECO:0000269|PubMed:8790283}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK82529.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN28744.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L19352; AAA32898.1; -; Genomic_DNA.
DR EMBL; DQ027018; AAY44844.1; -; mRNA.
DR EMBL; AB015469; BAB11504.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97620.1; -; Genomic_DNA.
DR EMBL; AY039851; AAK63955.1; -; mRNA.
DR EMBL; AY143805; AAN28744.1; ALT_SEQ; mRNA.
DR EMBL; AY048267; AAK82529.1; ALT_SEQ; mRNA.
DR EMBL; AY085367; AAM62597.1; -; mRNA.
DR PIR; S43782; S43782.
DR RefSeq; NP_568956.1; NM_125648.3.
DR AlphaFoldDB; P42746; -.
DR SMR; P42746; -.
DR STRING; 3702.AT5G62540.1; -.
DR PaxDb; P42746; -.
DR PRIDE; P42746; -.
DR ProteomicsDB; 228523; -.
DR EnsemblPlants; AT5G62540.1; AT5G62540.1; AT5G62540.
DR GeneID; 836374; -.
DR Gramene; AT5G62540.1; AT5G62540.1; AT5G62540.
DR KEGG; ath:AT5G62540; -.
DR Araport; AT5G62540; -.
DR TAIR; locus:2154104; AT5G62540.
DR eggNOG; KOG0419; Eukaryota.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; P42746; -.
DR OMA; QNMWSPS; -.
DR OrthoDB; 1292821at2759; -.
DR PhylomeDB; P42746; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P42746; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P42746; baseline and differential.
DR Genevisible; P42746; AT.
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:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0016574; P:histone ubiquitination; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..150
FT /note="Ubiquitin-conjugating enzyme E2 3"
FT /id="PRO_0000082572"
FT DOMAIN 4..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 88
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CONFLICT 13
FT /note="F -> L (in Ref. 5; AAK82529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 150 AA; 17137 MW; 993FE149D541F2AA CRC64;
MTTPAKKRLM WDFKRLQKDP PVGISGAPQD NNIMHWNALI FGPEDTPWDG GTFKLTLHFT
EDYPNKPPIV RFVSRMFHPN IYADGSICLD ILQNQWSPIY DVAAVLTSIQ SLLCDPNPDS
PANAEAARLF SENKREYNRK VIEIVEQSYV
