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   27-MAR-2024, entry version 156.
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};
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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.P42746; -.
DR   PaxDb; 3702-AT5G62540-1; -.
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; AT5G62540; UBC3.
DR   eggNOG; KOG0419; Eukaryota.
DR   HOGENOM; CLU_030988_10_2_1; -.
DR   InParanoid; P42746; -.
DR   OMA; QASIMWP; -.
DR   OrthoDB; 5478564at2759; -.
DR   PhylomeDB; P42746; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:P42746; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P42746; baseline and differential.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
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; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF369; UBIQUITIN-CONJUGATING ENZYME E2 3; 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; P42746; AT.
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
//