ID   UBC7_ARATH              Reviewed;         166 AA.
AC   Q42540; F4KHV0; Q8RXQ3;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 7;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 7;
DE   AltName: Full=Ubiquitin carrier protein 7;
DE   AltName: Full=Ubiquitin-protein ligase 7;
GN   Name=UBC7; OrderedLocusNames=At5g59300; ORFNames=MNC17.21;
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], AND FUNCTION.
RC   STRAIN=cv. Columbia; TISSUE=Seedling;
RX   PubMed=8647807; DOI=10.1074/jbc.271.21.12150;
RA   van Nocker S., Walker J.M., Vierstra R.D.;
RT   "The Arabidopsis thaliana UBC7/13/14 genes encode a family of
RT   multiubiquitin chain-forming E2 enzymes.";
RL   J. Biol. Chem. 271:12150-12158(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
RN   [3]
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   [4]
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   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. Involved in the formation of
CC       multiubiquitin chains. Signal the protein for selective degradation.
CC       {ECO:0000269|PubMed:8647807}.
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   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL86003.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAO64200.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U33757; AAC49321.1; -; Genomic_DNA.
DR   EMBL; AB016890; BAB09775.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97168.2; -; Genomic_DNA.
DR   EMBL; AY080733; AAL86003.1; ALT_INIT; mRNA.
DR   EMBL; BT005798; AAO64200.1; ALT_INIT; mRNA.
DR   PIR; S71209; S71209.
DR   RefSeq; NP_568902.3; NM_125320.3.
DR   AlphaFoldDB; Q42540; -.
DR   SMR; Q42540; -.
DR   BioGRID; 21292; 1.
DR   STRING; 3702.Q42540; -.
DR   iPTMnet; Q42540; -.
DR   PaxDb; 3702-AT5G59300-1; -.
DR   ProteomicsDB; 228693; -.
DR   EnsemblPlants; AT5G59300.1; AT5G59300.1; AT5G59300.
DR   GeneID; 836048; -.
DR   Gramene; AT5G59300.1; AT5G59300.1; AT5G59300.
DR   KEGG; ath:AT5G59300; -.
DR   Araport; AT5G59300; -.
DR   TAIR; AT5G59300; UBC7.
DR   eggNOG; KOG0425; Eukaryota.
DR   HOGENOM; CLU_030988_10_1_1; -.
DR   InParanoid; Q42540; -.
DR   OMA; MFEWEVM; -.
DR   OrthoDB; 149628at2759; -.
DR   PhylomeDB; Q42540; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q42540; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q42540; baseline and differential.
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:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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:SF298; UBIQUITIN-CONJUGATING ENZYME E2 13-RELATED; 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; Q42540; AT.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Nucleotide-binding; Reference proteome;
KW   Transferase; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..166
FT                   /note="Ubiquitin-conjugating enzyme E2 7"
FT                   /id="PRO_0000082586"
FT   DOMAIN          4..164
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        89
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   166 AA;  18722 MW;  967EF672ADBD6891 CRC64;
     MASQASLLLQ KQLKDLCKHP VDGFSAGLVD EKNIFEWSVT IIGPPDTLYE GGFFNAIMTF
     PQNYPNSPPT VRFTSDMWHP NVYSDGRVCI SILHPPGDDP SGYELASERW TPVHTVESIM
     LSIISMLSGP NDESPANVEA AKEWRDKRDE FKKKVSRCVR KSQEMF
//