ID   UBC32_ARATH             Reviewed;         309 AA.
AC   Q9LSP7; Q4TYX9;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 32;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 32;
DE   AltName: Full=Ubiquitin carrier protein 32;
GN   Name=UBC32; OrderedLocusNames=At3g17000; ORFNames=K14A17.7;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-273, TISSUE SPECIFICITY, 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).
CC   -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. {ECO:0000250|UniProtKB:P42743}.
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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AB026636; BAA94978.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75893.1; -; Genomic_DNA.
DR   EMBL; AF386935; AAK62380.1; -; mRNA.
DR   EMBL; BT020530; AAW52556.1; -; mRNA.
DR   EMBL; DQ027045; AAY44871.1; -; mRNA.
DR   RefSeq; NP_566563.1; NM_112576.3.
DR   AlphaFoldDB; Q9LSP7; -.
DR   SMR; Q9LSP7; -.
DR   BioGRID; 6289; 244.
DR   IntAct; Q9LSP7; 244.
DR   STRING; 3702.Q9LSP7; -.
DR   TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR   PaxDb; 3702-AT3G17000-1; -.
DR   ProteomicsDB; 228596; -.
DR   EnsemblPlants; AT3G17000.1; AT3G17000.1; AT3G17000.
DR   GeneID; 820956; -.
DR   Gramene; AT3G17000.1; AT3G17000.1; AT3G17000.
DR   KEGG; ath:AT3G17000; -.
DR   Araport; AT3G17000; -.
DR   TAIR; AT3G17000; UBC32.
DR   eggNOG; KOG0428; Eukaryota.
DR   HOGENOM; CLU_041481_0_0_1; -.
DR   InParanoid; Q9LSP7; -.
DR   OMA; CGCSHAD; -.
DR   OrthoDB; 180749at2759; -.
DR   PhylomeDB; Q9LSP7; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9LSP7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LSP7; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0016020; C:membrane; IDA:TAIR.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:TAIR.
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:0042631; P:cellular response to water deprivation; IGI:TAIR.
DR   GO; GO:1902457; P:negative regulation of stomatal opening; IGI: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; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067:SF257; UBC CORE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50127; UBC_2; 1.
DR   Genevisible; Q9LSP7; AT.
PE   2: Evidence at transcript level;
KW   ATP-binding; Membrane; Nucleotide-binding; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix; Ubl conjugation pathway.
FT   CHAIN           1..309
FT                   /note="Ubiquitin-conjugating enzyme E2 32"
FT                   /id="PRO_0000345197"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          11..166
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        93
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ   SEQUENCE   309 AA;  34322 MW;  B4C77186E1294D51 CRC64;
     MADERYNRKN PAVKRILQEV KEMQANPSDD FMSLPLEENI FEWQFAIRGP GDTEFEGGIY
     HGRIQLPADY PFKPPSFMLL TPNGRFETNT KICLSISNYH PEHWQPSWSV RTALVALIAF
     MPTSPNGALG SVDYPKDERR TLAIKSRETP PKYGSPERQK IIDEIHQYIL SKATVVPKPL
     PLECSQAPSI VSEAHSQVEP QEAITVVEER SIATTDTIVD DQIIEETAEA VNTAASVVPA
     AAPLPAVEVV VKASVSGEQR MARRAAQKPV DDRLFTWAAV GLTIAIMVLL LKKFIKSNGY
     STGFMDDQS
//