UBC32_ARATH
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 25-MAY-2022, entry version 135.
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.AT3G17000.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PaxDb; Q9LSP7; -.
DR PRIDE; Q9LSP7; -.
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; locus:2086067; AT3G17000.
DR eggNOG; KOG0428; Eukaryota.
DR HOGENOM; CLU_041481_0_0_1; -.
DR InParanoid; Q9LSP7; -.
DR OMA; CGCSHAD; -.
DR OrthoDB; 1230974at2759; -.
DR PhylomeDB; Q9LSP7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LSP7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSP7; baseline and differential.
DR Genevisible; Q9LSP7; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA:GO_Central.
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: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; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
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
