UBC33_ARATH
ID UBC33_ARATH Reviewed; 243 AA.
AC Q9FK29; Q2V2Z8; Q4TYX8;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable ubiquitin-conjugating enzyme E2 33;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 33;
DE AltName: Full=Ubiquitin carrier protein 33;
GN Name=UBC33; OrderedLocusNames=At5g50430; ORFNames=MXI22.15;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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] (ISOFORM 1).
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 [MRNA] OF 1-219, GENE FAMILY, AND 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FK29-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FK29-2; Sequence=VSP_034928;
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AB012248; BAB09462.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95943.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95944.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95945.1; -; Genomic_DNA.
DR EMBL; AF380654; AAK55735.1; -; mRNA.
DR EMBL; AY142040; AAM98304.1; -; mRNA.
DR EMBL; DQ027046; AAY44872.1; -; mRNA.
DR RefSeq; NP_001032048.2; NM_001036971.2. [Q9FK29-1]
DR RefSeq; NP_001032049.1; NM_001036972.2. [Q9FK29-2]
DR RefSeq; NP_199854.1; NM_124425.4. [Q9FK29-1]
DR AlphaFoldDB; Q9FK29; -.
DR SMR; Q9FK29; -.
DR STRING; 3702.AT5G50430.1; -.
DR TCDB; 3.A.16.1.5; the endoplasmic reticular retrotranslocon (er-rt) family.
DR PaxDb; Q9FK29; -.
DR PRIDE; Q9FK29; -.
DR ProteomicsDB; 228656; -. [Q9FK29-1]
DR EnsemblPlants; AT5G50430.1; AT5G50430.1; AT5G50430. [Q9FK29-1]
DR EnsemblPlants; AT5G50430.2; AT5G50430.2; AT5G50430. [Q9FK29-1]
DR EnsemblPlants; AT5G50430.3; AT5G50430.3; AT5G50430. [Q9FK29-2]
DR GeneID; 835111; -.
DR Gramene; AT5G50430.1; AT5G50430.1; AT5G50430. [Q9FK29-1]
DR Gramene; AT5G50430.2; AT5G50430.2; AT5G50430. [Q9FK29-1]
DR Gramene; AT5G50430.3; AT5G50430.3; AT5G50430. [Q9FK29-2]
DR KEGG; ath:AT5G50430; -.
DR Araport; AT5G50430; -.
DR TAIR; locus:2177502; AT5G50430.
DR eggNOG; KOG0894; Eukaryota.
DR HOGENOM; CLU_041481_1_0_1; -.
DR InParanoid; Q9FK29; -.
DR OMA; ECNTRIC; -.
DR OrthoDB; 1230974at2759; -.
DR PhylomeDB; Q9FK29; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FK29; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK29; baseline and differential.
DR Genevisible; Q9FK29; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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 Alternative splicing; ATP-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway.
FT CHAIN 1..243
FT /note="Probable ubiquitin-conjugating enzyme E2 33"
FT /id="PRO_0000345198"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 5..162
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 168..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT VAR_SEQ 38..51
FT /note="HYVLEGSEGTPFAG -> R (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034928"
SQ SEQUENCE 243 AA; 27357 MW; 0A461F79073C954D CRC64;
MAEKACIKRL QKEYRALCKE PVSHVVARPS PNDILEWHYV LEGSEGTPFA GGFYYGKIKF
PPEYPYKPPG ITMTTPNGRF VTQKKICLSM SDFHPESWNP MWSVSSILTG LLSFMMDNSP
TTGSVNTSVA EKQRLAKSSL AFNCKSVTFR KLFPEYVEKY SQQQVAEEEA ATQQTTTSEN
QDFPQKDNAK VESEKSVGLK KESIQEVGLK ERRRNKKEAL PGWIVLLLVS IVGVVMALPL
LQL
