ID   UBC8_ARATH              Reviewed;         148 AA.
AC   P35131; Q3E8J2; Q3E8J3; Q42308; Q43276; Q4TZ02; Q8LE19;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 8;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 8;
DE   AltName: Full=UBCAT4A;
DE   AltName: Full=Ubiquitin carrier protein 8;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 8;
DE   AltName: Full=Ubiquitin-protein ligase 8;
GN   Name=UBC8; Synonyms=UBC4A; OrderedLocusNames=At5g41700;
GN   ORFNames=MBK23.24;
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=Leaf;
RX   PubMed=8220461; DOI=10.1046/j.1365-313x.1993.03040545.x;
RA   Girod P.-A., Carpenter T.B., van Nocker S., Sullivan M.L., Vierstra R.D.;
RT   "Homologs of the essential ubiquitin conjugating enzymes UBC1, 4, and 5 in
RT   yeast are encoded by a multigene family in Arabidopsis thaliana.";
RL   Plant J. 3:545-552(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, GENE
RP   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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned P1
RT   clones.";
RL   DNA Res. 4:215-230(1997).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-74.
RC   STRAIN=cv. Columbia;
RX   PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA   Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA   Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA   Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA   Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA   Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA   Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT   "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT   a set of 5000 non-redundant ESTs.";
RL   Plant J. 9:101-124(1996).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-148.
RC   STRAIN=cv. Columbia; TISSUE=Green siliques;
RX   PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA   Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA   Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA   Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA   Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA   Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT   "An inventory of 1152 expressed sequence tags obtained by partial
RT   sequencing of cDNAs from Arabidopsis thaliana.";
RL   Plant J. 4:1051-1061(1993).
RN   [9]
RP   DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=8078482; DOI=10.1007/bf00583906;
RA   Genschik P., Durr A., Fleck J.;
RT   "Differential expression of several E2-type ubiquitin carrier protein genes
RT   at different developmental stages in Arabidopsis thaliana and Nicotiana
RT   sylvestris.";
RL   Mol. Gen. Genet. 244:548-556(1994).
RN   [10]
RP   INTERACTION WITH CIP8.
RX   PubMed=12028569; DOI=10.1046/j.1365-313x.2002.01298.x;
RA   Hardtke C.S., Okamoto H., Stoop-Myer C., Deng X.-W.;
RT   "Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1
RT   interacting protein 8 (CIP8).";
RL   Plant J. 30:385-394(2002).
RN   [11]
RP   INTERACTION WITH CHIP.
RX   PubMed=16640601; DOI=10.1111/j.1365-313x.2006.02730.x;
RA   Luo J., Shen G., Yan J., He C., Zhang H.;
RT   "AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A
RT   subunits and alters plant response to abscisic acid treatment.";
RL   Plant J. 46:649-657(2006).
RN   [12]
RP   INTERACTION WITH XERICO.
RX   PubMed=16792696; DOI=10.1111/j.1365-313x.2006.02782.x;
RA   Ko J.-H., Yang S.H., Han K.-H.;
RT   "Upregulation of an Arabidopsis RING-H2 gene, XERICO, confers drought
RT   tolerance through increased abscisic acid biosynthesis.";
RL   Plant J. 47:343-355(2006).
RN   [13]
RP   INTERACTION WITH NLA.
RX   PubMed=17355433; DOI=10.1111/j.1365-313x.2007.03050.x;
RA   Peng M., Hannam C., Gu H., Bi Y.-M., Rothstein S.J.;
RT   "A mutation in NLA, which encodes a RING-type ubiquitin ligase, disrupts
RT   the adaptability of Arabidopsis to nitrogen limitation.";
RL   Plant J. 50:320-337(2007).
CC   -!- FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. Mediates the selective
CC       degradation of short-lived and abnormal proteins.
CC       {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   -!- SUBUNIT: Interacts with CIP8, CHIP, NLA and XERICO.
CC       {ECO:0000269|PubMed:12028569, ECO:0000269|PubMed:16640601,
CC       ECO:0000269|PubMed:16792696, ECO:0000269|PubMed:17355433}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P35131-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P35131-2; Sequence=VSP_034925;
CC       Name=3;
CC         IsoId=P35131-3; Sequence=VSP_034926;
CC   -!- TISSUE SPECIFICITY: Highest expression in young stems, old leaves.
CC       Lowest levels in floral buds, anthers and young leaves.
CC       {ECO:0000269|PubMed:16339806}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during senescence, but not during the
CC       G0 to S phase transition. {ECO:0000269|PubMed:8078482}.
CC   -!- INDUCTION: Not induced by heat shock or wounding.
CC       {ECO:0000269|PubMed:8078482}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; Z14989; CAA78713.1; -; Genomic_DNA.
DR   EMBL; DQ027022; AAY44848.1; -; mRNA.
DR   EMBL; AB005233; BAB11476.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94711.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94712.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94713.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94714.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94715.1; -; Genomic_DNA.
DR   EMBL; AF325009; AAG40361.1; -; mRNA.
DR   EMBL; AY063074; AAL34248.1; -; mRNA.
DR   EMBL; AF370257; AAK44072.1; -; mRNA.
DR   EMBL; AY054595; AAK96786.1; -; mRNA.
DR   EMBL; AY057631; AAL15262.1; -; mRNA.
DR   EMBL; AY072514; AAL66929.1; -; mRNA.
DR   EMBL; AY085670; AAM62889.1; -; mRNA.
DR   EMBL; Z37225; CAA85527.1; -; mRNA.
DR   EMBL; Z17692; CAA79036.1; -; mRNA.
DR   RefSeq; NP_001190447.1; NM_001203518.1. [P35131-1]
DR   RefSeq; NP_568595.2; NM_123535.2. [P35131-2]
DR   RefSeq; NP_851114.1; NM_180783.2. [P35131-1]
DR   RefSeq; NP_851115.1; NM_180784.2. [P35131-1]
DR   RefSeq; NP_851116.1; NM_180785.2. [P35131-3]
DR   PDB; 4X57; X-ray; 2.80 A; A/C=1-148.
DR   PDBsum; 4X57; -.
DR   AlphaFoldDB; P35131; -.
DR   SMR; P35131; -.
DR   BioGRID; 19424; 17.
DR   IntAct; P35131; 2.
DR   STRING; 3702.P35131; -.
DR   PaxDb; 3702-AT5G41700-4; -.
DR   ProteomicsDB; 228602; -. [P35131-1]
DR   EnsemblPlants; AT5G41700.1; AT5G41700.1; AT5G41700. [P35131-1]
DR   EnsemblPlants; AT5G41700.2; AT5G41700.2; AT5G41700. [P35131-1]
DR   EnsemblPlants; AT5G41700.3; AT5G41700.3; AT5G41700. [P35131-3]
DR   EnsemblPlants; AT5G41700.4; AT5G41700.4; AT5G41700. [P35131-2]
DR   EnsemblPlants; AT5G41700.5; AT5G41700.5; AT5G41700. [P35131-1]
DR   GeneID; 834173; -.
DR   Gramene; AT5G41700.1; AT5G41700.1; AT5G41700. [P35131-1]
DR   Gramene; AT5G41700.2; AT5G41700.2; AT5G41700. [P35131-1]
DR   Gramene; AT5G41700.3; AT5G41700.3; AT5G41700. [P35131-3]
DR   Gramene; AT5G41700.4; AT5G41700.4; AT5G41700. [P35131-2]
DR   Gramene; AT5G41700.5; AT5G41700.5; AT5G41700. [P35131-1]
DR   KEGG; ath:AT5G41700; -.
DR   Araport; AT5G41700; -.
DR   TAIR; AT5G41700; UBC8.
DR   eggNOG; KOG0417; Eukaryota.
DR   HOGENOM; CLU_030988_13_3_1; -.
DR   InParanoid; P35131; -.
DR   OMA; NRIVWEW; -.
DR   OrthoDB; 333234at2759; -.
DR   PhylomeDB; P35131; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:P35131; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P35131; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; 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:0009960; P:endosperm development; IEP: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; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24068:SF537; UBIQUITIN-CONJUGATING ENZYME E2 8; 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; P35131; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Nucleotide-binding;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..148
FT                   /note="Ubiquitin-conjugating enzyme E2 8"
FT                   /id="PRO_0000082576"
FT   DOMAIN          1..147
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        85
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   VAR_SEQ         21..22
FT                   /note="CS -> CIF (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034925"
FT   VAR_SEQ         103..148
FT                   /note="LLSICSLLTDPNPDDPLVPEIAHMYKTDRAKYEATARNWTQKYAMG -> TL
FT                   IFQKHRFSNVRLCSKSIARASTFSARILLNAQALLLECLCM (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_034926"
FT   CONFLICT        72
FT                   /note="K -> M (in Ref. 5; AAL34248)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80
FT                   /note="S -> D (in Ref. 5;
FT                   AAK44072/AAL66929/AAL15262/AAK96786/AAG40361)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="T -> P (in Ref. 5;
FT                   AAK44072/AAL66929/AAL15262/AAK96786/AAG40361)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="E -> K (in Ref. 6; AAM62889)"
FT                   /evidence="ECO:0000305"
FT   HELIX           1..15
FT                   /evidence="ECO:0007829|PDB:4X57"
FT   STRAND          21..28
FT                   /evidence="ECO:0007829|PDB:4X57"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:4X57"
FT   TURN            44..47
FT                   /evidence="ECO:0007829|PDB:4X57"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:4X57"
FT   TURN            58..61
FT                   /evidence="ECO:0007829|PDB:4X57"
FT   STRAND          66..69
FT                   /evidence="ECO:0007829|PDB:4X57"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:4X57"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:4X57"
FT   HELIX           99..111
FT                   /evidence="ECO:0007829|PDB:4X57"
FT   HELIX           121..129
FT                   /evidence="ECO:0007829|PDB:4X57"
FT   HELIX           131..145
FT                   /evidence="ECO:0007829|PDB:4X57"
SQ   SEQUENCE   148 AA;  16533 MW;  27CAAEABBBE74972 CRC64;
     MASKRILKEL KDLQKDPPTS CSAGPVAEDM FHWQATIMGP AESPYSGGVF LVTIHFPPDY
     PFKPPKVAFR TKVFHPNINS NGSICLDILK EQWSPALTIS KVLLSICSLL TDPNPDDPLV
     PEIAHMYKTD RAKYEATARN WTQKYAMG
//