RCE1_ARATH
ID RCE1_ARATH Reviewed; 184 AA.
AC Q9SDY5; O23202; Q0WLB1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=NEDD8-conjugating enzyme Ubc12;
DE EC=2.3.2.-;
DE AltName: Full=RUB1 carrier protein 1;
DE AltName: Full=RUB1-conjugating enzyme 1;
GN Name=RCE1; OrderedLocusNames=At4g36800; ORFNames=C7A10.560;
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 [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=10611386; DOI=10.1073/pnas.96.26.15342;
RA del Pozo J.C., Estelle M.;
RT "The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related protein
RT RUB1.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15342-15347(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] (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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY, FUNCTION, AND INTERACTION WITH RBX1.
RX PubMed=12682009; DOI=10.1093/emboj/cdg190;
RA Dharmasiri S., Dharmasiri N., Hellmann H., Estelle M.;
RT "The RUB/Nedd8 conjugation pathway is required for early development in
RT Arabidopsis.";
RL EMBO J. 22:1762-1770(2003).
CC -!- FUNCTION: Accepts the ubiquitin-like protein NEDD8/RUB1 from the ECR1-
CC AXR1 E1 complex and catalyzes its covalent attachment to other
CC proteins. {ECO:0000269|PubMed:10611386, ECO:0000269|PubMed:12682009}.
CC -!- PATHWAY: Protein modification; protein neddylation.
CC -!- SUBUNIT: Interacts with RBX1. {ECO:0000269|PubMed:12682009}.
CC -!- INTERACTION:
CC Q9SDY5; Q940X7: RBX1A; NbExp=2; IntAct=EBI-595116, EBI-532404;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SDY5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SDY5-2; Sequence=VSP_034924;
CC -!- TISSUE SPECIFICITY: Expressed in shoot, root and floral meristems, and
CC in vascular tissues of leaves. {ECO:0000269|PubMed:12682009}.
CC -!- MISCELLANEOUS: Reduction in RCE1 levels leads to reduced organ length
CC and defects in gravitropism.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UBC12
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB16820.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80346.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF202771; AAF19827.1; -; mRNA.
DR EMBL; Z99708; CAB16820.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161590; CAB80346.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86703.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86704.1; -; Genomic_DNA.
DR EMBL; AY048210; AAK82473.1; -; mRNA.
DR EMBL; AY097381; AAM19897.1; -; mRNA.
DR EMBL; AK230295; BAF02096.1; -; mRNA.
DR PIR; E85434; E85434.
DR RefSeq; NP_001154289.1; NM_001160817.1. [Q9SDY5-1]
DR RefSeq; NP_568008.4; NM_119844.6. [Q9SDY5-1]
DR AlphaFoldDB; Q9SDY5; -.
DR SMR; Q9SDY5; -.
DR BioGRID; 15114; 5.
DR IntAct; Q9SDY5; 4.
DR STRING; 3702.AT4G36800.1; -.
DR iPTMnet; Q9SDY5; -.
DR PaxDb; Q9SDY5; -.
DR PRIDE; Q9SDY5; -.
DR ProteomicsDB; 236537; -. [Q9SDY5-1]
DR EnsemblPlants; AT4G36800.1; AT4G36800.1; AT4G36800. [Q9SDY5-1]
DR EnsemblPlants; AT4G36800.2; AT4G36800.2; AT4G36800. [Q9SDY5-1]
DR GeneID; 829833; -.
DR Gramene; AT4G36800.1; AT4G36800.1; AT4G36800. [Q9SDY5-1]
DR Gramene; AT4G36800.2; AT4G36800.2; AT4G36800. [Q9SDY5-1]
DR KEGG; ath:AT4G36800; -.
DR Araport; AT4G36800; -.
DR TAIR; locus:2115305; AT4G36800.
DR eggNOG; KOG0420; Eukaryota.
DR HOGENOM; CLU_030988_6_0_1; -.
DR InParanoid; Q9SDY5; -.
DR OMA; ICIELSE; -.
DR PhylomeDB; Q9SDY5; -.
DR UniPathway; UPA00885; -.
DR PRO; PR:Q9SDY5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SDY5; baseline and differential.
DR Genevisible; Q9SDY5; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019788; F:NEDD8 transferase activity; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..184
FT /note="NEDD8-conjugating enzyme Ubc12"
FT /id="PRO_0000082494"
FT DOMAIN 30..175
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 113
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT VAR_SEQ 102..184
FT /note="YHPNIDLEGNVCLNILREDWKPVLNINTVIYGLFHLFTEPNSEDPLNHDAAA
FT VLRDNPKLFETNVRRAMTGGYVGQTFFPRCI -> GLSSFYMPYIVYSFYFKIVCVVET
FT LCWFSCLGLSSQYRFGRKRLPEHL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_034924"
SQ SEQUENCE 184 AA; 20787 MW; 9F541991CED5C1E4 CRC64;
MIGLFKVKEK QREQAQNATR GGASVKKQSA GELRLHKDIS ELNLPSSCSI SFPNGKDDLM
NFEVSIKPDD GYYHNGTFVF TFQVSPVYPH EAPKVKCKTK VYHPNIDLEG NVCLNILRED
WKPVLNINTV IYGLFHLFTE PNSEDPLNHD AAAVLRDNPK LFETNVRRAM TGGYVGQTFF
PRCI
