XERIC_ARATH
ID XERIC_ARATH Reviewed; 162 AA.
AC Q9SI09;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable E3 ubiquitin-protein ligase XERICO;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase XERICO;
GN Name=XERICO; OrderedLocusNames=At2g04240; ORFNames=T23O15.13;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ABSCISIC ACID AND ABIOTIC
RP STRESSES, AND INTERACTION WITH UBC8 AND TULP9.
RC STRAIN=cv. Columbia;
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 [5]
RP FUNCTION, INDUCTION BY RGA AND GAI, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17933900; DOI=10.1105/tpc.107.054999;
RA Zentella R., Zhang Z.L., Park M., Thomas S.G., Endo A., Murase K.,
RA Fleet C.M., Jikumaru Y., Nambara E., Kamiya Y., Sun T.P.;
RT "Global analysis of della direct targets in early gibberellin signaling in
RT Arabidopsis.";
RL Plant Cell 19:3037-3057(2007).
RN [6]
RP INDUCTION BY RGL2.
RX PubMed=18941053; DOI=10.1105/tpc.108.061515;
RA Piskurewicz U., Jikumaru Y., Kinoshita N., Nambara E., Kamiya Y.,
RA Lopez-Molina L.;
RT "The gibberellic acid signaling repressor RGL2 inhibits Arabidopsis seed
RT germination by stimulating abscisic acid synthesis and ABI5 activity.";
RL Plant Cell 20:2729-2745(2008).
RN [7]
RP INDUCTION BY RGL2.
RX PubMed=23818171; DOI=10.1104/pp.113.219451;
RA Ariizumi T., Hauvermale A.L., Nelson S.K., Hanada A., Yamaguchi S.,
RA Steber C.M.;
RT "Lifting della repression of Arabidopsis seed germination by nonproteolytic
RT gibberellin signaling.";
RL Plant Physiol. 162:2125-2139(2013).
CC -!- FUNCTION: Function on abscisic acid homeostasis at post-translational
CC level, probably through ubiquitin/proteasome-dependent substrate-
CC specific degradation. {ECO:0000269|PubMed:16792696,
CC ECO:0000269|PubMed:17933900}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with UBC8 and TULP9. {ECO:0000269|PubMed:16792696}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Higher expression in actively growing
CC tissues. {ECO:0000269|PubMed:16792696}.
CC -!- INDUCTION: Up-regulated by salt and osmotic stress. Not regulated by
CC abscisic acid treatment. Up-regulated by the DELLA proteins RGL2, RGA
CC and GAI. {ECO:0000269|PubMed:16792696, ECO:0000269|PubMed:17933900,
CC ECO:0000269|PubMed:18941053, ECO:0000269|PubMed:23818171}.
CC -!- DISRUPTION PHENOTYPE: Contains lower amounts of endogenous abscisic
CC acid and is more resistant to abscisic acid treatment during seedling
CC establishment. {ECO:0000269|PubMed:17933900}.
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DR EMBL; AC007213; AAD27914.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05811.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05812.1; -; Genomic_DNA.
DR EMBL; AF324691; AAG40042.1; -; mRNA.
DR EMBL; AF326867; AAG41449.1; -; mRNA.
DR EMBL; AF339689; AAK00371.1; -; mRNA.
DR PIR; E84455; E84455.
DR RefSeq; NP_178507.1; NM_126459.3.
DR RefSeq; NP_973416.1; NM_201687.1.
DR AlphaFoldDB; Q9SI09; -.
DR SMR; Q9SI09; -.
DR BioGRID; 363; 8.
DR IntAct; Q9SI09; 6.
DR STRING; 3702.AT2G04240.2; -.
DR PaxDb; Q9SI09; -.
DR PRIDE; Q9SI09; -.
DR EnsemblPlants; AT2G04240.1; AT2G04240.1; AT2G04240.
DR EnsemblPlants; AT2G04240.2; AT2G04240.2; AT2G04240.
DR GeneID; 814962; -.
DR Gramene; AT2G04240.1; AT2G04240.1; AT2G04240.
DR Gramene; AT2G04240.2; AT2G04240.2; AT2G04240.
DR KEGG; ath:AT2G04240; -.
DR Araport; AT2G04240; -.
DR TAIR; locus:2059793; AT2G04240.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_013137_18_5_1; -.
DR InParanoid; Q9SI09; -.
DR OMA; ESFDFHL; -.
DR OrthoDB; 1590694at2759; -.
DR PhylomeDB; Q9SI09; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SI09; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SI09; baseline and differential.
DR Genevisible; Q9SI09; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009687; P:abscisic acid metabolic process; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0009739; P:response to gibberellin; IEP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044249; XERICO-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47258; PTHR47258; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid biosynthesis; Membrane; Metal-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..162
FT /note="Probable E3 ubiquitin-protein ligase XERICO"
FT /id="PRO_0000430492"
FT TRANSMEM 12..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 103..145
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 162 AA; 17928 MW; AE0FC6D24777756C CRC64;
MGLSSLPGPS EGMLCVILVN TALSISIVKG IVRSFLGIVG ISLSPSSSSP SSVTVSSENS
STSESFDFRV CQPESYLEEF RNRTPTLRFE SLCRCKKQAD NECSVCLSKF QGDSEINKLK
CGHLFHKTCL EKWIDYWNIT CPLCRTPLVV VPEDHQLSSN VW
