ID   XB32_ARATH              Reviewed;         508 AA.
AC   Q6NLQ8; Q9FHG9;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=E3 ubiquitin-protein ligase XBAT32;
DE            EC=2.3.2.27;
DE   AltName: Full=Ankyrin repeat domain and RING finger-containing protein XBAT32;
DE   AltName: Full=Protein XB3 homolog 2;
DE   AltName: Full=RING-type E3 ubiquitin transferase XBAT32;
GN   Name=XBAT32; OrderedLocusNames=At5g57740; ORFNames=MRI1.10;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT   features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT   clones.";
RL   DNA Res. 6:183-195(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;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15584963; DOI=10.1111/j.1365-313x.2004.02266.x;
RA   Nodzon L.A., Xu W.H., Wang Y., Pi L.Y., Chakrabarty P.K., Song W.Y.;
RT   "The ubiquitin ligase XBAT32 regulates lateral root development in
RT   Arabidopsis.";
RL   Plant J. 40:996-1006(2004).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH ACS4 AND ACS7.
RX   PubMed=20511490; DOI=10.1104/pp.110.156976;
RA   Prasad M.E., Schofield A., Lyzenga W., Liu H., Stone S.L.;
RT   "Arabidopsis RING E3 ligase XBAT32 regulates lateral root production
RT   through its role in ethylene biosynthesis.";
RL   Plant Physiol. 153:1587-1596(2010).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC       ACC synthases (ACS). Negatively regulates ethylene biosynthesis
CC       probably via ubiquitin-dependent degradation of ACS4 and ACS7 enzymes.
CC       Regulates lateral root formation and development by controlling
CC       ethylene production which inhibits lateral root formation at high
CC       concentration. {ECO:0000269|PubMed:15584963,
CC       ECO:0000269|PubMed:20511490}.
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 ACS4 and ACS7. {ECO:0000269|PubMed:20511490}.
CC   -!- TISSUE SPECIFICITY: Expressed in the vascular system of primary root,
CC       vascular tissue of leaves, stems and anthers.
CC       {ECO:0000269|PubMed:15584963}.
CC   -!- INDUCTION: By auxin. {ECO:0000269|PubMed:15584963}.
CC   -!- DISRUPTION PHENOTYPE: Delay in development and flowering. Deficiency in
CC       lateral root formation. {ECO:0000269|PubMed:15584963}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09592.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB018118; BAB09592.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED96944.1; -; Genomic_DNA.
DR   EMBL; BT011688; AAS49051.1; -; mRNA.
DR   EMBL; BT012272; AAS76759.1; -; mRNA.
DR   RefSeq; NP_200582.3; NM_125157.3.
DR   AlphaFoldDB; Q6NLQ8; -.
DR   SMR; Q6NLQ8; -.
DR   BioGRID; 21126; 4.
DR   STRING; 3702.AT5G57740.1; -.
DR   PaxDb; Q6NLQ8; -.
DR   PRIDE; Q6NLQ8; -.
DR   ProteomicsDB; 242402; -.
DR   EnsemblPlants; AT5G57740.1; AT5G57740.1; AT5G57740.
DR   GeneID; 835882; -.
DR   Gramene; AT5G57740.1; AT5G57740.1; AT5G57740.
DR   KEGG; ath:AT5G57740; -.
DR   Araport; AT5G57740; -.
DR   TAIR; locus:2172600; AT5G57740.
DR   eggNOG; ENOG502QR1Y; Eukaryota.
DR   HOGENOM; CLU_035461_0_0_1; -.
DR   InParanoid; Q6NLQ8; -.
DR   OMA; TPLCKPE; -.
DR   OrthoDB; 539223at2759; -.
DR   PhylomeDB; Q6NLQ8; -.
DR   BRENDA; 2.3.2.27; 399.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q6NLQ8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q6NLQ8; baseline and differential.
DR   Genevisible; Q6NLQ8; AT.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0010311; P:lateral root formation; IMP:UniProtKB.
DR   GO; GO:0010366; P:negative regulation of ethylene biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0009733; P:response to auxin; IEP:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR   Gene3D; 1.25.40.20; -; 2.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF12796; Ank_2; 3.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Developmental protein; Metal-binding; Reference proteome;
KW   Repeat; Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..508
FT                   /note="E3 ubiquitin-protein ligase XBAT32"
FT                   /id="PRO_0000395740"
FT   REPEAT          50..79
FT                   /note="ANK 1"
FT   REPEAT          83..112
FT                   /note="ANK 2"
FT   REPEAT          117..147
FT                   /note="ANK 3"
FT   REPEAT          177..206
FT                   /note="ANK 4"
FT   REPEAT          220..249
FT                   /note="ANK 5"
FT   ZN_FING         321..372
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   508 AA;  54586 MW;  D3702C865168E212 CRC64;
     MRFLSLVGNS FGCSASGERL VSAARDGDLQ EAKALLDYNP RLARYSTFGV RNSPLHYSAA
     QGHHEIVSLL VESGVDINLR NYRGQTALMQ ACQHGHWEVV LILILFGANI HRSDYLNGGT
     ALHLAALNGH PRCIRILLSE YIPSVPNCWS LLKNKKTSVA GFDSSVLHEV INRAADGGIT
     PLHVAALNGH IETVQLLLDL GASVTQVTVE DGTTIDLIGA GSTALHYASC GGNTQCCQLL
     ISKGACLAAV NSNGWTPMMV ARSWHRNWLE EILNPTTEQP QLHLPNVPSP FLCLPLMSIV
     NIAQECGWRE NDCLTPCRDP CAVCLERKCT VAADGCAHEF CTNCALYLST TSITSSKTSN
     VTPGSVPCPL CRNGIVSFTK LPHTTATTRT STSSRTSISL SFCTCSSDVL DTALLTNPHY
     SCKPVVSRTG SRTPQSARSS AFRSLSCRRF PPSLCLGGSD VDEPRSRLIG GSYSRSGVGF
     RRSTSQVEGK RSWFSALNHC VTTGGSAC