RHA2B_ARATH
ID RHA2B_ARATH Reviewed; 147 AA.
AC Q9ZU51;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=E3 ubiquitin-protein ligase RHA2B {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=RING-H2 finger A2b {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 zinc finger protein RHA2b {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RHA2B {ECO:0000305};
GN Name=RHA2B {ECO:0000303|PubMed:9781696}; OrderedLocusNames=At2g01150;
GN ORFNames=F10A8.3;
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].
RC STRAIN=cv. Columbia;
RX PubMed=9781696; DOI=10.1016/s0014-5793(98)01143-0;
RA Jensen R.B., Jensen K.L., Jespersen H.M., Skriver K.;
RT "Widespread occurrence of a highly conserved RING-H2 zinc finger motif in
RT the model plant Arabidopsis thaliana.";
RL FEBS Lett. 436:283-287(1998).
RN [2]
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 [3]
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 [4]
RP TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12062802; DOI=10.1016/s0378-1119(02)00556-5;
RA Lechner E., Goloubinoff P., Genschik P., Shen W.H.;
RT "A gene trap Dissociation insertion line, associated with a RING-H2 finger
RT gene, shows tissue specific and developmental regulated expression of the
RT gene in Arabidopsis.";
RL Gene 290:63-71(2002).
RN [5]
RP INTERACTION WITH NAC19.
RX PubMed=12646039; DOI=10.1042/bj20021123;
RA Greve K., La Cour T., Jensen M.K., Poulsen F.M., Skriver K.;
RT "Interactions between plant RING-H2 and plant-specific NAC
RT (NAM/ATAF1/2/CUC2) proteins: RING-H2 molecular specificity and cellular
RT localization.";
RL Biochem. J. 371:97-108(2003).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21478367; DOI=10.1104/pp.111.176214;
RA Li H., Jiang H., Bu Q., Zhao Q., Sun J., Xie Q., Li C.;
RT "The Arabidopsis RING finger E3 ligase RHA2b acts additively with RHA2a in
RT regulating abscisic acid signaling and drought response.";
RL Plant Physiol. 156:550-563(2011).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the positive
CC regulation of abscisic acid (ABA) signaling and responses to salt and
CC osmotic stresses during seed germination and early seedling
CC development. Acts additively with RHA2A in regulating ABA signaling and
CC drought response. Possesses E3 ubiquitin ligase activity in vitro.
CC {ECO:0000269|PubMed:21478367}.
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 NAC19. {ECO:0000269|PubMed:12646039}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21478367}. Nucleus
CC {ECO:0000269|PubMed:21478367}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular tissue, root tips, embryos
CC and pistils. {ECO:0000269|PubMed:12062802}.
CC -!- INDUCTION: By the proteasome inhibitor MG132. Down-regulated during
CC reinitiation of mitotic activity. {ECO:0000269|PubMed:12062802}.
CC -!- DOMAIN: The ring domain is sufficient for the interaction with NAC19.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:12062802}.
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DR EMBL; AF078823; AAC68672.1; -; mRNA.
DR EMBL; AC006200; AAD14516.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC05407.1; -; Genomic_DNA.
DR PIR; C84421; C84421.
DR PIR; T51843; T51843.
DR RefSeq; NP_001318169.1; NM_001335035.1.
DR AlphaFoldDB; Q9ZU51; -.
DR SMR; Q9ZU51; -.
DR BioGRID; 48; 1.
DR IntAct; Q9ZU51; 1.
DR STRING; 3702.AT2G01150.1; -.
DR iPTMnet; Q9ZU51; -.
DR PaxDb; Q9ZU51; -.
DR EnsemblPlants; AT2G01150.1; AT2G01150.1; AT2G01150.
DR GeneID; 814644; -.
DR Gramene; AT2G01150.1; AT2G01150.1; AT2G01150.
DR KEGG; ath:AT2G01150; -.
DR Araport; AT2G01150; -.
DR TAIR; locus:2038766; AT2G01150.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_013137_18_5_1; -.
DR InParanoid; Q9ZU51; -.
DR OMA; PIQIEEN; -.
DR PhylomeDB; Q9ZU51; -.
DR BRENDA; 2.3.2.27; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9ZU51; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU51; baseline and differential.
DR Genevisible; Q9ZU51; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 signaling pathway; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Stress response; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..147
FT /note="E3 ubiquitin-protein ligase RHA2B"
FT /id="PRO_0000056036"
FT ZN_FING 74..116
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 147 AA; 16241 MW; 490F91805457A162 CRC64;
MGLQGQLSDV SSDSIPLMLL ALLATFFRHV RSLLLFPSSA PVVVVTSNLS VLADQLNLNR
LFSYRYSDNA ASDCIVCLSK LKTGEEVRKL DCRHVFHKQC LEGWLQHLNF NCPLCRSPLL
PHHHQGHGSD ASISAFPLRS TSTASSH
