RHA2A_ARATH
ID RHA2A_ARATH Reviewed; 155 AA.
AC Q9ZT50; Q4TU39;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=E3 ubiquitin-protein ligase RHA2A {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=RING-H2 finger A2a {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 zinc finger protein RHA2a {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase RHA2A {ECO:0000305};
GN Name=RHA2A {ECO:0000303|PubMed:9781696}; OrderedLocusNames=At1g15100;
GN ORFNames=F9L1.3;
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], AND TISSUE SPECIFICITY.
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 [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-103 AND
RP 110-LYS-LYS-111, AND INTERACTION WITH NAC019.
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 [8]
RP FUNCTION, INTERACTION WITH NAC019 AND NAC055, TISSUE SPECIFICITY,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-89.
RX PubMed=19286935; DOI=10.1104/pp.109.135269;
RA Bu Q., Li H., Zhao Q., Jiang H., Zhai Q., Zhang J., Wu X., Sun J., Xie Q.,
RA Wang D., Li C.;
RT "The Arabidopsis RING finger E3 ligase RHA2a is a novel positive regulator
RT of abscisic acid signaling during seed germination and early seedling
RT development.";
RL Plant Physiol. 150:463-481(2009).
RN [9]
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 development
CC (PubMed:19286935, PubMed:21478367). Acts additively with RHA2B in
CC regulating ABA signaling and drought response (PubMed:21478367).
CC Possesses E3 ubiquitin ligase activity in vitro (PubMed:15644464,
CC PubMed:19286935). {ECO:0000269|PubMed:15644464,
CC ECO:0000269|PubMed:19286935, 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 NAC019 and NAC055.
CC {ECO:0000269|PubMed:12646039, ECO:0000269|PubMed:19286935}.
CC -!- INTERACTION:
CC Q9ZT50; Q9C932: NAC019; NbExp=3; IntAct=EBI-2025293, EBI-1786615;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12646039,
CC ECO:0000269|PubMed:21478367}. Nucleus {ECO:0000269|PubMed:12646039,
CC ECO:0000269|PubMed:21478367}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, flowers, cauline leaves,
CC rosettes, siliques, seeds and roots. {ECO:0000269|PubMed:12646039,
CC ECO:0000269|PubMed:19286935, ECO:0000269|PubMed:9781696}.
CC -!- DOMAIN: The ring domain is sufficient for the interaction with ANAC.
CC -!- DOMAIN: Presence of both a nuclear localization sequence (NLS) and a
CC nuclear export sequence (NES).
CC -!- DISRUPTION PHENOTYPE: Decreased sensitivity to ABA and salt and osmotic
CC stresses during seed germination and early seedling development.
CC {ECO:0000269|PubMed:19286935}.
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DR EMBL; AF078822; AAC68671.1; -; mRNA.
DR EMBL; DQ059097; AAY57583.1; -; mRNA.
DR EMBL; AC007591; AAD39638.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29264.1; -; Genomic_DNA.
DR EMBL; AY075590; AAL91611.1; -; mRNA.
DR EMBL; AY094057; AAM16213.1; -; mRNA.
DR EMBL; AY088303; AAM65842.1; -; mRNA.
DR PIR; T51842; T51842.
DR RefSeq; NP_172962.1; NM_101378.3.
DR AlphaFoldDB; Q9ZT50; -.
DR BioGRID; 23313; 1.
DR IntAct; Q9ZT50; 1.
DR STRING; 3702.AT1G15100.1; -.
DR PaxDb; Q9ZT50; -.
DR PRIDE; Q9ZT50; -.
DR EnsemblPlants; AT1G15100.1; AT1G15100.1; AT1G15100.
DR GeneID; 838073; -.
DR Gramene; AT1G15100.1; AT1G15100.1; AT1G15100.
DR KEGG; ath:AT1G15100; -.
DR Araport; AT1G15100; -.
DR TAIR; locus:2037683; AT1G15100.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_013137_18_5_1; -.
DR InParanoid; Q9ZT50; -.
DR OMA; KLECRHV; -.
DR OrthoDB; 1522472at2759; -.
DR PhylomeDB; Q9ZT50; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9ZT50; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZT50; baseline and differential.
DR Genevisible; Q9ZT50; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009789; P:positive regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
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..155
FT /note="E3 ubiquitin-protein ligase RHA2A"
FT /id="PRO_0000056035"
FT ZN_FING 86..128
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 89
FT /note="C->A: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:19286935"
FT MUTAGEN 103
FT /note="E->P: Decreased affinity for ANAC."
FT /evidence="ECO:0000269|PubMed:12646039"
FT MUTAGEN 110..111
FT /note="KK->NE: Abolishes the nuclear concentration."
FT /evidence="ECO:0000269|PubMed:12646039"
SQ SEQUENCE 155 AA; 16983 MW; 70764215A9C20E6C CRC64;
MGLQGQLSDV SSDSIPLMLL SLLAVFINHL RSFLLRLTSK SNPNLPVDDV SIASGLANII
VLADQLSLNR LFSYRCGDGG GGGSDCVVCL SKLKEGEEVR KLECRHVFHK KCLEGWLHQF
NFTCPLCRSA LVSDDCVSKT QRSVGRDLIS CFSLH
