RGSL1_ARATH
ID RGSL1_ARATH Reviewed; 398 AA.
AC F4ITM1; O80984;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=E3 ubiquitin-protein ligase RSL1 {ECO:0000303|PubMed:24388521};
DE EC=2.3.2.31 {ECO:0000269|PubMed:24388521};
DE AltName: Full=Protein RING FINGER OF SEED LONGEVITY 1 {ECO:0000303|PubMed:12446796, ECO:0000303|PubMed:24388521};
DE AltName: Full=RING-type E3 ubiquitin transferase RSL1 {ECO:0000303|PubMed:24388521};
GN Name=RSL1 {ECO:0000303|PubMed:12446796, ECO:0000303|PubMed:24388521};
GN OrderedLocusNames=At2g26130 {ECO:0000312|Araport:AT2G26130};
GN ORFNames=T19L18.6 {ECO:0000312|EMBL:AAC31224.1};
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 GENE FAMILY ORGANIZATION.
RX PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT "Evaluation and classification of RING-finger domains encoded by the
RT Arabidopsis genome.";
RL Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
RN [4]
RP GENE FAMILY.
RX PubMed=12446796; DOI=10.1093/oxfordjournals.molbev.a004029;
RA Marin I., Ferrus A.;
RT "Comparative genomics of the RBR family, including the Parkinson's disease-
RT related gene parkin and the genes of the ariadne subfamily.";
RL Mol. Biol. Evol. 19:2039-2050(2002).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH PYL4 AND PYR1, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=25330042; DOI=10.1111/tpj.12708;
RA Bueso E., Rodriguez L., Lorenzo-Orts L., Gonzalez-Guzman M., Sayas E.,
RA Munoz-Bertomeu J., Ibanez C., Serrano R., Rodriguez P.L.;
RT "The single-subunit RING-type E3 ubiquitin ligase RSL1 targets PYL4 and
RT PYR1 ABA receptors in plasma membrane to modulate abscisic acid
RT signaling.";
RL Plant J. 80:1057-1071(2014).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Col-2, and cv. Columbia;
RX PubMed=24388521; DOI=10.1016/j.plantsci.2013.11.004;
RA Bueso E., Ibanez C., Sayas E., Munoz-Bertomeu J., Gonzalez-Guzman M.,
RA Rodriguez P.L., Serrano R.;
RT "A forward genetic approach in Arabidopsis thaliana identifies a RING-type
RT ubiquitin ligase as a novel determinant of seed longevity.";
RL Plant Sci. 215:110-116(2014).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27495812; DOI=10.1105/tpc.16.00178;
RA Belda-Palazon B., Rodriguez L., Fernandez M.A., Castillo M.-C.,
RA Anderson E.M., Gao C., Gonzalez-Guzman M., Peirats-Llobet M., Zhao Q.,
RA De Winne N., Gevaert K., De Jaeger G., Jiang L., Leon J., Mullen R.T.,
RA Rodriguez P.L.;
RT "FYVE1/FREE1 interacts with the PYL4 ABA receptor and mediates its delivery
RT to the vacuolar degradation pathway.";
RL Plant Cell 28:2291-2311(2016).
CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase, or as part of E3
CC complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC enzymes and then transfers it to substrates (PubMed:24388521). Negative
CC regulator of the abscisic acid (ABA) signaling pathway which targets
CC PYL4 and PYR1 ABA receptors in plasma membrane to promote their
CC FREE1/FYVE1-dependent trafficking and degradation upon ubiquitynation;
CC this process involves clathrin-mediated endocytosis and trafficking
CC through the ESCRT pathway (PubMed:25330042, PubMed:27495812). Involved
CC in the maintenance of seed longevity (PubMed:24388521). May enhance
CC gibberellins responses (PubMed:24388521). {ECO:0000269|PubMed:24388521,
CC ECO:0000269|PubMed:25330042, ECO:0000269|PubMed:27495812}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000269|PubMed:24388521};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 4 Zn(2+) ions per subunit. {ECO:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with the PYL4 and PYR1 ABA receptors at the plasma
CC membrane. {ECO:0000269|PubMed:25330042}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25330042};
CC Single-pass membrane protein {ECO:0000255}. Vacuole membrane
CC {ECO:0000269|PubMed:27495812}; Single-pass membrane protein
CC {ECO:0000255}. Note=Localized transiently in the vacuole when in
CC complex with PYL4 and PYR1. {ECO:0000269|PubMed:27495812}.
CC -!- DOMAIN: The RING-type zinc finger domains mediate binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Enhanced sensitivity to abscisic acid (ABA)
CC (PubMed:25330042). Decreased seed longevity (PubMed:24388521).
CC {ECO:0000269|PubMed:24388521, ECO:0000269|PubMed:25330042}.
CC -!- SIMILARITY: Belongs to the RBR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC31224.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004747; AAC31224.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07797.1; -; Genomic_DNA.
DR PIR; T02611; T02611.
DR RefSeq; NP_180182.2; NM_128171.3.
DR AlphaFoldDB; F4ITM1; -.
DR SMR; F4ITM1; -.
DR STRING; 3702.AT2G26130.1; -.
DR PaxDb; F4ITM1; -.
DR PRIDE; F4ITM1; -.
DR EnsemblPlants; AT2G26130.1; AT2G26130.1; AT2G26130.
DR GeneID; 817153; -.
DR Gramene; AT2G26130.1; AT2G26130.1; AT2G26130.
DR KEGG; ath:AT2G26130; -.
DR Araport; AT2G26130; -.
DR TAIR; locus:2057401; AT2G26130.
DR eggNOG; KOG1812; Eukaryota.
DR HOGENOM; CLU_022048_8_0_1; -.
DR InParanoid; F4ITM1; -.
DR OMA; HMIELSS; -.
DR OrthoDB; 1140368at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4ITM1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0140547; P:acquisition of seed longevity; IMP:UniProtKB.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010476; P:gibberellin mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0010431; P:seed maturation; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; PTHR11685; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF13456; RVT_3; 1.
DR SMART; SM00647; IBR; 2.
DR PROSITE; PS51873; TRIAD; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Cell membrane;
KW Gibberellin signaling pathway; Membrane; Metal-binding; Reference proteome;
KW Repeat; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Vacuole; Zinc; Zinc-finger.
FT CHAIN 1..398
FT /note="E3 ubiquitin-protein ligase RSL1"
FT /id="PRO_0000453287"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 159..208
FT /note="RING-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 159..207
FT /note="RING-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 233..292
FT /note="IBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ZN_FING 321..356
FT /note="RING-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 321..349
FT /note="RING-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT REGION 155..374
FT /note="TRIAD supradomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT ACT_SITE 334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01221"
SQ SEQUENCE 398 AA; 44554 MW; 70EBE1A697A66C3D CRC64;
MEEDDLNPAG KPLYRLYFKG LVTEEKEMLL AGFGVAICGD KDDLLFDLKV SIHDPTITLL
EVELIALKSG LNQAVSLGIN HISICCDHEY IFELVMGIST PKQESIALLL RDVQGIRKYL
TSSIPVMLTQ NQSNLAYDFA IEAISSEIII DIPAQKETCN ICLNDDINAD QMFSVDKSGH
MCCSECVKRH IEVRLLEGSL ITCPHYRCNS LLTSVRCGNL LTPKLNKMWE QKTKDELIPV
MDRVYCPNPR CSTLMSETEL SGLNIGVRRC CVKCGEPFCV KCKVSWHNNL SCDEYKTLHP
NPTENDGRLR DLANEKSWRQ CSKCKHMIEL SSGCISVVCR CGHTFCYQCG ADAGDCFHGL
GRDDLDLTQC CGSCCCFVFF LVIIAIVVTI ILLVRRFS
