RGLG5_ARATH
ID RGLG5_ARATH Reviewed; 433 AA.
AC Q8LB88;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=E3 ubiquitin-protein ligase RGLG5 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING domain ligase 5 {ECO:0000303|PubMed:27577789};
GN Name=RGLG5 {ECO:0000303|PubMed:27577789};
GN OrderedLocusNames=At1g67800 {ECO:0000312|Araport:AT1G67800};
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=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 [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 Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH PP2CA.
RX PubMed=27577789; DOI=10.1105/tpc.16.00364;
RA Wu Q., Zhang X., Peirats-Llobet M., Belda-Palazon B., Wang X., Cui S.,
RA Yu X., Rodriguez P.L., An C.;
RT "Ubiquitin ligases RGLG1 and RGLG5 regulate abscisic acid signaling by
RT controlling the turnover of phosphatase PP2CA.";
RL Plant Cell 28:2178-2196(2016).
CC -!- FUNCTION: Together with RGLG1, mediates the ubiquitination and
CC subsequent proteasomal degradation of the target protein PP2CA.
CC Functions as positive regulator of abscisic acid (ABA) signaling
CC through ABA-dependent degradation of PP2CA, a major inhibitor of ABA
CC signaling. {ECO:0000269|PubMed:27577789}.
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; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with PP2CA. {ECO:0000269|PubMed:27577789}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q8LB88-1; Sequence=Displayed;
CC -!- PTM: N-myristoylated. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC008113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE34697.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34699.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34700.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59315.1; -; Genomic_DNA.
DR EMBL; BT029741; ABM06011.1; -; mRNA.
DR EMBL; AY087355; AAM64905.1; -; mRNA.
DR RefSeq; NP_001077787.1; NM_001084318.3. [Q8LB88-1]
DR RefSeq; NP_001319339.1; NM_001334325.1. [Q8LB88-1]
DR RefSeq; NP_564907.1; NM_105448.5. [Q8LB88-1]
DR RefSeq; NP_974100.1; NM_202371.2. [Q8LB88-1]
DR AlphaFoldDB; Q8LB88; -.
DR SMR; Q8LB88; -.
DR IntAct; Q8LB88; 5.
DR STRING; 3702.AT1G67800.2; -.
DR PRIDE; Q8LB88; -.
DR EnsemblPlants; AT1G67800.1; AT1G67800.1; AT1G67800. [Q8LB88-1]
DR EnsemblPlants; AT1G67800.3; AT1G67800.3; AT1G67800. [Q8LB88-1]
DR EnsemblPlants; AT1G67800.4; AT1G67800.4; AT1G67800. [Q8LB88-1]
DR EnsemblPlants; AT1G67800.6; AT1G67800.6; AT1G67800. [Q8LB88-1]
DR GeneID; 843106; -.
DR Gramene; AT1G67800.1; AT1G67800.1; AT1G67800. [Q8LB88-1]
DR Gramene; AT1G67800.3; AT1G67800.3; AT1G67800. [Q8LB88-1]
DR Gramene; AT1G67800.4; AT1G67800.4; AT1G67800. [Q8LB88-1]
DR Gramene; AT1G67800.6; AT1G67800.6; AT1G67800. [Q8LB88-1]
DR KEGG; ath:AT1G67800; -.
DR Araport; AT1G67800; -.
DR eggNOG; KOG1327; Eukaryota.
DR HOGENOM; CLU_035766_1_0_1; -.
DR PhylomeDB; Q8LB88; -.
DR PRO; PR:Q8LB88; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LB88; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
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:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:InterPro.
DR CDD; cd16729; RING-HC_RGLG_plant; 1.
DR CDD; cd01459; vWA_copine_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR010734; Copine_C.
DR InterPro; IPR045317; RING-HC_RGLG_plant.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF07002; Copine; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; Cell membrane;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..433
FT /note="E3 ubiquitin-protein ligase RGLG5"
FT /id="PRO_0000438718"
FT DOMAIN 93..313
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 390..423
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 433 AA; 47498 MW; B6F644BB2F9CDD56 CRC64;
MGGSSSKESP RGGGSGRRYE RSVSGSSSYS SAWDQSSYYQ TPNHPSASPV SSYNSGRQTP
KNLERKYSRI ADNYRSIDEV TAALSHAGLE SSNLIVGIDV TKSNEWTGAR SFGRKSLHFI
GTTPNPYQQA ISIIGKTLSV FDEDNLIPCY GFGDATTHDQ DVFSFNPNDT YCNGFEEVLM
CYREIVPQLR LSGPTSFAPI IERAMTIVEE SGGQYHVLLI IADGQVTRSV DTDNGGFSPQ
EQQTIDAIVR ASEYPLSIVL VGVGDGPWDT MRQFDDNIPA RAFDNFQFVN FTDIMSKNID
PARKEAEFAL SALMEIPSQY KATLELGLLG QRTGHCPDRI ALPPPTYATQ SMRNSPRTSR
STSFQNKPYD NGVSSTPPST THNESQQQFC PVCLVSAKNM AFNCGHQTCA GCGEDLHVCP
ICRSSISVRI KLY
