RING3_ARATH
ID RING3_ARATH Reviewed; 231 AA.
AC Q8LE94; Q56XU2; Q9SRU5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=E3 ubiquitin-protein ligase At3g02290;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein At3g02290;
DE AltName: Full=RING-type E3 ubiquitin transferase At3g02290 {ECO:0000305};
GN OrderedLocusNames=At3g02290; ORFNames=F14P3.6;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP IDENTIFICATION.
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).
CC -!- FUNCTION: Mediates E2-dependent protein ubiquitination. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LE94-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LE94-2; Sequence=VSP_036336;
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF02127.1; Type=Erroneous gene model prediction; Evidence={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; AC009755; AAF02127.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73788.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73789.2; -; Genomic_DNA.
DR EMBL; CP002686; ANM63853.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63854.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63855.1; -; Genomic_DNA.
DR EMBL; AK221581; BAD95066.1; -; mRNA.
DR EMBL; BT024610; ABD43008.1; -; mRNA.
DR EMBL; AY085549; AAM62773.1; -; mRNA.
DR RefSeq; NP_001319449.1; NM_001337393.1. [Q8LE94-1]
DR RefSeq; NP_001325921.1; NM_001337395.1. [Q8LE94-1]
DR RefSeq; NP_001325922.1; NM_001337397.1. [Q8LE94-1]
DR RefSeq; NP_001325923.1; NM_001337394.1. [Q8LE94-1]
DR RefSeq; NP_566169.1; NM_111096.4. [Q8LE94-1]
DR AlphaFoldDB; Q8LE94; -.
DR SMR; Q8LE94; -.
DR BioGRID; 6512; 2.
DR IntAct; Q8LE94; 2.
DR STRING; 3702.AT3G02290.1; -.
DR iPTMnet; Q8LE94; -.
DR PaxDb; Q8LE94; -.
DR ProteomicsDB; 236254; -. [Q8LE94-1]
DR EnsemblPlants; AT3G02290.1; AT3G02290.1; AT3G02290. [Q8LE94-1]
DR EnsemblPlants; AT3G02290.2; AT3G02290.2; AT3G02290. [Q8LE94-1]
DR EnsemblPlants; AT3G02290.3; AT3G02290.3; AT3G02290. [Q8LE94-1]
DR EnsemblPlants; AT3G02290.4; AT3G02290.4; AT3G02290. [Q8LE94-1]
DR EnsemblPlants; AT3G02290.6; AT3G02290.6; AT3G02290. [Q8LE94-1]
DR GeneID; 821179; -.
DR Gramene; AT3G02290.1; AT3G02290.1; AT3G02290. [Q8LE94-1]
DR Gramene; AT3G02290.2; AT3G02290.2; AT3G02290. [Q8LE94-1]
DR Gramene; AT3G02290.3; AT3G02290.3; AT3G02290. [Q8LE94-1]
DR Gramene; AT3G02290.4; AT3G02290.4; AT3G02290. [Q8LE94-1]
DR Gramene; AT3G02290.6; AT3G02290.6; AT3G02290. [Q8LE94-1]
DR KEGG; ath:AT3G02290; -.
DR Araport; AT3G02290; -.
DR TAIR; locus:2076542; AT3G02290.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_081123_0_0_1; -.
DR InParanoid; Q8LE94; -.
DR PhylomeDB; Q8LE94; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8LE94; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LE94; baseline and differential.
DR Genevisible; Q8LE94; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..231
FT /note="E3 ubiquitin-protein ligase At3g02290"
FT /id="PRO_0000271543"
FT ZN_FING 181..222
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 103..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 187..231
FT /note="EYTSENPKIVTKCSHHFHLSCIYEWMERSENCPVCGKVMEFNETP -> GNN
FT NPIQQSPFCSFSIHILLVFCRIYIREPKDCDKMFTPFPP (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_036336"
SQ SEQUENCE 231 AA; 26258 MW; 3B93D1B13C2AAA8D CRC64;
MGCVSSCFRV EDIDEYMNPN SSVYRNCPCI RCLAHNFLNL YISVFRRGET RSLPSSVQAT
ASITSSSSHD NFLSEAFRST PRPLPYDADP RYFRSLVSRR EKGSSHSHEE VEPLRSDSDA
DSESFGVGGC KWANNKSTLS DKDSKEEYSS KSSLRILRSR SKSIMADSEN MYILSEDEDV
CPTCLEEYTS ENPKIVTKCS HHFHLSCIYE WMERSENCPV CGKVMEFNET P
