RNG1A_ARATH
ID RNG1A_ARATH Reviewed; 522 AA.
AC Q9FKW0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Putative E3 ubiquitin-protein ligase RING1a;
DE EC=2.3.2.27;
DE AltName: Full=Polycomb complex protein RING1a;
DE AltName: Full=Protein RING1a;
DE Short=AtRING1a;
DE AltName: Full=RING-type E3 ubiquitin transferase RING1a {ECO:0000305};
DE AltName: Full=Ring finger protein 434;
GN Name=RING1A; Synonyms=RF434; OrderedLocusNames=At5g44280; ORFNames=K9L2.3;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CLF, COMPONENT OF THE
RP PRC1-LIKE COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=19097900; DOI=10.1016/j.cub.2008.11.019;
RA Xu L., Shen W.H.;
RT "Polycomb silencing of KNOX genes confines shoot stem cell niches in
RT Arabidopsis.";
RL Curr. Biol. 18:1966-1971(2008).
CC -!- FUNCTION: Putative E3 ubiquitin-protein ligase that mediates
CC monoubiquitination of 'Lys-119' of histone H2A (H2AK119ub), thereby
CC playing a central role in histone code and gene regulation.
CC {ECO:0000250}.
CC -!- FUNCTION: As part of the PRC1-like complex, repress class I KNOX gene
CC expression. PcG PRC1 complex maintains the transcriptionally repressive
CC state of many genes, including Hox genes, throughout development. PcG
CC PRC1 complex acts via chromatin remodeling and modification of
CC histones, rendering chromatin heritably changed in its expressibility.
CC {ECO:0000269|PubMed:19097900}.
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: Homodimer or heterodimer with RING1B. Interacts with CLF.
CC Component of the PRC1-like complex, at least composed of RING1A, RING1B
CC and LHP1. {ECO:0000269|PubMed:19097900}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19097900}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FKW0-1; Sequence=Displayed;
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Normal phenotype. Drastic growth defects like
CC ectopic meristem formation and sterility when associated with the
CC disruption of RING1B. {ECO:0000269|PubMed:19097900}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK228896; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB10113.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB011475; BAB10113.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95085.1; -; Genomic_DNA.
DR EMBL; AK228896; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_199241.2; NM_123795.5. [Q9FKW0-1]
DR PDB; 5XVW; X-ray; 1.85 A; D/F=358-371.
DR PDB; 5Y21; X-ray; 1.77 A; C/D=304-317.
DR PDBsum; 5XVW; -.
DR PDBsum; 5Y21; -.
DR AlphaFoldDB; Q9FKW0; -.
DR SMR; Q9FKW0; -.
DR BioGRID; 19701; 5.
DR STRING; 3702.AT5G44280.2; -.
DR iPTMnet; Q9FKW0; -.
DR PRIDE; Q9FKW0; -.
DR ProteomicsDB; 227973; -. [Q9FKW0-1]
DR EnsemblPlants; AT5G44280.1; AT5G44280.1; AT5G44280. [Q9FKW0-1]
DR GeneID; 834451; -.
DR Gramene; AT5G44280.1; AT5G44280.1; AT5G44280. [Q9FKW0-1]
DR KEGG; ath:AT5G44280; -.
DR Araport; AT5G44280; -.
DR eggNOG; KOG0311; Eukaryota.
DR HOGENOM; CLU_025237_0_0_1; -.
DR InParanoid; Q9FKW0; -.
DR OMA; MDEFIIV; -.
DR PhylomeDB; Q9FKW0; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FKW0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKW0; baseline and differential.
DR Genevisible; Q9FKW0; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0001709; P:cell fate determination; IMP:UniProtKB.
DR GO; GO:0010076; P:maintenance of floral meristem identity; IMP:UniProtKB.
DR GO; GO:0010077; P:maintenance of inflorescence meristem identity; IMP:UniProtKB.
DR GO; GO:0010492; P:maintenance of shoot apical meristem identity; IMP:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IGI:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044592; RING1A/B.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46537; PTHR46537; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Metal-binding;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..522
FT /note="Putative E3 ubiquitin-protein ligase RING1a"
FT /id="PRO_0000397096"
FT ZN_FING 136..176
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..107
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 59198 MW; BFC30DE83876D712 CRC64;
MSVKNNSFSS AEIPDVADQP RDRFNPEATQ DLQEKDETKE EKEGDEEVKH DEAEEDQEVV
KPNDAEEDDD GDDAEEDEEE EVEAEEDEEA EEEEEEEEEE EEEEEDSKER SPSSISGDQS
EFMEIDLGEI RKDVQCPICL GIIKKTRTVM ECLHRFCREC IDKSMRLGNN ECPACRKHCA
SRRSLRDDPK FDALIAALFT NIDSYEEEEL AFHEDEMARN KQIQASIAQI SQRQSEALVK
RRSLGKEAAV LMRSPRIASG SRRRRNSRNM EQQNASEAHE DDDNDDNNNR GRDKDSSSDE
RGTEVRQKKR RKRSTSRSTQ HPSSSGANKN NGNCADNDTE VYRDTKGISP GLVWNPEILA
WGRGGTRSNT RHGNNTSGGS SKSVRNARVN KLVEYLRSSV DGSSVELDIH VKLVSLDTKC
IPDLPQPYLC CRPTLLVKQL REFVALQIHL KTEEVELLVT RRRVGEDAAI ENLPAVTPAS
AAASKDEMLS LEDNETLSRL KIDFISSHEQ HLIIAYRKKQ TE
