RNG1L_ARATH
ID RNG1L_ARATH Reviewed; 328 AA.
AC Q8LPN7; Q8GXE4; Q9LT14;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=E3 ubiquitin-protein ligase RING1-like;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase RING1-like {ECO:0000305};
GN OrderedLocusNames=At3g19950; ORFNames=MPN9.19;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-328.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=20376576; DOI=10.1007/s12033-010-9280-7;
RA Ho M.-H., Saha S., Jenkins J.N., Ma D.-P.;
RT "Characterization and promoter analysis of a cotton RING-type ubiquitin
RT ligase (E3) gene.";
RL Mol. Biotechnol. 46:140-148(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. Promotes
CC polyubiquitination of target proteins. {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 -!- TISSUE SPECIFICITY: Expressed in leaves, roots, trichomes, stipules,
CC and also in anthers and stigma of flowers.
CC {ECO:0000269|PubMed:20376576}.
CC -!- PTM: Auto-ubiquitinated as part of the enzymatic reaction.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01310.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC42901.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB025631; BAB01310.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76311.1; -; Genomic_DNA.
DR EMBL; AY095995; AAM19951.1; -; mRNA.
DR EMBL; BT000583; AAN18152.1; -; mRNA.
DR EMBL; AK118283; BAC42901.1; ALT_INIT; mRNA.
DR RefSeq; NP_001326918.1; NM_001338429.1.
DR RefSeq; NP_001326919.1; NM_001338430.1.
DR RefSeq; NP_188629.1; NM_112885.5.
DR AlphaFoldDB; Q8LPN7; -.
DR SMR; Q8LPN7; -.
DR BioGRID; 6865; 3.
DR IntAct; Q8LPN7; 2.
DR STRING; 3702.AT3G19950.1; -.
DR iPTMnet; Q8LPN7; -.
DR PaxDb; Q8LPN7; -.
DR PRIDE; Q8LPN7; -.
DR ProteomicsDB; 227999; -.
DR EnsemblPlants; AT3G19950.1; AT3G19950.1; AT3G19950.
DR GeneID; 821533; -.
DR Gramene; AT3G19950.1; AT3G19950.1; AT3G19950.
DR KEGG; ath:AT3G19950; -.
DR Araport; AT3G19950; -.
DR TAIR; locus:2092231; AT3G19950.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_034892_3_2_1; -.
DR OMA; HSHCIVP; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q8LPN7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8LPN7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LPN7; baseline and differential.
DR Genevisible; Q8LPN7; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF14369; zinc_ribbon_9; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..328
FT /note="E3 ubiquitin-protein ligase RING1-like"
FT /id="PRO_0000396833"
FT ZN_FING 216..257
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 264..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 328 AA; 35705 MW; 255D81BE993C5682 CRC64;
MSSGVNSTGS AAAAPEVDKM FFCYQCNQTV TISISSSADP FCPICNQGFL EEYEDPNPNQ
SLNFNPNSSD SFFPMADPFS TLLPLIFGSS AAAPSGMDFM SLFGPSMQPQ ARSTQQNPQS
DAFDPFTFLQ NHLQTLRSSG THFEFVIENH PSDPGNRMPG NFGDYFFGPG LEQLIQQLAE
NDPNRYGTPP ASKSAIDALP TVKVTKDMLK SEMNQCAVCM DEFEDGSDVK QMPCKHVFHQ
DCLLPWLELH NSCPVCRFEL PTDDPDYENR SQGSQGSGDG QGSVEGQQTP RFSIQLPWPF
RRQDGSGSGS GAPGTGGGNL ETRGEDLD
