LUL3_ARATH
ID LUL3_ARATH Reviewed; 378 AA.
AC Q84ME1; Q8L7V9;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable E3 ubiquitin-protein ligase LUL3;
DE EC=2.3.2.27;
DE AltName: Full=Probable RING-type E3 ubiquitin transferase LUL3 {ECO:0000305};
DE AltName: Full=Protein LOG2-LIKE UBIQUITIN LIGASE 3;
DE AltName: Full=RING finger protein 398;
GN Name=LUL3; Synonyms=RF398; OrderedLocusNames=At5g19080;
GN ORFNames=T16G12.120;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 DOMAIN.
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).
RN [6]
RP GENE SUBFAMILY, FUNCTION, MUTAGENESIS OF GLY-2, AND MYRISTOYLATION AT
RP GLY-2.
RX PubMed=22291198; DOI=10.1104/pp.111.191965;
RA Pratelli R., Guerra D.D., Yu S., Wogulis M., Kraft E., Frommer W.B.,
RA Callis J., Pilot G.;
RT "The ubiquitin E3 ligase LOSS OF GDU2 is required for GLUTAMINE DUMPER1-
RT induced amino acid secretion in Arabidopsis.";
RL Plant Physiol. 158:1628-1642(2012).
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 (in vitro).
CC {ECO:0000269|PubMed:22291198}.
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 -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- PTM: Myristoylated (in vitro). {ECO:0000269|PubMed:22291198}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. LOG2
CC subfamily. {ECO:0000305}.
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DR EMBL; AC068809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92649.1; -; Genomic_DNA.
DR EMBL; AY125510; AAM78102.1; -; mRNA.
DR EMBL; BT006357; AAP21165.1; -; mRNA.
DR RefSeq; NP_197409.1; NM_121913.3.
DR AlphaFoldDB; Q84ME1; -.
DR BioGRID; 17303; 7.
DR IntAct; Q84ME1; 7.
DR STRING; 3702.AT5G19080.1; -.
DR iPTMnet; Q84ME1; -.
DR PaxDb; Q84ME1; -.
DR PRIDE; Q84ME1; -.
DR ProteomicsDB; 238618; -.
DR EnsemblPlants; AT5G19080.1; AT5G19080.1; AT5G19080.
DR GeneID; 832027; -.
DR Gramene; AT5G19080.1; AT5G19080.1; AT5G19080.
DR KEGG; ath:AT5G19080; -.
DR Araport; AT5G19080; -.
DR TAIR; locus:2179594; AT5G19080.
DR eggNOG; KOG4265; Eukaryota.
DR HOGENOM; CLU_016631_0_0_1; -.
DR InParanoid; Q84ME1; -.
DR OMA; FNSSFNG; -.
DR OrthoDB; 883624at2759; -.
DR PhylomeDB; Q84ME1; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q84ME1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84ME1; baseline and differential.
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:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd16789; mRING-HC-C3HC5_MGRN1_like---blasttree; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045194; MGRN1/RNF157-like.
DR InterPro; IPR045195; MGRN1/RNF157_mRING_C3HC5.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22996; PTHR22996; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Lipoprotein; Metal-binding; Myristate; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:22291198"
FT CHAIN 2..378
FT /note="Probable E3 ubiquitin-protein ligase LUL3"
FT /id="PRO_0000419949"
FT ZN_FING 321..360
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..283
FT /note="DAR2 domain"
FT COMPBIAS 24..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..71
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:22291198"
FT MUTAGEN 2
FT /note="G->A: Abolishes myristoylation."
FT /evidence="ECO:0000269|PubMed:22291198"
FT CONFLICT 340
FT /note="C -> S (in Ref. 3; AAM78102)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42309 MW; 48AFE2DB67E3DAFB CRC64;
MGISLSKRRR DNNNNHHHPH HNPPYYYSDP PPQQPPPQNG YSYSHNYPVS TPQLSLPPPP
AQPPSSSQPP PSQISYRPYG QNYHQNQYYP QQAPPYFTGY HHNGFNPMMR PVYFGPTPVA
VMEPPAPYVE HQTAKKVKND VNVNKATVRL VADDLNPGHY LVSFVFDALF DGSFTIIFFG
EEESKCTIVP HLPEAFPPIK VPFQKGAGQK FLQAPGTGID LGFFSLDDLS KPSPEEVYPL
VISAETVISP SSVSEEPLVH KQITQAVLEK TNDGSFKVKV MKQILWIEGE RYELQELYGI
DNSITQGTAA SGLEDTGGKE CVICLTEPKD TAVMPCRHLC LCSDCAEELR FQTNKCPICR
QPIHELVKIK VESSDEQH
