LUL1_ARATH
ID LUL1_ARATH Reviewed; 337 AA.
AC Q9LYW5; Q8GZ27; Q8L8P7;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable E3 ubiquitin-protein ligase LUL1;
DE EC=2.3.2.27;
DE AltName: Full=Probable RING-type E3 ubiquitin transferase LUL1 {ECO:0000305};
DE AltName: Full=Protein LOG2-LIKE UBIQUITIN LIGASE 1;
DE AltName: Full=RING finger protein 370;
GN Name=LUL1; Synonyms=RF370; OrderedLocusNames=At5g03200;
GN ORFNames=F15A17_230, MOK16.11;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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 [9]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20716180; DOI=10.1111/j.1742-4658.2010.07768.x;
RA Yamauchi S., Fusada N., Hayashi H., Utsumi T., Uozumi N., Endo Y.,
RA Tozawa Y.;
RT "The consensus motif for N-myristoylation of plant proteins in a wheat germ
RT cell-free translation system.";
RL FEBS J. 277:3596-3607(2010).
RN [10]
RP GENE SUBFAMILY, AND FUNCTION.
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:20716180}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. LOG2
CC subfamily. {ECO:0000305}.
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DR EMBL; AB005240; BAB08380.1; -; Genomic_DNA.
DR EMBL; AL163002; CAB86087.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90569.1; -; Genomic_DNA.
DR EMBL; AK117244; BAC41920.1; -; mRNA.
DR EMBL; BT025883; ABF85785.1; -; mRNA.
DR EMBL; AY088884; AAM67190.1; -; mRNA.
DR PIR; T48341; T48341.
DR RefSeq; NP_195940.1; NM_120398.3.
DR AlphaFoldDB; Q9LYW5; -.
DR SMR; Q9LYW5; -.
DR BioGRID; 17184; 11.
DR IntAct; Q9LYW5; 11.
DR STRING; 3702.AT5G03200.1; -.
DR iPTMnet; Q9LYW5; -.
DR PaxDb; Q9LYW5; -.
DR PRIDE; Q9LYW5; -.
DR ProteomicsDB; 238782; -.
DR EnsemblPlants; AT5G03200.1; AT5G03200.1; AT5G03200.
DR GeneID; 831908; -.
DR Gramene; AT5G03200.1; AT5G03200.1; AT5G03200.
DR KEGG; ath:AT5G03200; -.
DR Araport; AT5G03200; -.
DR TAIR; locus:2143493; AT5G03200.
DR eggNOG; KOG4265; Eukaryota.
DR HOGENOM; CLU_016631_0_0_1; -.
DR InParanoid; Q9LYW5; -.
DR OMA; PPITFDF; -.
DR OrthoDB; 883624at2759; -.
DR PhylomeDB; Q9LYW5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LYW5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYW5; baseline and differential.
DR Genevisible; Q9LYW5; AT.
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 CHAIN 2..337
FT /note="Probable E3 ubiquitin-protein ligase LUL1"
FT /id="PRO_0000419947"
FT ZN_FING 285..324
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 139..255
FT /note="DAR2 domain"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20716180"
FT CONFLICT 29
FT /note="E -> D (in Ref. 4; BAC41920)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="V -> A (in Ref. 6; AAM67190)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="H -> D (in Ref. 4; BAC41920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37720 MW; FF353C1900702147 CRC64;
MGNLISLIFC CGRRQRSNIP PAMETAPLEL PPNRFVFAAV PPYLNPNPNY VDQYPGNCLP
PPVTEPPMLP YNFNHLHHYP PNSYQLPHPL FHGGRYPILP PPTYVHQKAV TIRNDVNLKK
KTLTLIPDPE NPNRLLVSFT FDASMPGRIT VVFFATEDAE CNLRATKEDT LPPITFDFGE
GLGQKFIQSS GTGIDLTAFK DSELFKEVDT DVFPLAVKAE ATPAEEGKSG STNVQITQVV
YTKEKGEIKI EVVKQILWVN KRRYELLEIY GIENTVDGSD EGKECVVCLS EPRDTTVLPC
RHMCMCSGCA KALRFQTNLC PVCRQPVEML LEINKNG
