ATL45_ARATH
ID ATL45_ARATH Reviewed; 200 AA.
AC Q9ZT49; Q4TU10;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable E3 ubiquitin-protein ligase ATL45 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-H2 finger A3b {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 finger protein ATL45 {ECO:0000305};
DE AltName: Full=RING-H2 zinc finger protein RHA3b {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL45 {ECO:0000305};
GN Name=ATL45 {ECO:0000303|PubMed:16557337};
GN Synonyms=RHA3B {ECO:0000303|PubMed:9781696};
GN OrderedLocusNames=At4g35480 {ECO:0000312|Araport:AT4G35480};
GN ORFNames=F15J1.50 {ECO:0000312|EMBL:CAB54876.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=9781696; DOI=10.1016/s0014-5793(98)01143-0;
RA Jensen R.B., Jensen K.L., Jespersen H.M., Skriver K.;
RT "Widespread occurrence of a highly conserved RING-H2 zinc finger motif in
RT the model plant Arabidopsis thaliana.";
RL FEBS Lett. 436:283-287(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista-Mercan V.R., Kim C.J., Chen H., Quan R., De Los Reyes C.,
RA Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2007) 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 NOMENCLATURE, AND GENE FAMILY ORGANIZATION.
RX PubMed=16557337; DOI=10.1007/s00239-005-0038-y;
RA Serrano M., Parra S., Alcaraz L.D., Guzman P.;
RT "The ATL gene family from Arabidopsis thaliana and Oryza sativa comprises a
RT large number of putative ubiquitin ligases of the RING-H2 type.";
RL J. Mol. Evol. 62:434-445(2006).
RN [9]
RP INDUCTION BY CHITIN.
RX PubMed=17722694; DOI=10.1094/mpmi-20-8-0900;
RA Libault M., Wan J., Czechowski T., Udvardi M., Stacey G.;
RT "Identification of 118 Arabidopsis transcription factor and 30 ubiquitin-
RT ligase genes responding to chitin, a plant-defense elicitor.";
RL Mol. Plant Microbe Interact. 20:900-911(2007).
RN [10]
RP FUNCTION, AND INTERACTION WITH BIK1.
RX DOI=10.1038/s41586-020-2210-3;
RA Xiyu M., Lucas A.N.C., Michelle E.L., Kai T., Zhiping W., Jun L., Xiao Y.,
RA Bo L., Jinggeng Z., Daniel V.S., Junmin P., Brett M.T., Antje H.,
RA Eugenia R., Ping H., Libo S.;
RT "Ligand-induced monoubiquitination of BIK1 regulates plant immunity.";
RL Nature 0:0-0(2020).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that possess E3 ubiquitin ligase
CC activity in vitro and mediates protein monoubiquitination (Ref.10).
CC Triggers the monoubiquitination of phosphorylated BIK1 in response to
CC pathogen-associated molecular pattern (PAMP) detection (Ref.10). May be
CC involved in the early steps of the plant defense signaling pathway
CC (Probable). {ECO:0000269|Ref.10, ECO:0000305|PubMed:17722694}.
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; Evidence={ECO:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with BIK1. {ECO:0000269|Ref.10}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by chitin. {ECO:0000269|PubMed:17722694}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC {ECO:0000305}.
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DR EMBL; AF078825; AAC68674.1; -; mRNA.
DR EMBL; DQ059126; AAY57612.1; -; mRNA.
DR EMBL; AL117188; CAB54876.1; -; Genomic_DNA.
DR EMBL; AL161587; CAB80264.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86520.1; -; Genomic_DNA.
DR EMBL; BT030633; ABR46213.1; -; mRNA.
DR EMBL; AY087082; AAM64643.1; -; mRNA.
DR PIR; T41745; T41745.
DR RefSeq; NP_195273.1; NM_119713.4.
DR AlphaFoldDB; Q9ZT49; -.
DR SMR; Q9ZT49; -.
DR STRING; 3702.AT4G35480.1; -.
DR PaxDb; Q9ZT49; -.
DR PRIDE; Q9ZT49; -.
DR ProteomicsDB; 246761; -.
DR EnsemblPlants; AT4G35480.1; AT4G35480.1; AT4G35480.
DR GeneID; 829700; -.
DR Gramene; AT4G35480.1; AT4G35480.1; AT4G35480.
DR KEGG; ath:AT4G35480; -.
DR Araport; AT4G35480; -.
DR TAIR; locus:2117622; AT4G35480.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_013137_9_1_1; -.
DR InParanoid; Q9ZT49; -.
DR OMA; ICITEFS; -.
DR OrthoDB; 1348127at2759; -.
DR PhylomeDB; Q9ZT49; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9ZT49; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZT49; baseline and differential.
DR Genevisible; Q9ZT49; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006513; P:protein monoubiquitination; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Membrane; Metal-binding; Plant defense; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..200
FT /note="Probable E3 ubiquitin-protein ligase ATL45"
FT /id="PRO_0000055805"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 113..155
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 200 AA; 21083 MW; 0AAEB71B868A759D CRC64;
MTRSSRFLGT ASPPPPEEIL AAETDMVVIL SALLCALVCV AGLAAVARCA WLRRLTGVNP
AAVGEAPPPN KGLKKKALQA LPKSTYTASA STAAAADDLP CSSVGDGDSS TECAICITEF
SEGEEIRILP LCSHAFHVAC IDKWLTSRSS CPSCRRILVP VKCDRCGHHA STAETQVKDQ
PPHHQHPSQF TSAIIPAFLP
