ATL2_ARATH
ID ATL2_ARATH Reviewed; 304 AA.
AC Q8L9T5; O24008; Q4FE42; Q9LUR1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=RING-H2 finger protein ATL2;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Protein ARABIDOPSIS TOXICOS EN LEVADURA 2;
DE Short=Protein ATL2;
DE AltName: Full=RING-type E3 ubiquitin transferase ATL2 {ECO:0000305};
GN Name=ATL2; OrderedLocusNames=At3g16720; ORFNames=MGL6.19;
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 [GENOMIC DNA].
RX PubMed=8914520; DOI=10.1007/bf02172405;
RA Martinez-Garcia M., Garciduenas-Pina C., Guzman P.;
RT "Gene isolation in Arabidopsis thaliana by conditional overexpression of
RT cDNAs toxic to Saccharomyces cerevisiae: identification of a novel early
RT response zinc-finger gene.";
RL Mol. Gen. Genet. 252:587-596(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Flower, Leaf, and Seedling;
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=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 [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;
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 [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 INDUCTION.
RX PubMed=10480382; DOI=10.1023/a:1006267201855;
RA Salinas-Mondragon R.E., Garciduenas-Pina C., Guzman P.;
RT "Early elicitor induction in members of a novel multigene family coding for
RT highly related RING-H2 proteins in Arabidopsis thaliana.";
RL Plant Mol. Biol. 40:579-590(1999).
RN [8]
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 [9]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15238540; DOI=10.1534/genetics.104.028043;
RA Serrano M., Guzman P.;
RT "Isolation and gene expression analysis of Arabidopsis thaliana mutants
RT with constitutive expression of ATL2, an early elicitor-response RING-H2
RT zinc-finger gene.";
RL Genetics 167:919-929(2004).
RN [10]
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 [11]
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).
CC -!- FUNCTION: May be involved in the early steps of the plant defense
CC signaling pathway.
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.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed around the apical meristem
CC region. {ECO:0000269|PubMed:15238540}.
CC -!- INDUCTION: Up-regulated by chitin or cellulases elicitors.
CC {ECO:0000269|PubMed:10480382, ECO:0000269|PubMed:15238540,
CC 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; L76926; AAC77829.1; -; Genomic_DNA.
DR EMBL; DQ086849; AAZ14073.1; -; mRNA.
DR EMBL; AB022217; BAB02764.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75857.1; -; Genomic_DNA.
DR EMBL; AY062865; AAL32943.1; -; mRNA.
DR EMBL; AY081621; AAM10183.1; -; mRNA.
DR EMBL; AY088232; AAM65773.1; -; mRNA.
DR PIR; T52079; T52079.
DR RefSeq; NP_188294.1; NM_112545.2.
DR AlphaFoldDB; Q8L9T5; -.
DR SMR; Q8L9T5; -.
DR BioGRID; 6258; 11.
DR STRING; 3702.AT3G16720.1; -.
DR iPTMnet; Q8L9T5; -.
DR PaxDb; Q8L9T5; -.
DR PRIDE; Q8L9T5; -.
DR ProteomicsDB; 246751; -.
DR EnsemblPlants; AT3G16720.1; AT3G16720.1; AT3G16720.
DR GeneID; 820924; -.
DR Gramene; AT3G16720.1; AT3G16720.1; AT3G16720.
DR KEGG; ath:AT3G16720; -.
DR Araport; AT3G16720; -.
DR TAIR; locus:2089398; AT3G16720.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_066543_0_0_1; -.
DR InParanoid; Q8L9T5; -.
DR OMA; SECCNSE; -.
DR OrthoDB; 1458622at2759; -.
DR PhylomeDB; Q8L9T5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8L9T5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L9T5; baseline and differential.
DR Genevisible; Q8L9T5; 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; IDA:TAIR.
DR GO; GO:0006952; P:defense response; IDA:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044675; RING1-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45676; PTHR45676; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Membrane; Metal-binding; Plant defense; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..304
FT /note="RING-H2 finger protein ATL2"
FT /id="PRO_0000055791"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 119..161
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 194..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 83
FT /note="S -> F (in Ref. 1; AAC77829)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="S -> P (in Ref. 6; AAM65773)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="S -> G (in Ref. 1; AAC77829)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 34052 MW; 99AD96D6CEC3010F CRC64;
MNSNDQDPIP FRPEDNNFSG SKTYAMSGKI MLSAIVILFF VVILMVFLHL YARWYLLRAR
RRHLRRRSRN RRATMVFFTA DPSTAATSVV ASRGLDPNVI KSLPVFTFSD ETHKDPIECA
VCLSEFEESE TGRVLPNCQH TFHVDCIDMW FHSHSTCPLC RSLVESLAGI ESTAAARERE
VVIAVDSDPV LVIEPSSSSG LTDEPHGSGS SQMLREDSGR KPAAIEVPRR TFSEFEDELT
RRDSPASQSF RSPMSRMLSF TRMLSRDRRS ASSPIAGAPP LSPTLSCRIQ MTESDIERGG
EESR
