ATL9_ARATH
ID ATL9_ARATH Reviewed; 378 AA.
AC O64763; Q4TU26;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=E3 ubiquitin-protein ligase ATL9;
DE EC=2.3.2.27 {ECO:0000269|PubMed:15644464};
DE AltName: Full=RING-H2 finger protein ATL9;
DE AltName: Full=RING-type E3 ubiquitin transferase ATL9 {ECO:0000305};
DE Flags: Precursor;
GN Name=ATL9; OrderedLocusNames=At2g35000; ORFNames=F19I3.23;
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], FUNCTION, AND CATALYTIC ACTIVITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP IDENTIFICATION.
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY CHITIN.
RX PubMed=15923325; DOI=10.1104/pp.105.060947;
RA Ramonell K., Berrocal-Lobo M., Koh S., Wan J., Edwards H., Stacey G.,
RA Somerville S.;
RT "Loss-of-function mutations in chitin responsive genes show increased
RT susceptibility to the powdery mildew pathogen Erysiphe cichoracearum.";
RL Plant Physiol. 138:1027-1036(2005).
RN [9]
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase able to catalyze
CC polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8 in vitro.
CC May be involved in the early steps of the plant defense signaling
CC pathway. {ECO:0000269|PubMed:15644464, ECO:0000269|PubMed:15923325}.
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:0000269|PubMed:15644464};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by chitin elicitors.
CC {ECO:0000269|PubMed:15923325}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Susceptibility to powdery mildew pathogen
CC E.cichoracearum. {ECO:0000269|PubMed:15923325}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ059110; AAY57596.1; -; mRNA.
DR EMBL; AC004238; AAC12839.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09047.1; -; Genomic_DNA.
DR EMBL; BT015733; AAU84670.1; -; mRNA.
DR EMBL; BT020192; AAV43794.1; -; mRNA.
DR EMBL; AK228813; BAF00709.1; -; mRNA.
DR PIR; T00481; T00481.
DR RefSeq; NP_181045.1; NM_129052.3.
DR AlphaFoldDB; O64763; -.
DR SMR; O64763; -.
DR STRING; 3702.AT2G35000.1; -.
DR iPTMnet; O64763; -.
DR PaxDb; O64763; -.
DR PRIDE; O64763; -.
DR ProteomicsDB; 246580; -.
DR EnsemblPlants; AT2G35000.1; AT2G35000.1; AT2G35000.
DR GeneID; 818064; -.
DR Gramene; AT2G35000.1; AT2G35000.1; AT2G35000.
DR KEGG; ath:AT2G35000; -.
DR Araport; AT2G35000; -.
DR TAIR; locus:2044757; AT2G35000.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_035191_1_0_1; -.
DR InParanoid; O64763; -.
DR OMA; ERSAFPY; -.
DR OrthoDB; 1087626at2759; -.
DR PhylomeDB; O64763; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O64763; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64763; baseline and differential.
DR Genevisible; O64763; 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:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0010200; P:response to chitin; IEP:TAIR.
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; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..378
FT /note="E3 ubiquitin-protein ligase ATL9"
FT /id="PRO_0000030706"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 135..177
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 187..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 41880 MW; 7FEEC36D6BCDBDC6 CRC64;
MAILDTKSSR WIPHNLLFLL LLLLLQSVPY GFGQTQTTPP GTTKTKPNDP VVVVITVLFL
VIFFMVFGSI FCRRSNAQFS RSSIFRSTDA DAESQVVRIR RLTARGLDAE AIETFPTFLY
SEVKAVRIGK GGVECAVCLC EFEDDETLRL MPPCCHVFHA DCVDVWLSEH STCPLCRADL
VLNQQGDDDD STESYSGTDP GTISSSTDPE RGMVLESSDA HLLDAVTWSN SNITPRSKST
GLSSWQITGI LFPRSHSTGH SLIQPAGNLD RFTLRLPDDV RRQLMKTSRT MGHVALLPQA
RSSRSGYRSG SVGSERSAFP YGRKSNNNNR RLHSLSFSFS FRSGSVRSTF SGDAPKNLPT
SIEAGERSFE RLRPDERV
