ATL44_ARATH
ID ATL44_ARATH Reviewed; 185 AA.
AC O22755;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable E3 ubiquitin-protein ligase ATL44 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-H2 finger A3a {ECO:0000303|PubMed:9781696};
DE AltName: Full=RING-H2 finger protein ATL44 {ECO:0000305};
DE AltName: Full=RING-H2 zinc finger protein RHA3a {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL44 {ECO:0000305};
GN Name=ATL44 {ECO:0000303|PubMed:16557337};
GN Synonyms=RHA3A {ECO:0000303|PubMed:9781696};
GN OrderedLocusNames=At2g17450 {ECO:0000312|Araport:AT2G17450};
GN ORFNames=F5J6.22, MJB20 {ECO:0000312|EMBL:AAD32903.1};
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], AND TISSUE SPECIFICITY.
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 [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;
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 [5]
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 [6]
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 [7]
RP FUNCTION, MUTAGENESIS OF ILE-104, 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.7).
CC Triggers the monoubiquitination of phosphorylated BIK1 in response to
CC pathogen-associated molecular pattern (PAMP) detection (Ref.7).
CC {ECO:0000269|Ref.7}.
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.7}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, flowers and green siliques.
CC {ECO:0000269|PubMed:9781696}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- PTM: Auto-monoubiquitination. {ECO:0000269|Ref.7}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC {ECO:0000305}.
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DR EMBL; AF078824; AAC68673.1; -; mRNA.
DR EMBL; AC007584; AAD32903.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06631.1; -; Genomic_DNA.
DR EMBL; AF370239; AAK44054.1; -; mRNA.
DR EMBL; AY062961; AAL33807.1; -; mRNA.
DR PIR; T51844; T51844.
DR RefSeq; NP_179337.1; NM_127300.4.
DR AlphaFoldDB; O22755; -.
DR SMR; O22755; -.
DR STRING; 3702.AT2G17450.1; -.
DR PaxDb; O22755; -.
DR PRIDE; O22755; -.
DR EnsemblPlants; AT2G17450.1; AT2G17450.1; AT2G17450.
DR GeneID; 816251; -.
DR Gramene; AT2G17450.1; AT2G17450.1; AT2G17450.
DR KEGG; ath:AT2G17450; -.
DR Araport; AT2G17450; -.
DR TAIR; locus:2053863; AT2G17450.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_013137_9_1_1; -.
DR OMA; RRYANSP; -.
DR OrthoDB; 1348127at2759; -.
DR PhylomeDB; O22755; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O22755; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22755; baseline and differential.
DR Genevisible; O22755; 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:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IGI: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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..185
FT /note="Probable E3 ubiquitin-protein ligase ATL44"
FT /id="PRO_0000055775"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 102..144
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 163..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 104
FT /note="I->A: Impaired E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|Ref.7"
SQ SEQUENCE 185 AA; 19937 MW; C3258EA5598DD9ED CRC64;
MTRPSRLLET AAPPPQPSEE MIAAESDMVV ILSALLCALI CVAGLAAVVR CAWLRRFTAG
GDSPSPNKGL KKKALQSLPR STFTAAESTS GAAAEEGDST ECAICLTDFA DGEEIRVLPL
CGHSFHVECI DKWLVSRSSC PSCRRILTPV RCDRCGHAST AEMKDQAHRH QHHQHSSTTI
PTFLP
