ATL23_ARATH
ID ATL23_ARATH Reviewed; 163 AA.
AC Q8L9W3; Q4FE34; Q9FHW6;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=E3 ubiquitin-protein ligase ATL23;
DE EC=2.3.2.27 {ECO:0000269|PubMed:15644464, ECO:0000269|PubMed:16339806};
DE AltName: Full=RING-H2 finger protein ATL23;
DE AltName: Full=RING-type E3 ubiquitin transferase ATL23 {ECO:0000305};
GN Name=ATL23; OrderedLocusNames=At5g42200; ORFNames=MJC20.31;
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], 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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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 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 [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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16339806; DOI=10.1104/pp.105.067983;
RA Kraft E., Stone S.L., Ma L., Su N., Gao Y., Lau O.-S., Deng X.-W.,
RA Callis J.;
RT "Genome analysis and functional characterization of the E2 and RING-type E3
RT ligase ubiquitination enzymes of Arabidopsis.";
RL Plant Physiol. 139:1597-1611(2005).
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase able to catalyze
CC polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8, UBC10,
CC UBC11, UBC28 and UBC29 in vitro. {ECO:0000269|PubMed:15644464,
CC ECO:0000269|PubMed:16339806}.
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 ECO:0000269|PubMed:16339806};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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; DQ086857; AAZ14061.1; -; Genomic_DNA.
DR EMBL; AB017067; BAB08453.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94778.1; -; Genomic_DNA.
DR EMBL; BT003837; AAO41888.1; -; mRNA.
DR EMBL; BT005191; AAO50724.1; -; mRNA.
DR EMBL; AY088186; AAM65729.1; -; mRNA.
DR RefSeq; NP_199035.1; NM_123585.4.
DR AlphaFoldDB; Q8L9W3; -.
DR SMR; Q8L9W3; -.
DR BioGRID; 19475; 1.
DR IntAct; Q8L9W3; 1.
DR STRING; 3702.AT5G42200.1; -.
DR PaxDb; Q8L9W3; -.
DR PRIDE; Q8L9W3; -.
DR EnsemblPlants; AT5G42200.1; AT5G42200.1; AT5G42200.
DR GeneID; 834225; -.
DR Gramene; AT5G42200.1; AT5G42200.1; AT5G42200.
DR KEGG; ath:AT5G42200; -.
DR Araport; AT5G42200; -.
DR TAIR; locus:2165735; AT5G42200.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_013137_15_5_1; -.
DR InParanoid; Q8L9W3; -.
DR OMA; MESQELW; -.
DR OrthoDB; 1411835at2759; -.
DR PhylomeDB; Q8L9W3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8L9W3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8L9W3; baseline and differential.
DR Genevisible; Q8L9W3; 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:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA: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; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..163
FT /note="E3 ubiquitin-protein ligase ATL23"
FT /id="PRO_0000055813"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 104..146
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 24
FT /note="G -> D (in Ref. 4; AAM65729)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="T -> A (in Ref. 4; AAM65729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 163 AA; 17757 MW; 4AA7E0FE8D3A6355 CRC64;
MHYTRISPAL VPSLSPTAAA ESSGGGTMIA TVFMALLLPC VGMCIVFLIY LFLLWCSTRR
RIERLRFAEP VKPVTGKGLS VLELEKIPKL TGRELAVIAR STECAVCLED IESGQSTRLV
PGCNHGFHQL CADTWLSNHT VCPVCRAELA PNLPQCNENQ SPC
