ATL55_ARATH
ID ATL55_ARATH Reviewed; 301 AA.
AC Q9LX93;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=E3 ubiquitin-protein ligase RING1;
DE EC=2.3.2.27 {ECO:0000269|PubMed:18643987};
DE AltName: Full=RING-H2 finger protein ATL55;
DE AltName: Full=RING-type E3 ubiquitin transferase ATL55 {ECO:0000305};
GN Name=ATL55; Synonyms=RING1; OrderedLocusNames=At5g10380;
GN ORFNames=F12B17_270;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS
RP OF CYS-135 AND CYS-138, AND DISRUPTION PHENOTYPE.
RX PubMed=18643987; DOI=10.1111/j.1365-313x.2008.03625.x;
RA Lin S.S., Martin R., Mongrand S., Vandenabeele S., Chen K.C., Jang I.C.,
RA Chua N.H.;
RT "RING1 E3 ligase localizes to plasma membrane lipid rafts to trigger FB1-
RT induced programmed cell death in Arabidopsis.";
RL Plant J. 56:550-561(2008).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that may be involved in positive
CC regulation of programmed cell death (PCD) by facilitating degradation
CC of negative regulators of PCD. May be involved in the early steps of
CC the plant defense signaling pathway. Undergoes auto-ubiquitination.
CC {ECO:0000269|PubMed:18643987}.
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:18643987};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18643987};
CC Single-pass membrane protein {ECO:0000269|PubMed:18643987}.
CC -!- INDUCTION: Up-regulated by chitin. Up-regulated by the fungal toxin
CC fumonisin B1 (FB1) treatment and pathogen infection.
CC {ECO:0000269|PubMed:17722694, ECO:0000269|PubMed:18643987}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- PTM: Auto-ubiquitinated.
CC -!- DISRUPTION PHENOTYPE: Hyposensitivity to the fungal toxin fumonisin B1
CC (FB1). {ECO:0000269|PubMed:18643987}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC {ECO:0000305}.
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DR EMBL; AL353995; CAB89405.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91534.1; -; Genomic_DNA.
DR EMBL; AK176500; BAD44263.1; -; mRNA.
DR PIR; T50001; T50001.
DR RefSeq; NP_196600.1; NM_121076.3.
DR AlphaFoldDB; Q9LX93; -.
DR SMR; Q9LX93; -.
DR BioGRID; 16180; 7.
DR IntAct; Q9LX93; 4.
DR STRING; 3702.AT5G10380.1; -.
DR iPTMnet; Q9LX93; -.
DR PaxDb; Q9LX93; -.
DR PRIDE; Q9LX93; -.
DR ProteomicsDB; 246565; -.
DR EnsemblPlants; AT5G10380.1; AT5G10380.1; AT5G10380.
DR GeneID; 830902; -.
DR Gramene; AT5G10380.1; AT5G10380.1; AT5G10380.
DR KEGG; ath:AT5G10380; -.
DR Araport; AT5G10380; -.
DR TAIR; locus:2142449; AT5G10380.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_967562_0_0_1; -.
DR InParanoid; Q9LX93; -.
DR OMA; TEPPHQE; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q9LX93; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LX93; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LX93; baseline and differential.
DR Genevisible; Q9LX93; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IMP:TAIR.
DR GO; GO:0012501; P:programmed cell death; IC:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; IEP:UniProtKB.
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 1: Evidence at protein level;
KW Apoptosis; Cell membrane; Membrane; Metal-binding; Plant defense;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..301
FT /note="E3 ubiquitin-protein ligase RING1"
FT /id="PRO_0000055810"
FT TRANSMEM 46..66
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 188..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 135
FT /note="C->S: Abolishes the E3 ligase activity; when
FT associated with Ser-138."
FT /evidence="ECO:0000269|PubMed:18643987"
FT MUTAGEN 138
FT /note="C->S: Abolishes the E3 ligase activity; when
FT associated with Ser-135."
FT /evidence="ECO:0000269|PubMed:18643987"
SQ SEQUENCE 301 AA; 34042 MW; E72189674B7E1471 CRC64;
MAFNHRKMLL SCLQFKDLRF CFRQYPPPPP PPPPPRELSL LLPTSICVVG SIILFLFLVF
FLYLHITQQR RISAASVTPG DTNQQEDEDE TEERDFSDFH HVWQIPTVGL HRSAINSITV
VGFKKGEGII DGTECSVCLN EFEEDESLRL LPKCSHAFHL NCIDTWLLSH KNCPLCRAPV
LLITEPPHQE TETNHQPDSE SSNDLRGRQD SSRSRRNHNI FLPRAQSDLA NYCGSGRVEN
VRRSFSIGGS LSLCDGINNA TRSGRQFYTS FSANLFSSSR RVRNEQPIPQ NQMPSVTGNT
S
