ATL6_ARATH
ID ATL6_ARATH Reviewed; 398 AA.
AC Q8RXX9; Q4FE31; Q9MA99; Q9XF65;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=E3 ubiquitin-protein ligase ATL6;
DE EC=2.3.2.27 {ECO:0000269|PubMed:15644464};
DE AltName: Full=RING-H2 finger protein ATL6;
DE AltName: Full=RING-type E3 ubiquitin transferase ATL6 {ECO:0000305};
DE Flags: Precursor;
GN Name=ATL6; OrderedLocusNames=At3g05200; ORFNames=T12H1.17;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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] OF 1-388.
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 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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
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).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [12]
RP FUNCTION.
RA Maekawa S., Sato T., Asada Y., Yasuda S., Yoshida M., Yamaguchi J.;
RT "SSV1 and ATL6 as C/N regulatory E3 ligase, are also involved in immune
RT response system in Arabidopsis.";
RL (In) Proceedings of the 20th international conference on Arabidopsis
RL research, abstract#322, Edinburgh (2009).
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 plant C/N response and the early steps of the
CC plant defense signaling pathway. {ECO:0000269|PubMed:15644464,
CC ECO:0000269|Ref.12}.
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 or cellulases elicitors.
CC {ECO:0000269|PubMed:10480382, 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF27026.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF132016; AAD33584.1; -; mRNA.
DR EMBL; DQ086860; AAZ14076.1; -; mRNA.
DR EMBL; AC009177; AAF27026.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE74204.1; -; Genomic_DNA.
DR EMBL; AY080617; AAL86301.1; -; mRNA.
DR RefSeq; NP_566249.1; NM_111393.3.
DR AlphaFoldDB; Q8RXX9; -.
DR SMR; Q8RXX9; -.
DR BioGRID; 5019; 6.
DR IntAct; Q8RXX9; 4.
DR STRING; 3702.AT3G05200.1; -.
DR iPTMnet; Q8RXX9; -.
DR PaxDb; Q8RXX9; -.
DR PRIDE; Q8RXX9; -.
DR ProteomicsDB; 246574; -.
DR EnsemblPlants; AT3G05200.1; AT3G05200.1; AT3G05200.
DR GeneID; 819684; -.
DR Gramene; AT3G05200.1; AT3G05200.1; AT3G05200.
DR KEGG; ath:AT3G05200; -.
DR Araport; AT3G05200; -.
DR TAIR; locus:2096309; AT3G05200.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_035191_1_0_1; -.
DR InParanoid; Q8RXX9; -.
DR OMA; FRHCSGV; -.
DR OrthoDB; 776201at2759; -.
DR PhylomeDB; Q8RXX9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8RXX9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8RXX9; baseline and differential.
DR Genevisible; Q8RXX9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0098542; P:defense response to other organism; IEP: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; Phosphoprotein; Plant defense; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..398
FT /note="E3 ubiquitin-protein ligase ATL6"
FT /id="PRO_0000030707"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 128..170
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 368..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 54
FT /note="V -> E (in Ref. 1; AAD33584)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="M -> R (in Ref. 1; AAD33584)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="Y -> N (in Ref. 1; AAD33584)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="A -> V (in Ref. 1; AAD33584)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 43274 MW; 150DD04311F587C2 CRC64;
MRSSDHMAFA GVLPIVFLLI LSSADLAASQ SQPGPTNQPY NYGRLSPAMA VIVVILIAAL
FFMGFFSIYF RHCSGVPDAG VSPAGGARSR ATVNAAARGL DVSVVETFPT FLYSDVKTQK
LGKGELECAI CLNEFEDDET LRLLPKCDHV FHPHCIDAWL EAHVTCPVCR ANLAEQVAEG
ESVEPGGTEP DLELQQVVVN PEPVVTAPVP EQLVTSEVDS RRLPGVPVDL KRVKFSRSHT
TGHSVVQPGE CTERFTLRLP EDVRKRIMKD WKLNRTNSLL VLPRGGSSRR GKPIDRSRAR
SDRWLFRKTP SFLWRSRDDG SIRLGATGSV RASAVPNSTG SDSVRAGDRW AFLRNASFLW
RNSSVHVPRG GVNKDGEGTS VKSTGASGST SGSVRLPV
