ACD6_ARATH
ID ACD6_ARATH Reviewed; 670 AA.
AC Q8LPS2; B9DFF6; D9IWZ2; O23296; Q56YD7; Q682F8; Q8GW50;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Protein ACCELERATED CELL DEATH 6 {ECO:0000303|PubMed:10488236};
GN Name=ACD6 {ECO:0000303|PubMed:10488236};
GN OrderedLocusNames=At4g14400 {ECO:0000312|EMBL:AEE83439.1};
GN ORFNames=dl3240w {ECO:0000312|EMBL:CAB10219.1},
GN FCAALL.190 {ECO:0000312|EMBL:CAB78482.1};
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 {ECO:0000312|EMBL:AAM19791.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP TISSUE SPECIFICITY, AND INDUCTION BY VIRULENT PATHOGENS AND LIGHT.
RX PubMed=14507999; DOI=10.1105/tpc.015412;
RA Lu H., Rate D.N., Song J.T., Greenberg J.T.;
RT "ACD6, a novel ankyrin protein, is a regulator and an effector of salicylic
RT acid signaling in the Arabidopsis defense response.";
RL Plant Cell 15:2408-2420(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-583, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia, and cv. Ei-2;
RX PubMed=20520716; DOI=10.1038/nature09083;
RA Todesco M., Balasubramanian S., Hu T.T., Traw M.B., Horton M., Epple P.,
RA Kuhns C., Sureshkumar S., Schwartz C., Lanz C., Laitinen R.A.E., Huang Y.,
RA Chory J., Lipka V., Borevitz J.O., Dangl J.L., Bergelson J., Nordborg M.,
RA Weigel D.;
RT "Natural allelic variation underlying a major fitness trade-off in
RT Arabidopsis thaliana.";
RL Nature 465:632-636(2010).
RN [10]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10488236; DOI=10.2307/3871047;
RA Rate D.N., Cuenca J.V., Bowman G.R., Guttman D.S., Greenberg J.T.;
RT "The gain-of-function Arabidopsis acd6 mutant reveals novel regulation and
RT function of the salicylic acid signaling pathway in controlling cell death,
RT defenses, and cell growth.";
RL Plant Cell 11:1695-1708(1999).
RN [11]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11722764; DOI=10.1046/j.1365-313x.2001.01158.x;
RA Vanacker H., Lu H., Rate D.N., Greenberg J.T.;
RT "A role for salicylic acid and NPR1 in regulating cell growth in
RT Arabidopsis.";
RL Plant J. 28:209-216(2001).
RN [12]
RP FUNCTION, MUTAGENESIS OF GLY-73; ALA-142; ALA-186; ALA-269; LEU-300;
RP GLY-303; GLY-307; GLY-311; GLU-348; ALA-498; ALA-508; SER-550; LEU-557;
RP LEU-591 AND SER-638, AND SUBCELLULAR LOCATION.
RX PubMed=16297071; DOI=10.1111/j.1365-313x.2005.02567.x;
RA Lu H., Liu Y., Greenberg J.T.;
RT "Structure-function analysis of the plasma membrane- localized Arabidopsis
RT defense component ACD6.";
RL Plant J. 44:798-809(2005).
RN [13]
RP FUNCTION.
RX PubMed=19144005; DOI=10.1111/j.1365-313x.2009.03791.x;
RA Lu H., Salimian S., Gamelin E., Wang G., Fedorowski J., LaCourse W.,
RA Greenberg J.T.;
RT "Genetic analysis of acd6-1 reveals complex defense networks and leads to
RT identification of novel defense genes in Arabidopsis.";
RL Plant J. 58:401-412(2009).
RN [14]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=19959255; DOI=10.1016/j.jplph.2009.11.003;
RA Miura K., Ohta M.;
RT "SIZ1, a small ubiquitin-related modifier ligase, controls cold signaling
RT through regulation of salicylic acid accumulation.";
RL J. Plant Physiol. 167:555-560(2010).
RN [15]
RP MUTAGENESIS OF GLY-303; GLY-307; GLU-348 AND LEU-591, SUBCELLULAR LOCATION,
RP SUBUNIT, UBIQUITINATION, AND DEGRADATION BY PROTEASOME.
RC STRAIN=cv. Columbia;
RX PubMed=24923602; DOI=10.1093/mp/ssu072;
RA Zhang Z., Shrestha J., Tateda C., Greenberg J.T.;
RT "Salicylic acid signaling controls the maturation and localization of the
RT arabidopsis defense protein ACCELERATED CELL DEATH6.";
RL Mol. Plant 7:1365-1383(2014).
CC -!- FUNCTION: Dose-dependent activator of the defense response against
CC virulent pathogens, including bacteria, fungi and oomycetes, that acts
CC in a positive feedback loop with the defense signal salicylic acid (SA)
CC (PubMed:14507999, PubMed:20520716, PubMed:10488236, PubMed:16297071,
CC PubMed:19144005). Regulates the salicylic acid (SA) signaling pathway
CC leading to cell death and modulating cell fate (e.g. cell enlargement
CC and/or cell division) (PubMed:14507999, PubMed:10488236,
CC PubMed:11722764). In response to SA signaling, triggers the
CC accumulation of FLS2 at the plasma membrane, thus priming defenses
CC (PubMed:24923602). Involved in SA-dependent freezing signaling and
CC tolerance (PubMed:19959255). {ECO:0000269|PubMed:10488236,
CC ECO:0000269|PubMed:11722764, ECO:0000269|PubMed:14507999,
CC ECO:0000269|PubMed:16297071, ECO:0000269|PubMed:19144005,
CC ECO:0000269|PubMed:19959255, ECO:0000269|PubMed:20520716,
CC ECO:0000269|PubMed:24923602}.
CC -!- SUBUNIT: Component of large complexes containing, at least, FLS2, HSP70
CC and ACD6 in endoplasmic reticulum, plasma membrane and soluble
CC fraction. Associated with HSP70 proteins during endoplasmic reticulum-
CC associated degradation (ERAD). Reduced complex levels upon
CC benzothiazole (BTH) treatment. {ECO:0000269|PubMed:24923602}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16297071,
CC ECO:0000269|PubMed:24923602}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16297071, ECO:0000269|PubMed:24923602}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:24923602}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:24923602}. Note=Constitutively undergoes
CC endoplasmic reticulum-associated degradation (ERAD), via ubiquitination
CC and subsequent degradation by the proteasome. During salicylic acid
CC (SA) signaling, the soluble pool decreases, whereas the plasma membrane
CC pool increases. {ECO:0000269|PubMed:24923602}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8LPS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LPS2-2; Sequence=VSP_057943;
CC -!- TISSUE SPECIFICITY: Basal expression requires light and salicylic acid
CC (SA). {ECO:0000269|PubMed:14507999}.
CC -!- DEVELOPMENTAL STAGE: Expression in leaves increases with age.
CC {ECO:0000269|PubMed:20520716}.
CC -!- INDUCTION: Accumulates in systemic uninfected tissues during
CC Pseudomonas syringae infection or upon benzothiazole (BTH) treatment.
CC Induced by light, but repressed by dark (PubMed:14507999). Accumulates
CC upon MG132 treatment, a proteasome inhibitor. Target of endoplasmic
CC reticulum-associated degradation (ERAD) when ubiquitinated
CC (PubMed:24923602). {ECO:0000269|PubMed:14507999,
CC ECO:0000269|PubMed:24923602}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:24923602}.
CC -!- DISRUPTION PHENOTYPE: Reduced responsiveness to benzothiazole (BTH) and
CC upon P. syringae infection with reduced salicylic acid (SA) levels and
CC increased disease susceptibility and attenuated defenses
CC (PubMed:14507999). Increased sensitivity to biotrophic fungi (e.g.
CC Golovinomyces orontii T1 and G. cichoracearum UCSC1), biotrophic
CC oomycetes (e.g. Hyaloperonospora arabidopsidis Noco2) and hemi-
CC biotrophic bacteria (e.g. Pseudomonas syringae pv. tomato DC3000)
CC (PubMed:20520716). {ECO:0000269|PubMed:14507999,
CC ECO:0000269|PubMed:20520716}.
CC -!- MISCELLANEOUS: Sequence variations impacting defense responses are
CC observed between cultivars. Enhanced resistance is correlated with a
CC substantial reduction in vegetative biomass.
CC {ECO:0000269|PubMed:20520716}.
CC -!- MISCELLANEOUS: The dominant gain-of-function mutant acd6-1 and over-
CC expressing plant ACD6-o is dwarf and shows spontaneous cell death and
CC increased disease resistance, as well as increased defenses and better
CC responsiveness to salicylic acid (SA). These symptoms are SA-dependent
CC (PubMed:14507999, PubMed:20520716, PubMed:10488236, PubMed:16297071,
CC PubMed:19144005). In acd6-1, constitutively high free and total SA
CC levels leading to collapsed dead cells with adjacent enlarged cells in
CC the palisade parenchyma cell layer. This phenotype is absent in NahG
CC background, in which SA is degraded (PubMed:11722764). Strong
CC accumulation of camalexin (an anti-fungal compound) and SA in acd6-1
CC (PubMed:19144005). The mutant acd6-1 exhibits freezing sensitivity,
CC this sensitivity is suppressed in nahG background (PubMed:19959255).
CC {ECO:0000269|PubMed:10488236, ECO:0000269|PubMed:11722764,
CC ECO:0000269|PubMed:14507999, ECO:0000269|PubMed:16297071,
CC ECO:0000269|PubMed:19144005, ECO:0000269|PubMed:19959255,
CC ECO:0000269|PubMed:20520716}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10219.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78482.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY344843; AAQ24110.1; -; mRNA.
DR EMBL; Z97336; CAB10219.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161538; CAB78482.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83437.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83438.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83439.1; -; Genomic_DNA.
DR EMBL; AK119077; BAC43653.1; -; mRNA.
DR EMBL; AY094416; AAM19791.1; -; mRNA.
DR EMBL; BT002281; AAN72292.1; -; mRNA.
DR EMBL; AK316751; BAH19473.1; -; mRNA.
DR EMBL; AK175409; BAD43172.1; -; mRNA.
DR EMBL; AK176809; BAD44572.1; -; mRNA.
DR EMBL; AK221386; BAD94307.1; -; mRNA.
DR EMBL; HM214854; ADJ38625.1; -; Genomic_DNA.
DR EMBL; HM214855; ADJ38626.1; -; Genomic_DNA.
DR PIR; A71406; A71406.
DR RefSeq; NP_567430.1; NM_117519.4. [Q8LPS2-1]
DR RefSeq; NP_849381.1; NM_179050.2. [Q8LPS2-2]
DR RefSeq; NP_849382.1; NM_179051.1. [Q8LPS2-2]
DR AlphaFoldDB; Q8LPS2; -.
DR SMR; Q8LPS2; -.
DR STRING; 3702.AT4G14400.1; -.
DR TCDB; 9.A.43.1.14; the cadmium tolerance efflux pump (ctep) family.
DR iPTMnet; Q8LPS2; -.
DR PaxDb; Q8LPS2; -.
DR PRIDE; Q8LPS2; -.
DR ProteomicsDB; 244547; -. [Q8LPS2-1]
DR DNASU; 827085; -.
DR EnsemblPlants; AT4G14400.1; AT4G14400.1; AT4G14400. [Q8LPS2-1]
DR EnsemblPlants; AT4G14400.2; AT4G14400.2; AT4G14400. [Q8LPS2-2]
DR EnsemblPlants; AT4G14400.3; AT4G14400.3; AT4G14400. [Q8LPS2-2]
DR GeneID; 827085; -.
DR Gramene; AT4G14400.1; AT4G14400.1; AT4G14400. [Q8LPS2-1]
DR Gramene; AT4G14400.2; AT4G14400.2; AT4G14400. [Q8LPS2-2]
DR Gramene; AT4G14400.3; AT4G14400.3; AT4G14400. [Q8LPS2-2]
DR KEGG; ath:AT4G14400; -.
DR Araport; AT4G14400; -.
DR TAIR; locus:2129690; AT4G14400.
DR eggNOG; KOG0504; Eukaryota.
DR InParanoid; Q8LPS2; -.
DR OrthoDB; 1156472at2759; -.
DR PhylomeDB; Q8LPS2; -.
DR PRO; PR:Q8LPS2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LPS2; baseline and differential.
DR Genevisible; Q8LPS2; AT.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0071446; P:cellular response to salicylic acid stimulus; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1902290; P:positive regulation of defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0050826; P:response to freezing; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IMP:TAIR.
DR GO; GO:0009615; P:response to virus; IEP:TAIR.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR032846; ACD6.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR026961; PGG_dom.
DR PANTHER; PTHR24177:SF322; PTHR24177:SF322; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13962; PGG; 1.
DR SMART; SM00248; ANK; 9.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cell membrane; Endoplasmic reticulum;
KW Membrane; Plant defense; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..670
FT /note="Protein ACCELERATED CELL DEATH 6"
FT /id="PRO_0000434534"
FT TOPO_DOM 1..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..492
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..537
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..577
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..638
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..670
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 66..95
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 100..129
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 134..163
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 182..211
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 216..248
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 260..290
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 295..325
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 329..358
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT REPEAT 363..391
FT /note="ANK 9"
FT /evidence="ECO:0000255"
FT REPEAT 399..428
FT /note="ANK 10"
FT /evidence="ECO:0000255"
FT REGION 18..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform 2)"
FT /id="VSP_057943"
FT MUTAGEN 73
FT /note="G->D: In E46; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility."
FT /evidence="ECO:0000269|PubMed:16297071"
FT MUTAGEN 142
FT /note="A->V: In E11; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility."
FT /evidence="ECO:0000269|PubMed:16297071"
FT MUTAGEN 186
FT /note="A->V: In E19; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility."
FT /evidence="ECO:0000269|PubMed:16297071"
FT MUTAGEN 269
FT /note="A->V: In E38; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility."
FT /evidence="ECO:0000269|PubMed:16297071"
FT MUTAGEN 300
FT /note="L->F: In E3; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility."
FT /evidence="ECO:0000269|PubMed:16297071"
FT MUTAGEN 303
FT /note="G->E: In E4; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility.
FT Aberrant complex formation leading to reduced subcellular
FT location at the plasma membrane."
FT /evidence="ECO:0000269|PubMed:16297071,
FT ECO:0000269|PubMed:24923602"
FT MUTAGEN 307
FT /note="G->E: In E1; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility.
FT Aberrant complex formation leading to reduced subcellular
FT location at the plasma membrane."
FT /evidence="ECO:0000269|PubMed:16297071,
FT ECO:0000269|PubMed:24923602"
FT MUTAGEN 311
FT /note="G->E: In E7; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility."
FT /evidence="ECO:0000269|PubMed:16297071"
FT MUTAGEN 348
FT /note="E->K: In E44; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility.
FT Aberrant complex formation leading to reduced subcellular
FT location at the plasma membrane."
FT /evidence="ECO:0000269|PubMed:16297071,
FT ECO:0000269|PubMed:24923602"
FT MUTAGEN 498
FT /note="A->T: In E27; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility."
FT /evidence="ECO:0000269|PubMed:16297071"
FT MUTAGEN 508
FT /note="A->T: In E35; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility."
FT /evidence="ECO:0000269|PubMed:16297071"
FT MUTAGEN 550
FT /note="S->F: In E14; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility."
FT /evidence="ECO:0000269|PubMed:16297071"
FT MUTAGEN 557
FT /note="L->F: In E40; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility."
FT /evidence="ECO:0000269|PubMed:16297071"
FT MUTAGEN 591
FT /note="L->F: In acd6-1; gain-of-function leading to SA-
FT dependent spontaneous cell death and increased disease
FT resistance. Stronger accumulation at the plasma membrane."
FT /evidence="ECO:0000269|PubMed:16297071,
FT ECO:0000269|PubMed:24923602"
FT MUTAGEN 638
FT /note="S->F: In E25; suppression of acd6-1-conferred
FT phenotypes and increased P. syringae susceptibility."
FT /evidence="ECO:0000269|PubMed:16297071"
FT CONFLICT 347
FT /note="K -> E (in Ref. 8; BAD94307)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="R -> G (in Ref. 5; BAC43653)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 73527 MW; 9EAD26D13EE25BB5 CRC64;
MDSSGADLDR IEAQRSMLVS HDQRKDFSHS GGVGTTSPTG DTEPVPKFRT NLKLSDLFAL
PGEDVEMTPE IFGGMSNGEK ECLEKLRSNG TPMERVKSNT GDSILHIAAK WGHLELVKEI
IFECPCLLFE QNSSRQTPLH VATHGGHTKV VEALVASVTS ALASLSTEES EGLNPHVLKD
EDGNTALYYA IEGRYLEMAT CLVNADKDAP FLGNNKGISS LYEAVDAGNK FEDLVKAILK
TTDDNVDREV RKFNLDSKLQ GNKHLAHVAL KAKSIGVLDV ILDEYPSLMD EQDEDGRTCL
SYGASIGYYK GLCNILNRST KGVYVCDQDG SFPIHSAAKN EHYEIIKEFI KRCPASKYLL
NRLGQNILHV AAKNEASLTA YMLMHDKDTK HLGVGQDVDG NTPLHLAVMN WDFDSITCLA
SRNHEILKLR NKSGLRARDI AESEVKPNYI FHERWTLALL LYAIHSSGFE SVKSLTIQSV
PLDPKKNRHY VNALLVVAAL VATVTFAAGF TIPGGYISDS KKPNLGRATL ATNPTLFIFL
LFDILAMQSS VATICTLIWA QLGDLALILK SLHVALPLLL FSLLCMPVAF LFGVITAIAH
VKWLLVTISI ISGGFFLFAI FILGPHVMLQ RSHLPPSSGI FLKTFMLTID ISELFVILIK
ACFGCVACSE
