SG101_ARATH
ID SG101_ARATH Reviewed; 537 AA.
AC Q4F883; F4K898; Q8LCZ8; Q9LFR2;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Senescence-associated carboxylesterase 101;
DE EC=3.1.1.1;
DE Flags: Precursor;
GN Name=SAG101; OrderedLocusNames=At5g14930; ORFNames=F2G14.50;
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] (ISOFORM 1), FUNCTION, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11971136; DOI=10.1105/tpc.010422;
RA He Y., Gan S.;
RT "A gene encoding an acyl hydrolase is involved in leaf senescence in
RT Arabidopsis.";
RL Plant Cell 14:805-815(2002).
RN [2]
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 [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] (ISOFORM 2).
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EDS1.
RC STRAIN=cv. Columbia;
RX PubMed=16040633; DOI=10.1105/tpc.105.033910;
RA Feys B.J., Wiermer M., Bhat R.A., Moisan L.J., Medina-Escobar N., Neu C.,
RA Cabral A., Parker J.E.;
RT "Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and signals within an
RT ENHANCED DISEASE SUSCEPTIBILITY1 complex in plant innate immunity.";
RL Plant Cell 17:2601-2613(2005).
RN [6]
RP INDUCTION BY SENESCENCE, AND DEVELOPMENTAL STAGE.
RX PubMed=19143996; DOI=10.1111/j.1365-313x.2008.03782.x;
RA Ay N., Irmler K., Fischer A., Uhlemann R., Reuter G., Humbeck K.;
RT "Epigenetic programming via histone methylation at WRKY53 controls leaf
RT senescence in Arabidopsis thaliana.";
RL Plant J. 58:333-346(2009).
RN [7]
RP FUNCTION, AND INTERACTION WITH EDS1.
RX PubMed=21434927; DOI=10.1111/j.1469-8137.2011.03675.x;
RA Rietz S., Stamm A., Malonek S., Wagner S., Becker D., Medina-Escobar N.,
RA Vlot A.C., Feys B.J., Niefind K., Parker J.E.;
RT "Different roles of Enhanced Disease Susceptibility1 (EDS1) bound to and
RT dissociated from Phytoalexin Deficient4 (PAD4) in Arabidopsis immunity.";
RL New Phytol. 191:107-119(2011).
RN [8]
RP FUNCTION, SUBUNIT, INTERACTION WITH EDS1, AND SUBCELLULAR LOCATION.
RX PubMed=22072959; DOI=10.1371/journal.ppat.1002318;
RA Zhu S., Jeong R.-D., Venugopal S.C., Lapchyk L., Navarre D., Kachroo A.,
RA Kachroo P.;
RT "SAG101 forms a ternary complex with EDS1 and PAD4 and is required for
RT resistance signaling against turnip crinkle virus.";
RL PLoS Pathog. 7:E1002318-E1002318(2011).
RN [9]
RP FUNCTION.
RX PubMed=23356583; DOI=10.1111/nph.12155;
RA Langenbach C., Campe R., Schaffrath U., Goellner K., Conrath U.;
RT "UDP-glucosyltransferase UGT84A2/BRT1 is required for Arabidopsis nonhost
RT resistance to the Asian soybean rust pathogen Phakopsora pachyrhizi.";
RL New Phytol. 198:536-545(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) IN COMPLEX WITH EDS1, AND INTERACTION
RP WITH EDS1.
RX PubMed=21301097; DOI=10.1107/s1744309110051249;
RA Wagner S., Rietz S., Parker J.E., Niefind K.;
RT "Crystallization and preliminary crystallographic analysis of Arabidopsis
RT thaliana EDS1, a key component of plant immunity, in complex with its
RT signalling partner SAG101.";
RL Acta Crystallogr. F 67:245-248(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-537 IN COMPLEX WITH EDS1, AND
RP MUTAGENESIS OF LEU-12; LEU-21; ILE-141 AND TYR-306.
RX PubMed=24331460; DOI=10.1016/j.chom.2013.11.006;
RA Wagner S., Stuttmann J., Rietz S., Guerois R., Brunstein E., Bautor J.,
RA Niefind K., Parker J.E.;
RT "Structural basis for signaling by exclusive EDS1 heteromeric complexes
RT with SAG101 or PAD4 in plant innate immunity.";
RL Cell Host Microbe 14:619-630(2013).
CC -!- FUNCTION: Acyl hydrolase that triggers the leaf senescence onset. Can
CC use triolein as substrate to produce oleic acids.
CC -!- FUNCTION: Involved in the EDS1-dependent intrinsic and indispensable
CC resistance signaling pathway; together with PAD4, required for
CC programmed cell death triggered by RPS4 in response to avirulent
CC pathogens (e.g. P.syringae pv. tomato strain DC3000 and H.parasitica
CC isolates CALA2 and EMWA1) and in restricting the growth of virulent
CC pathogens (e.g. H.parasitica isolates NOCO2 and P.syringae pv. tomato
CC strain DC3000 avrRps4). Contributes in reinforcing the immune response
CC around hypersensitive response foci (PubMed:21434927). Regulates the
CC nuclear localization of EDS1. Essential for the RPP8/HRT-mediated
CC resistance to the turnip crinkle virus (TCV). Involved in the post-
CC invasion resistance to P.pachyrhizi in the mesophyll.
CC {ECO:0000269|PubMed:21434927, ECO:0000269|PubMed:22072959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC Evidence={ECO:0000269|PubMed:11971136};
CC -!- SUBUNIT: Part of a nuclear complex made of EDS1, PAD4 and SAG101, that
CC can be redirected to the cytoplasm in the presence of an extranuclear
CC form of EDS1 (PubMed:22072959). Interacts directly with EDS1.
CC {ECO:0000269|PubMed:16040633, ECO:0000269|PubMed:21301097,
CC ECO:0000269|PubMed:21434927, ECO:0000269|PubMed:22072959,
CC ECO:0000269|PubMed:24331460}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:22072959}. Cytoplasm
CC {ECO:0000269|PubMed:22072959}. Note=Can move to the cytoplasm when in
CC complex with PAD4 and EDS1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q4F883-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4F883-2; Sequence=VSP_047931, VSP_047932;
CC -!- TISSUE SPECIFICITY: Expressed in senescing leaves.
CC {ECO:0000269|PubMed:11971136}.
CC -!- DEVELOPMENTAL STAGE: Not expressed until the onset of senescence in
CC leaves. {ECO:0000269|PubMed:11971136, ECO:0000269|PubMed:19143996}.
CC -!- INDUCTION: Specifically induced during senescence via a complex
CC epigenetic processe involving histone methylation.
CC {ECO:0000269|PubMed:19143996}.
CC -!- DISRUPTION PHENOTYPE: Delayed onset of leaf senescence (about 4 days
CC later). Reduced resistance to both virulent and avirulent pathogens
CC (Pseudomonas syringae pv. tomato and Hyaloperonospora parasitica).
CC {ECO:0000269|PubMed:11971136}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC01812.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ103714; AAZ15704.1; -; mRNA.
DR EMBL; AL391146; CAC01812.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92091.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92092.1; -; Genomic_DNA.
DR EMBL; AY086301; AAM64373.1; -; mRNA.
DR PIR; T51438; T51438.
DR RefSeq; NP_568307.3; NM_121497.5. [Q4F883-1]
DR RefSeq; NP_851039.1; NM_180708.2. [Q4F883-2]
DR PDB; 4NFU; X-ray; 2.21 A; B=2-537.
DR PDBsum; 4NFU; -.
DR AlphaFoldDB; Q4F883; -.
DR SMR; Q4F883; -.
DR BioGRID; 16622; 2.
DR ComplexPortal; CPX-1321; EDS1-SAG101 complex, variant EDS1.
DR ComplexPortal; CPX-1325; EDS1-PAD4-SAG101 complex, variant EDS1.
DR ComplexPortal; CPX-1617; EDS1-SAG101 complex, variant EDS1B.
DR ComplexPortal; CPX-1619; EDS1-PAD4-SAG101 complex, variant EDS1B.
DR STRING; 3702.AT5G14930.2; -.
DR ESTHER; arath-At5g14930; Plant_lipase_EDS1-like.
DR iPTMnet; Q4F883; -.
DR PaxDb; Q4F883; -.
DR PRIDE; Q4F883; -.
DR ProteomicsDB; 234488; -. [Q4F883-1]
DR EnsemblPlants; AT5G14930.1; AT5G14930.1; AT5G14930. [Q4F883-2]
DR EnsemblPlants; AT5G14930.2; AT5G14930.2; AT5G14930. [Q4F883-1]
DR GeneID; 831345; -.
DR Gramene; AT5G14930.1; AT5G14930.1; AT5G14930. [Q4F883-2]
DR Gramene; AT5G14930.2; AT5G14930.2; AT5G14930. [Q4F883-1]
DR KEGG; ath:AT5G14930; -.
DR Araport; AT5G14930; -.
DR TAIR; locus:2147825; AT5G14930.
DR eggNOG; ENOG502QTKG; Eukaryota.
DR HOGENOM; CLU_016367_3_0_1; -.
DR InParanoid; Q4F883; -.
DR OMA; KISMAYI; -.
DR OrthoDB; 405905at2759; -.
DR PhylomeDB; Q4F883; -.
DR BioCyc; ARA:AT5G14930-MON; -.
DR PRO; PR:Q4F883; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q4F883; baseline and differential.
DR Genevisible; Q4F883; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0106093; C:EDS1 disease-resistance complex; IDA:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:TAIR.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0007568; P:aging; IMP:TAIR.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0060866; P:leaf abscission; IMP:TAIR.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009626; P:plant-type hypersensitive response; IC:ComplexPortal.
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:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
DR GO; GO:1900057; P:positive regulation of leaf senescence; IMP:UniProtKB.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:ComplexPortal.
DR DisProt; DP02640; -.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR041266; EDS1_EP.
DR InterPro; IPR002921; Fungal_lipase-like.
DR InterPro; IPR044603; SAG101-like.
DR PANTHER; PTHR46898; PTHR46898; 1.
DR Pfam; PF18117; EDS1_EP; 1.
DR Pfam; PF01764; Lipase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Nucleus; Plant defense;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..537
FT /note="Senescence-associated carboxylesterase 101"
FT /id="PRO_0000423498"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 130..131
FT /note="LL -> VI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047931"
FT VAR_SEQ 132..537
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_047932"
FT MUTAGEN 12
FT /note="L->A: No effect on interaction with EDS1; when
FT associated with A-21. No effect on interaction with EDS1;
FT when associated with A-21 and A-141. Loss of interaction
FT with EDS1; when associated with A-21; A-141 and A-306."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 21
FT /note="L->A: No effect on interaction with EDS1; when
FT associated with A-12. No effect on interaction with EDS1;
FT when associated with A-12 and A-141. Loss of interaction
FT with EDS1; when associated with A-12; A-141 and A-306."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 141
FT /note="I->A: No effect on interaction with EDS1; when
FT associated with A-12 and A-21. Loss of interaction with
FT EDS1; when associated with A-12; A-21 and A-306."
FT /evidence="ECO:0000269|PubMed:24331460"
FT MUTAGEN 306
FT /note="Y->A: Loss of interaction with EDS1; when associated
FT with A-12; A-21 and A-141."
FT /evidence="ECO:0000269|PubMed:24331460"
FT CONFLICT 40
FT /note="H -> Q (in Ref. 4; AAM64373)"
FT /evidence="ECO:0000305"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 21..33
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 273..286
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 287..294
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 295..316
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 335..342
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 344..361
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 364..373
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 375..395
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 408..417
FT /evidence="ECO:0007829|PDB:4NFU"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 421..428
FT /evidence="ECO:0007829|PDB:4NFU"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 444..460
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 466..488
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 502..514
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 520..526
FT /evidence="ECO:0007829|PDB:4NFU"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:4NFU"
SQ SEQUENCE 537 AA; 62066 MW; 03158AC6E636CDD5 CRC64;
MESSSSLKGS ALGKLVVTSG LLHSSWSKIL EIHNPPYSNH DPGLQVSKKK KDSGLEFQIH
REEKFTLVVF SAPPICRSSS SDSTLLHVKD KENPFPFLCS ENNPSFSLHT PAFNLFTSAS
TSLTYLKSEL LQTLKSEKPV IITGAALGGS VASLYTLWLL ETIEPTLKRP LCITFGSPLI
GDASLQQILE NSVRNSCFLH VVSAQTRIKM DFFKPFGTFL ICFDSGCVCI EDHVAVTELL
NGVHDSGLVD YSQVLNRLDQ SMLSLADSRL IPEDVIKGIE KRAEMKNLRF DMMFKKLNDM
KISMAYIEWY KKKCKEVKIG YYDRFKTQLA FPSKEFDINI KNHHKSELNR FWKSVVEEVE
RRPQSDASIL KRRFLFSGNN YRRMIEPLDI AEYYLEGRKE YRTTGRSHHY VMLEKWFGME
SILIEKERCK KRDLSDLLTF DSCFWAEVED SLIVINQLNT TVGMRDDVRE VLTRKLVEFE
GYVWEIITKR EVSPEIFLEE SSFMKWWKEY KKIKGFNSSY LTEFMNTRKY ESYGKSQ
