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Senescence-associated carboxylesterase 101 (EC 3.1.1.1)

 SG101_ARATH             Reviewed;         537 AA.
Q4F883; F4K898; Q8LCZ8; Q9LFR2;
18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
30-AUG-2005, sequence version 1.
30-AUG-2017, entry version 84.
RecName: Full=Senescence-associated carboxylesterase 101;
EC=3.1.1.1;
Flags: Precursor;
Name=SAG101; OrderedLocusNames=At5g14930; ORFNames=F2G14.50;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION
PHENOTYPE, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND TISSUE
SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=11971136; DOI=10.1105/tpc.010422;
He Y., Gan S.;
"A gene encoding an acyl hydrolase is involved in leaf senescence in
Arabidopsis.";
Plant Cell 14:805-815(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EDS1.
STRAIN=cv. Columbia;
PubMed=16040633; DOI=10.1105/tpc.105.033910;
Feys B.J., Wiermer M., Bhat R.A., Moisan L.J., Medina-Escobar N.,
Neu C., Cabral A., Parker J.E.;
"Arabidopsis SENESCENCE-ASSOCIATED GENE101 stabilizes and signals
within an ENHANCED DISEASE SUSCEPTIBILITY1 complex in plant innate
immunity.";
Plant Cell 17:2601-2613(2005).
[6]
INDUCTION BY SENESCENCE, AND DEVELOPMENTAL STAGE.
PubMed=19143996; DOI=10.1111/j.1365-313X.2008.03782.x;
Ay N., Irmler K., Fischer A., Uhlemann R., Reuter G., Humbeck K.;
"Epigenetic programming via histone methylation at WRKY53 controls
leaf senescence in Arabidopsis thaliana.";
Plant J. 58:333-346(2009).
[7]
FUNCTION, AND INTERACTION WITH EDS1.
PubMed=21434927; DOI=10.1111/j.1469-8137.2011.03675.x;
Rietz S., Stamm A., Malonek S., Wagner S., Becker D.,
Medina-Escobar N., Vlot A.C., Feys B.J., Niefind K., Parker J.E.;
"Different roles of Enhanced Disease Susceptibility1 (EDS1) bound to
and dissociated from Phytoalexin Deficient4 (PAD4) in Arabidopsis
immunity.";
New Phytol. 191:107-119(2011).
[8]
FUNCTION, SUBUNIT, INTERACTION WITH EDS1, AND SUBCELLULAR LOCATION.
PubMed=22072959; DOI=10.1371/journal.ppat.1002318;
Zhu S., Jeong R.-D., Venugopal S.C., Lapchyk L., Navarre D.,
Kachroo A., Kachroo P.;
"SAG101 forms a ternary complex with EDS1 and PAD4 and is required for
resistance signaling against turnip crinkle virus.";
PLoS Pathog. 7:E1002318-E1002318(2011).
[9]
FUNCTION.
PubMed=23356583; DOI=10.1111/nph.12155;
Langenbach C., Campe R., Schaffrath U., Goellner K., Conrath U.;
"UDP-glucosyltransferase UGT84A2/BRT1 is required for Arabidopsis
nonhost resistance to the Asian soybean rust pathogen Phakopsora
pachyrhizi.";
New Phytol. 198:536-545(2013).
[10]
X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) IN COMPLEX WITH EDS1, AND
INTERACTION WITH EDS1.
PubMed=21301097; DOI=10.1107/S1744309110051249;
Wagner S., Rietz S., Parker J.E., Niefind K.;
"Crystallization and preliminary crystallographic analysis of
Arabidopsis thaliana EDS1, a key component of plant immunity, in
complex with its signalling partner SAG101.";
Acta Crystallogr. F 67:245-248(2011).
[11]
X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-537 IN COMPLEX WITH EDS1,
AND MUTAGENESIS OF LEU-12; LEU-21; ILE-141 AND TYR-306.
PubMed=24331460; DOI=10.1016/j.chom.2013.11.006;
Wagner S., Stuttmann J., Rietz S., Guerois R., Brunstein E.,
Bautor J., Niefind K., Parker J.E.;
"Structural basis for signaling by exclusive EDS1 heteromeric
complexes with SAG101 or PAD4 in plant innate immunity.";
Cell Host Microbe 14:619-630(2013).
-!- FUNCTION: Acyl hydrolase that triggers the leaf senescence onset.
Can use triolein as substrate to produce oleic acids.
-!- FUNCTION: Involved in the EDS1-dependent intrinsic and
indispensable resistance signaling pathway; together with PAD4,
required for programmed cell death triggered by RPS4 in response
to avirulent pathogens (e.g. P.syringae pv. tomato strain DC3000
and H.parasitica isolates CALA2 and EMWA1) and in restricting the
growth of virulent pathogens (e.g. H.parasitica isolates NOCO2 and
P.syringae pv. tomato strain DC3000 avrRps4). Contributes in
reinforcing the immune response around hypersensitive response
foci (PubMed:21434927). Regulates the nuclear localization of
EDS1. Essential for the RPP8/HRT-mediated resistance to the turnip
crinkle virus (TCV). Involved in the post-invasion resistance to
P.pachyrhizi in the mesophyll. {ECO:0000269|PubMed:21434927,
ECO:0000269|PubMed:22072959}.
-!- CATALYTIC ACTIVITY: A carboxylic ester + H(2)O = an alcohol + a
carboxylate. {ECO:0000269|PubMed:11971136}.
-!- SUBUNIT: Part of a nuclear complex made of EDS1, PAD4 and SAG101,
that can be redirected to the cytoplasm in the presence of an
extranuclear form of EDS1 (PubMed:22072959). Interacts directly
with EDS1. {ECO:0000269|PubMed:16040633,
ECO:0000269|PubMed:21301097, ECO:0000269|PubMed:21434927,
ECO:0000269|PubMed:22072959, ECO:0000269|PubMed:24331460}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:22072959}.
Cytoplasm {ECO:0000269|PubMed:22072959}. Note=Can move to the
cytoplasm when in complex with PAD4 and EDS1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q4F883-1; Sequence=Displayed;
Name=2;
IsoId=Q4F883-2; Sequence=VSP_047931, VSP_047932;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in senescing leaves.
{ECO:0000269|PubMed:11971136}.
-!- DEVELOPMENTAL STAGE: Not expressed until the onset of senescence
in leaves. {ECO:0000269|PubMed:11971136,
ECO:0000269|PubMed:19143996}.
-!- INDUCTION: Specifically induced during senescence via a complex
epigenetic processe involving histone methylation.
{ECO:0000269|PubMed:19143996}.
-!- DISRUPTION PHENOTYPE: Delayed onset of leaf senescence (about 4
days later). Reduced resistance to both virulent and avirulent
pathogens (Pseudomonas syringae pv. tomato and Hyaloperonospora
parasitica). {ECO:0000269|PubMed:11971136}.
-!- SEQUENCE CAUTION:
Sequence=CAC01812.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; DQ103714; AAZ15704.1; -; mRNA.
EMBL; AL391146; CAC01812.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED92091.1; -; Genomic_DNA.
EMBL; CP002688; AED92092.1; -; Genomic_DNA.
EMBL; AY086301; AAM64373.1; -; mRNA.
PIR; T51438; T51438.
RefSeq; NP_568307.3; NM_121497.5. [Q4F883-1]
RefSeq; NP_851039.1; NM_180708.2. [Q4F883-2]
UniGene; At.23431; -.
PDB; 4NFU; X-ray; 2.21 A; B=2-537.
PDBsum; 4NFU; -.
ProteinModelPortal; Q4F883; -.
SMR; Q4F883; -.
BioGrid; 16622; 2.
STRING; 3702.AT5G14930.2; -.
ESTHER; arath-At5g14930; Plant_lipase_EDS1-like.
iPTMnet; Q4F883; -.
PaxDb; Q4F883; -.
EnsemblPlants; AT5G14930.1; AT5G14930.1; AT5G14930. [Q4F883-2]
EnsemblPlants; AT5G14930.2; AT5G14930.2; AT5G14930. [Q4F883-1]
GeneID; 831345; -.
Gramene; AT5G14930.1; AT5G14930.1; AT5G14930.
Gramene; AT5G14930.2; AT5G14930.2; AT5G14930.
KEGG; ath:AT5G14930; -.
Araport; AT5G14930; -.
TAIR; locus:2147825; AT5G14930.
eggNOG; ENOG410IKTV; Eukaryota.
eggNOG; ENOG410Y5MT; LUCA.
HOGENOM; HOG000091160; -.
InParanoid; Q4F883; -.
OMA; WAEVEDS; -.
OrthoDB; EOG093606TF; -.
PhylomeDB; Q4F883; -.
BioCyc; ARA:AT5G14930-MONOMER; -.
PRO; PR:Q4F883; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q4F883; baseline and differential.
Genevisible; Q4F883; AT.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:TAIR.
GO; GO:0007568; P:aging; IMP:TAIR.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
GO; GO:1902290; P:positive regulation of defense response to oomycetes; IMP:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
GO; GO:1900057; P:positive regulation of leaf senescence; IMP:UniProtKB.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR002921; Fungal_lipase-like.
Pfam; PF01764; Lipase_3; 1.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Hydrolase; Lipid degradation; Lipid metabolism; Membrane; Nucleus;
Plant defense; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 537 Senescence-associated carboxylesterase
101.
/FTId=PRO_0000423498.
TRANSMEM 140 160 Helical. {ECO:0000255}.
COMPBIAS 48 51 Poly-Lys.
COMPBIAS 78 83 Poly-Ser.
VAR_SEQ 130 131 LL -> VI (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_047931.
VAR_SEQ 132 537 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_047932.
MUTAGEN 12 12 L->A: No effect on interaction with EDS1;
when associated with A-21. No effect on
interaction with EDS1; when associated
with A-21 and A-141. Loss of interaction
with EDS1; when associated with A-21; A-
141 and A-306.
{ECO:0000269|PubMed:24331460}.
MUTAGEN 21 21 L->A: No effect on interaction with EDS1;
when associated with A-12. No effect on
interaction with EDS1; when associated
with A-12 and A-141. Loss of interaction
with EDS1; when associated with A-12; A-
141 and A-306.
{ECO:0000269|PubMed:24331460}.
MUTAGEN 141 141 I->A: No effect on interaction with EDS1;
when associated with A-12 and A-21. Loss
of interaction with EDS1; when associated
with A-12; A-21 and A-306.
{ECO:0000269|PubMed:24331460}.
MUTAGEN 306 306 Y->A: Loss of interaction with EDS1; when
associated with A-12; A-21 and A-141.
{ECO:0000269|PubMed:24331460}.
CONFLICT 40 40 H -> Q (in Ref. 4; AAM64373).
{ECO:0000305}.
HELIX 4 18 {ECO:0000244|PDB:4NFU}.
HELIX 21 33 {ECO:0000244|PDB:4NFU}.
STRAND 56 61 {ECO:0000244|PDB:4NFU}.
STRAND 66 71 {ECO:0000244|PDB:4NFU}.
HELIX 77 79 {ECO:0000244|PDB:4NFU}.
STRAND 83 87 {ECO:0000244|PDB:4NFU}.
HELIX 96 98 {ECO:0000244|PDB:4NFU}.
STRAND 104 109 {ECO:0000244|PDB:4NFU}.
HELIX 110 117 {ECO:0000244|PDB:4NFU}.
HELIX 120 135 {ECO:0000244|PDB:4NFU}.
STRAND 140 145 {ECO:0000244|PDB:4NFU}.
HELIX 147 159 {ECO:0000244|PDB:4NFU}.
TURN 160 162 {ECO:0000244|PDB:4NFU}.
STRAND 171 176 {ECO:0000244|PDB:4NFU}.
HELIX 183 189 {ECO:0000244|PDB:4NFU}.
HELIX 193 197 {ECO:0000244|PDB:4NFU}.
STRAND 198 203 {ECO:0000244|PDB:4NFU}.
STRAND 211 214 {ECO:0000244|PDB:4NFU}.
STRAND 217 223 {ECO:0000244|PDB:4NFU}.
STRAND 226 230 {ECO:0000244|PDB:4NFU}.
HELIX 233 240 {ECO:0000244|PDB:4NFU}.
HELIX 251 262 {ECO:0000244|PDB:4NFU}.
HELIX 273 286 {ECO:0000244|PDB:4NFU}.
TURN 287 294 {ECO:0000244|PDB:4NFU}.
HELIX 295 316 {ECO:0000244|PDB:4NFU}.
HELIX 321 330 {ECO:0000244|PDB:4NFU}.
HELIX 335 342 {ECO:0000244|PDB:4NFU}.
HELIX 344 361 {ECO:0000244|PDB:4NFU}.
HELIX 364 373 {ECO:0000244|PDB:4NFU}.
HELIX 375 395 {ECO:0000244|PDB:4NFU}.
HELIX 401 404 {ECO:0000244|PDB:4NFU}.
HELIX 408 417 {ECO:0000244|PDB:4NFU}.
STRAND 418 420 {ECO:0000244|PDB:4NFU}.
HELIX 421 428 {ECO:0000244|PDB:4NFU}.
TURN 429 431 {ECO:0000244|PDB:4NFU}.
HELIX 444 460 {ECO:0000244|PDB:4NFU}.
HELIX 466 488 {ECO:0000244|PDB:4NFU}.
HELIX 494 497 {ECO:0000244|PDB:4NFU}.
HELIX 502 514 {ECO:0000244|PDB:4NFU}.
HELIX 520 526 {ECO:0000244|PDB:4NFU}.
HELIX 529 532 {ECO:0000244|PDB:4NFU}.
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


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