SOBR1_ARATH
ID SOBR1_ARATH Reviewed; 228 AA.
AC Q84WK4; A4KWB0; O49635;
DT 24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Carboxylesterase SOBER1 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:17293566, ECO:0000269|PubMed:19918071};
DE AltName: Full=Phospholipase A2 SOBER1 {ECO:0000305};
DE AltName: Full=Protein SUPPRESSOR OF AVRBST-ELICITED RESISTANCE 1 {ECO:0000303|PubMed:17293566};
GN Name=SOBER1 {ECO:0000303|PubMed:17293566};
GN OrderedLocusNames=At4g22305 {ECO:0000312|Araport:AT4G22305};
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], FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF SER-106 AND HIS-192.
RC STRAIN=cv. Columbia;
RX PubMed=17293566; DOI=10.1105/tpc.106.048710;
RA Cunnac S., Wilson A., Nuwer J., Kirik A., Baranage G., Mudgett M.B.;
RT "A conserved carboxylesterase is a SUPPRESSOR OF AVRBST-ELICITED RESISTANCE
RT in Arabidopsis.";
RL Plant Cell 19:688-705(2007).
RN [2]
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 [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].
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 [5]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND MUTAGENESIS OF HIS-192.
RX PubMed=19918071; DOI=10.1073/pnas.0903859106;
RA Kirik A., Mudgett M.B.;
RT "SOBER1 phospholipase activity suppresses phosphatidic acid accumulation
RT and plant immunity in response to bacterial effector AvrBsT.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20532-20537(2009).
CC -!- FUNCTION: Possesses carboxylesterase activity in vitro with a
CC preference for short acyl chain substrates. Functions as a negative
CC regulator of the hypersensitive response (HR) triggered by the
CC bacterial type III effector protein AvrBsT (PubMed:17293566). Possesses
CC phospholipase A2 (PLA2) activity and hydrolyzes phosphatidylcholine
CC (PC), a lipid that is hydrolyzed by phospholipase D (PLD) to produce
CC phosphatidic acid (PA). Required to suppress AvrBsT-dependent HR and
CC PLD-dependent production of PA in response to AvrBsT elicitation
CC (PubMed:19918071). {ECO:0000269|PubMed:17293566,
CC ECO:0000269|PubMed:19918071}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show hypersensitive response to infection
CC with the bacterial pathogen Xanthomonas campestris pv. vesicatoria
CC containing the type III effector protein AvrBsT.
CC {ECO:0000269|PubMed:17293566}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16780.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79185.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EF100725; ABO26813.1; -; mRNA.
DR EMBL; AL021712; CAA16780.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161557; CAB79185.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84590.1; -; Genomic_DNA.
DR EMBL; BT003123; AAO24555.1; -; mRNA.
DR EMBL; AK227671; BAE99658.1; -; mRNA.
DR PIR; T04911; T04911.
DR RefSeq; NP_001190797.1; NM_001203868.2.
DR PDB; 6AVV; X-ray; 1.51 A; A=1-228.
DR PDB; 6AVW; X-ray; 2.14 A; A=1-228.
DR PDB; 6AVX; X-ray; 1.27 A; A=1-228.
DR PDBsum; 6AVV; -.
DR PDBsum; 6AVW; -.
DR PDBsum; 6AVX; -.
DR AlphaFoldDB; Q84WK4; -.
DR SMR; Q84WK4; -.
DR STRING; 3702.AT4G22305.1; -.
DR ESTHER; arath-SOBR1; LYsophospholipase_carboxylesterase.
DR PaxDb; Q84WK4; -.
DR PRIDE; Q84WK4; -.
DR ProteomicsDB; 232599; -.
DR EnsemblPlants; AT4G22305.1; AT4G22305.1; AT4G22305.
DR GeneID; 10723040; -.
DR Gramene; AT4G22305.1; AT4G22305.1; AT4G22305.
DR KEGG; ath:AT4G22305; -.
DR Araport; AT4G22305; -.
DR TAIR; locus:6530298215; AT4G22305.
DR eggNOG; KOG2112; Eukaryota.
DR HOGENOM; CLU_049413_1_0_1; -.
DR OMA; PGWFDLY; -.
DR OrthoDB; 1373549at2759; -.
DR PRO; PR:Q84WK4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84WK4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:TAIR.
DR GO; GO:0008474; F:palmitoyl-(protein) hydrolase activity; IBA:GO_Central.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0098542; P:defense response to other organism; IMP:TAIR.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0002084; P:protein depalmitoylation; IBA:GO_Central.
DR GO; GO:0010363; P:regulation of plant-type hypersensitive response; IMP:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR003140; PLipase/COase/thioEstase.
DR Pfam; PF02230; Abhydrolase_2; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid metabolism; Hydrolase; Lipid metabolism;
KW Plant defense; Reference proteome.
FT CHAIN 1..228
FT /note="Carboxylesterase SOBER1"
FT /id="PRO_0000433446"
FT ACT_SITE 106
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O75608"
FT MUTAGEN 106
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17293566"
FT MUTAGEN 192
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:17293566,
FT ECO:0000269|PubMed:19918071"
FT CONFLICT 155
FT /note="S -> C (in Ref. 1; ABO26813)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:6AVX"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:6AVX"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:6AVX"
FT TURN 29..33
FT /evidence="ECO:0007829|PDB:6AVX"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6AVX"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6AVX"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:6AVX"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6AVX"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:6AVX"
FT HELIX 73..92
FT /evidence="ECO:0007829|PDB:6AVX"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6AVX"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:6AVX"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:6AVX"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:6AVX"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:6AVX"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:6AVX"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:6AVX"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:6AVX"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:6AVX"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:6AVX"
FT HELIX 196..210
FT /evidence="ECO:0007829|PDB:6AVX"
SQ SEQUENCE 228 AA; 24845 MW; 1244DA117D7348A1 CRC64;
MARTFILWLH GLGDSGPANE PIQTQFKSSE LSNASWLFPS APFNPVTCNN GAVMRSWFDV
PELPFKVGSP IDESSVLEAV KNVHAIIDQE IAEGTNPENV FICGLSQGGA LTLASVLLYP
KTLGGGAVLS GWVPFTSSII SQFPEEAKKT PILWSHGTDD RMVLFEAGQA ALPFLKEAGV
TCEFKAYPGL GHSISNKELK YIESWIKRRL KGSSSTCLQL NCLKEMFH
