CSE_ARATH
ID CSE_ARATH Reviewed; 332 AA.
AC Q9C942;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Caffeoylshikimate esterase;
DE EC=3.1.1.-;
DE AltName: Full=Lysophospholipase 2;
DE Short=LysoPL2;
GN Name=CSE; OrderedLocusNames=At1g52760; ORFNames=F14G24.3;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
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 [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH ACBP2,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20345607; DOI=10.1111/j.1365-313x.2010.04209.x;
RA Gao W., Li H.Y., Xiao S., Chye M.L.;
RT "Acyl-CoA-binding protein 2 binds lysophospholipase 2 and lysoPC to promote
RT tolerance to cadmium-induced oxidative stress in transgenic Arabidopsis.";
RL Plant J. 62:989-1003(2010).
RN [5]
RP FUNCTION.
RX PubMed=20657176; DOI=10.4161/psb.5.8.12294;
RA Gao W., Li H.Y., Xiao S., Chye M.L.;
RT "Protein interactors of acyl-CoA-binding protein ACBP2 mediate cadmium
RT tolerance in Arabidopsis.";
RL Plant Signal. Behav. 5:1025-1027(2010).
RN [6]
RP FUNCTION.
RX PubMed=22915575; DOI=10.1104/pp.112.202135;
RA Vijayaraj P., Jashal C.B., Vijayakumar A., Rani S.H., Venkata Rao D.K.,
RA Rajasekharan R.;
RT "A bifunctional enzyme that has both monoacylglycerol acyltransferase and
RT acyl hydrolase activities.";
RL Plant Physiol. 160:667-683(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23950498; DOI=10.1126/science.1241602;
RA Vanholme R., Cesarino I., Rataj K., Xiao Y., Sundin L., Goeminne G.,
RA Kim H., Cross J., Morreel K., Araujo P., Welsh L., Haustraete J.,
RA McClellan C., Vanholme B., Ralph J., Simpson G.G., Halpin C., Boerjan W.;
RT "Caffeoyl shikimate esterase (CSE) is an enzyme in the lignin biosynthetic
RT pathway in Arabidopsis.";
RL Science 341:1103-1106(2013).
CC -!- FUNCTION: Esterase involved in the biosynthesis of lignin. Hydrolyzes
CC caffeoylshikimate into caffeate and shikimate. Together with 4-
CC coumarate--CoA ligase (4CL), acts on an alternative reaction for the
CC formation of caffeoyl-CoA and bypasses the second reaction of shikimate
CC O-hydroxycinnamoyltransferase (HST). Accepts also 4-coumaroylshikimate
CC as substrate, but with lower activity. According to PubMed:20345607 and
CC PubMed:22915575, posseses monoacylglycerol O-acyltransferase,
CC monoacylglycerol lipase and lysophospholipase activities in vitro. With
CC the association of ACBP2, may promote the degradation of
CC lysophosphatidylcholine and detoxify the peroxidized membrane in
CC response to cadmium-induced oxidative stress. However these results
CC require additional confirmation in vivo. {ECO:0000269|PubMed:20345607,
CC ECO:0000269|PubMed:20657176, ECO:0000269|PubMed:22915575,
CC ECO:0000269|PubMed:23950498}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-O-[(E)-caffeoyl]-shikimate + H2O = (E)-caffeate + H(+) +
CC shikimate; Xref=Rhea:RHEA:49264, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36208, ChEBI:CHEBI:57770,
CC ChEBI:CHEBI:91005; Evidence={ECO:0000269|PubMed:23950498};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=96.5 uM for caffeoylshikimate {ECO:0000269|PubMed:20345607,
CC ECO:0000269|PubMed:23950498};
CC KM=211 uM for 4-coumarylshikimate {ECO:0000269|PubMed:20345607,
CC ECO:0000269|PubMed:23950498};
CC KM=6.6 uM for lysophosphatidylcholine (at pH 8.0 and 33 degrees
CC Celsius) {ECO:0000269|PubMed:20345607, ECO:0000269|PubMed:23950498};
CC Vmax=9.3 pmol/sec/mg enzyme toward caffeoylshikimate
CC {ECO:0000269|PubMed:20345607, ECO:0000269|PubMed:23950498};
CC Vmax=0.66 pmol/sec/mg enzyme toward 4-coumarylshikimate
CC {ECO:0000269|PubMed:20345607, ECO:0000269|PubMed:23950498};
CC Vmax=0.030 umol/min/mg enzyme toward lysophosphatidylcholine (at pH
CC 8.0 and 33 degrees Celsius) {ECO:0000269|PubMed:20345607,
CC ECO:0000269|PubMed:23950498};
CC -!- SUBUNIT: Interacts with ACBP2. {ECO:0000269|PubMed:20345607}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:20345607};
CC Peripheral membrane protein {ECO:0000305|PubMed:20345607}.
CC Note=Colocalizes with ACBP2.
CC -!- TISSUE SPECIFICITY: Expressed in vasculature of roots and leaves,
CC stems, flowers and siliques. {ECO:0000269|PubMed:20345607,
CC ECO:0000269|PubMed:23950498}.
CC -!- INDUCTION: By zinc and H(2)O(2). {ECO:0000269|PubMed:20345607}.
CC -!- DISRUPTION PHENOTYPE: Reduced height and weight of senescent plants due
CC to reduced lignin content. {ECO:0000269|PubMed:23950498}.
CC -!- MISCELLANEOUS: Mutant plants exhibit increased sensitivity to zinc,
CC cadmium and H(2)O(2). {ECO:0000305|PubMed:20345607}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Monoacylglycerol
CC lipase family. {ECO:0000305}.
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DR EMBL; AC019018; AAG52273.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32849.1; -; Genomic_DNA.
DR EMBL; AY054577; AAK96768.1; -; mRNA.
DR EMBL; BT008729; AAP42742.1; -; mRNA.
DR PIR; F96568; F96568.
DR RefSeq; NP_175685.1; NM_104154.4.
DR AlphaFoldDB; Q9C942; -.
DR SMR; Q9C942; -.
DR BioGRID; 26934; 6.
DR STRING; 3702.AT1G52760.1; -.
DR ESTHER; arath-F14G24.3; Monoglyceridelipase_lysophospholip.
DR MEROPS; S33.A37; -.
DR PaxDb; Q9C942; -.
DR PRIDE; Q9C942; -.
DR ProteomicsDB; 222654; -.
DR EnsemblPlants; AT1G52760.1; AT1G52760.1; AT1G52760.
DR GeneID; 841709; -.
DR Gramene; AT1G52760.1; AT1G52760.1; AT1G52760.
DR KEGG; ath:AT1G52760; -.
DR Araport; AT1G52760; -.
DR TAIR; locus:2011511; AT1G52760.
DR eggNOG; KOG1455; Eukaryota.
DR HOGENOM; CLU_026209_0_2_1; -.
DR InParanoid; Q9C942; -.
DR OMA; FVIPENM; -.
DR OrthoDB; 919091at2759; -.
DR PhylomeDB; Q9C942; -.
DR PRO; PR:Q9C942; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C942; baseline and differential.
DR Genevisible; Q9C942; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IDA:TAIR.
DR GO; GO:0090430; F:caffeoyl-CoA: alcohol caffeoyl transferase activity; IDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IDA:TAIR.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:TAIR.
DR GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046686; P:response to cadmium ion; IMP:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR022742; Hydrolase_4.
DR Pfam; PF12146; Hydrolase_4; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Lignin biosynthesis; Membrane;
KW Reference proteome.
FT CHAIN 1..332
FT /note="Caffeoylshikimate esterase"
FT /id="PRO_0000424295"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 268
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 298
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
SQ SEQUENCE 332 AA; 36975 MW; 985297835CF58AE6 CRC64;
MPSEAESSAN SAPATPPPPP NFWGTMPEEE YYTSQGVRNS KSYFETPNGK LFTQSFLPLD
GEIKGTVYMS HGYGSDTSWM FQKICMSFSS WGYAVFAADL LGHGRSDGIR CYMGDMEKVA
ATSLAFFKHV RCSDPYKDLP AFLFGESMGG LVTLLMYFQS EPETWTGLMF SAPLFVIPED
MKPSKAHLFA YGLLFGLADT WAAMPDNKMV GKAIKDPEKL KIIASNPQRY TGKPRVGTMR
ELLRKTQYVQ ENFGKVTIPV FTAHGTADGV TCPTSSKLLY EKASSADKTL KIYEGMYHSL
IQGEPDENAE IVLKDMREWI DEKVKKYGSK TA
