CXE1_ARATH
ID CXE1_ARATH Reviewed; 318 AA.
AC Q9LMA7; Q84W95;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable carboxylesterase 1;
DE AltName: Full=AtCXE1;
DE EC=3.1.1.1;
GN Name=CXE1; OrderedLocusNames=At1g19190; ORFNames=T29M8.6;
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;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-318.
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 TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14738307; DOI=10.1007/s00239-003-2492-8;
RA Marshall S.D., Putterill J.J., Plummer K.M., Newcomb R.D.;
RT "The carboxylesterase gene family from Arabidopsis thaliana.";
RL J. Mol. Evol. 57:487-500(2003).
CC -!- FUNCTION: Carboxylesterase acting on esters with varying acyl chain
CC length. {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers and siliques.
CC {ECO:0000269|PubMed:14738307}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AC069143; AAF82230.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29816.1; -; Genomic_DNA.
DR EMBL; BT029511; ABL66767.1; -; mRNA.
DR EMBL; BT004093; AAO42119.1; -; mRNA.
DR PIR; D86325; D86325.
DR RefSeq; NP_173353.1; NM_101777.2.
DR AlphaFoldDB; Q9LMA7; -.
DR SMR; Q9LMA7; -.
DR STRING; 3702.AT1G19190.1; -.
DR ESTHER; arath-CXE1; Plant_carboxylesterase.
DR PaxDb; Q9LMA7; -.
DR PRIDE; Q9LMA7; -.
DR ProteomicsDB; 220513; -.
DR EnsemblPlants; AT1G19190.1; AT1G19190.1; AT1G19190.
DR GeneID; 838502; -.
DR Gramene; AT1G19190.1; AT1G19190.1; AT1G19190.
DR KEGG; ath:AT1G19190; -.
DR Araport; AT1G19190; -.
DR TAIR; locus:2202190; AT1G19190.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_012494_22_0_1; -.
DR InParanoid; Q9LMA7; -.
DR OMA; WIFTHIT; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q9LMA7; -.
DR BioCyc; ARA:AT1G19190-MON; -.
DR PRO; PR:Q9LMA7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMA7; baseline and differential.
DR Genevisible; Q9LMA7; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..318
FT /note="Probable carboxylesterase 1"
FT /id="PRO_0000402547"
FT MOTIF 79..81
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9SMN0"
SQ SEQUENCE 318 AA; 36081 MW; 552D50328B58D1FB CRC64;
MDSEIAFDYS PRFRIFKNGG IERLVPETFV PPSLNPENGV VSKDAVYSPE KNLSLRIYLP
QNSVYETGEK KIPLLVYFHG GGFIMETAFS PIYHTFLTSA VSATDCIAVS VEYRRAPEHP
IPTLYEDSWD AIQWIFTHIT RSGPEDWLNK HADFSKVFLA GDSAGANIAH HMAIRVDKEK
LPPENFKISG MILFHPYFLS KALIEEMEVE AMRYYERLWR IASPDSGNGV EDPWINVVGS
DLTGLGCRRV LVMVAGNDVL ARGGWSYVAE LEKSGWIGKV KVMETKEEGH VFHLRDPDSE
NARRVLRNFA EFLKEETF
