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CXE18_ARATH
ID   CXE18_ARATH             Reviewed;         335 AA.
AC   Q9LT10; Q8L8W1;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable carboxylesterase 18;
DE   AltName: Full=AtCXE18;
DE            EC=3.1.1.1;
GN   Name=CXE18; OrderedLocusNames=At5g23530; ORFNames=MQM1.21;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(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   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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
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).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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, 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; AB025633; BAA97248.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93179.1; -; Genomic_DNA.
DR   EMBL; AK226851; BAE98944.1; -; mRNA.
DR   EMBL; BT028935; ABI49482.1; -; mRNA.
DR   EMBL; AY088776; AAM67089.1; -; mRNA.
DR   RefSeq; NP_197744.1; NM_122260.4.
DR   AlphaFoldDB; Q9LT10; -.
DR   SMR; Q9LT10; -.
DR   STRING; 3702.AT5G23530.1; -.
DR   ESTHER; arath-CXE18; Plant_carboxylesterase.
DR   MEROPS; S09.A10; -.
DR   iPTMnet; Q9LT10; -.
DR   PaxDb; Q9LT10; -.
DR   PRIDE; Q9LT10; -.
DR   ProteomicsDB; 220376; -.
DR   EnsemblPlants; AT5G23530.1; AT5G23530.1; AT5G23530.
DR   GeneID; 832418; -.
DR   Gramene; AT5G23530.1; AT5G23530.1; AT5G23530.
DR   KEGG; ath:AT5G23530; -.
DR   Araport; AT5G23530; -.
DR   TAIR; locus:2171681; AT5G23530.
DR   eggNOG; KOG1515; Eukaryota.
DR   HOGENOM; CLU_012494_22_1_1; -.
DR   InParanoid; Q9LT10; -.
DR   OMA; RYISPGM; -.
DR   OrthoDB; 1263520at2759; -.
DR   PhylomeDB; Q9LT10; -.
DR   BioCyc; ARA:AT5G23530-MON; -.
DR   PRO; PR:Q9LT10; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LT10; baseline and differential.
DR   Genevisible; Q9LT10; AT.
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:0009860; P:pollen tube growth; IEP:TAIR.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR013094; AB_hydrolase_3.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Hydrolase; Reference proteome; Serine esterase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..335
FT                   /note="Probable carboxylesterase 18"
FT                   /id="PRO_0000402562"
FT   MOTIF           94..96
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        173
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CONFLICT        300
FT                   /note="P -> S (in Ref. 5; AAM67089)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   335 AA;  37715 MW;  6A265F9E310C676C CRC64;
     MATDSQPNQK LTLPLKTRIA LTVISTMTDN AQRPDGTINR RFLRLFDFRA PPNPKPVNIV
     STSDFVVDQS RDLWFRLYTP HVSGDKIPVV VFFHGGGFAF LSPNAYPYDN VCRRFARKLP
     AYVISVNYRL APEHRYPAQY DDGFDALKYI EENHGSILPA NADLSRCFFA GDSAGGNIAH
     NVAIRICREP RSSFTAVKLI GLISIQPFFG GEERTEAEKQ LVGAPLVSPD RTDWCWKAMG
     LNRDHEAVNV GGPNAVDISG LDYPETMVVV AGFDPLKDWQ RSYYEWLKLC GKKATLIEYP
     NMFHAFYIFP ELPEAGQLIM RIKDFVDERV ASLSA
 
 
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