CXE12_ARATH
ID CXE12_ARATH Reviewed; 324 AA.
AC Q9SMN0; Q0WVA6; Q8VZG3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable carboxylesterase 12;
DE AltName: Full=AtCXE12;
DE EC=3.1.1.1;
GN Name=CXE12; OrderedLocusNames=At3g48690; ORFNames=T8P19.200;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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 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 MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 leaves, stems, flowers and siliques.
CC {ECO:0000269|PubMed:14738307}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL133315; CAB62358.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78446.1; -; Genomic_DNA.
DR EMBL; AY064980; AAL57633.1; -; mRNA.
DR EMBL; BT015037; AAT70488.1; -; mRNA.
DR EMBL; AK226849; BAE98942.1; -; mRNA.
DR PIR; T46213; T46213.
DR RefSeq; NP_190438.1; NM_114728.5.
DR AlphaFoldDB; Q9SMN0; -.
DR SMR; Q9SMN0; -.
DR BioGRID; 9348; 3.
DR IntAct; Q9SMN0; 3.
DR STRING; 3702.AT3G48690.1; -.
DR ChEMBL; CHEMBL1932906; -.
DR ESTHER; arath-CXE12; Plant_carboxylesterase.
DR MEROPS; S09.A09; -.
DR iPTMnet; Q9SMN0; -.
DR PaxDb; Q9SMN0; -.
DR PRIDE; Q9SMN0; -.
DR ProteomicsDB; 220375; -.
DR EnsemblPlants; AT3G48690.1; AT3G48690.1; AT3G48690.
DR GeneID; 824030; -.
DR Gramene; AT3G48690.1; AT3G48690.1; AT3G48690.
DR KEGG; ath:AT3G48690; -.
DR Araport; AT3G48690; -.
DR TAIR; locus:2114450; AT3G48690.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_012494_22_0_1; -.
DR InParanoid; Q9SMN0; -.
DR OMA; ANIVHHM; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q9SMN0; -.
DR BioCyc; ARA:AT3G48690-MON; -.
DR PRO; PR:Q9SMN0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SMN0; baseline and differential.
DR Genevisible; Q9SMN0; AT.
DR GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; 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 1: Evidence at protein level;
KW Acetylation; Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..324
FT /note="Probable carboxylesterase 12"
FT /id="PRO_0000402557"
FT MOTIF 78..80
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 162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 95
FT /note="F -> L (in Ref. 5; BAE98942)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="E -> D (in Ref. 3; AAL57633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 35567 MW; F47FC29B48B7888C CRC64;
MDSEIAVDCS PLLKIYKSGR IERLMGEATV PPSSEPQNGV VSKDVVYSAD NNLSVRIYLP
EKAAAETDSK LPLLVYFHGG GFIIETAFSP TYHTFLTTSV SASNCVAVSV DYRRAPEHPI
SVPFDDSWTA LKWVFTHITG SGQEDWLNKH ADFSRVFLSG DSAGANIVHH MAMRAAKEKL
SPGLNDTGIS GIILLHPYFW SKTPIDEKDT KDETLRMKIE AFWMMASPNS KDGTDDPLLN
VVQSESVDLS GLGCGKVLVM VAEKDALVRQ GWGYAAKLEK SGWKGEVEVV ESEGEDHVFH
LLKPECDNAI EVMHKFSGFI KGGN
