CXE17_ARATH
ID CXE17_ARATH Reviewed; 344 AA.
AC Q9LFR7; Q8LAT4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable carboxylesterase 17;
DE AltName: Full=AtCXE17;
DE EC=3.1.1.1;
GN Name=CXE17; OrderedLocusNames=At5g16080; ORFNames=F1N13.220;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
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 [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 -!- INTERACTION:
CC Q9LFR7; Q17TI5: BRX; NbExp=5; IntAct=EBI-4456165, EBI-4426649;
CC Q9LFR7; O23160: MYB73; NbExp=3; IntAct=EBI-4456165, EBI-25506855;
CC Q9LFR7; P49598: PP2CA; NbExp=3; IntAct=EBI-4456165, EBI-1764934;
CC Q9LFR7; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-4456165, EBI-4426144;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers.
CC {ECO:0000269|PubMed:14738307}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL391145; CAC01807.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92244.1; -; Genomic_DNA.
DR EMBL; AF370327; AAK44142.1; -; mRNA.
DR EMBL; AY113907; AAM44955.1; -; mRNA.
DR EMBL; AY087623; AAM65164.1; -; mRNA.
DR PIR; T51391; T51391.
DR RefSeq; NP_197112.1; NM_121613.3.
DR AlphaFoldDB; Q9LFR7; -.
DR SMR; Q9LFR7; -.
DR BioGRID; 16741; 10.
DR IntAct; Q9LFR7; 10.
DR STRING; 3702.AT5G16080.1; -.
DR ESTHER; arath-F1N13.220; Plant_carboxylesterase.
DR MEROPS; S09.A12; -.
DR PaxDb; Q9LFR7; -.
DR PRIDE; Q9LFR7; -.
DR ProteomicsDB; 220326; -.
DR EnsemblPlants; AT5G16080.1; AT5G16080.1; AT5G16080.
DR GeneID; 831465; -.
DR Gramene; AT5G16080.1; AT5G16080.1; AT5G16080.
DR KEGG; ath:AT5G16080; -.
DR Araport; AT5G16080; -.
DR TAIR; locus:2146097; AT5G16080.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_012494_22_1_1; -.
DR InParanoid; Q9LFR7; -.
DR OMA; INYALAP; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q9LFR7; -.
DR BioCyc; ARA:AT5G16080-MON; -.
DR PRO; PR:Q9LFR7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFR7; baseline and differential.
DR Genevisible; Q9LFR7; AT.
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 Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..344
FT /note="Probable carboxylesterase 17"
FT /id="PRO_0000402561"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 99..101
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 184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT CONFLICT 156..159
FT /note="VKQQ -> IKQH (in Ref. 4; AAM65164)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> V (in Ref. 4; AAM65164)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="P -> L (in Ref. 4; AAM65164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 37698 MW; E24D0838E4DED93B CRC64;
MATISFSHNH QSSDNRRGGS HHHRHGPVVE EIEGLIKVFN DGCVERPPIV PIVSPTIHPS
SKATAFDIKL SNDTWTRVYI PDAAAASPSV TLPLLVYFHG GGFCVGSAAW SCYHDFLTSL
AVKARCVIVS VNYRLAPEHR LPAAYDDGVN VVSWLVKQQI STGGGYPSWL SKCNLSNVFL
AGDSAGANIA YQVAVRIMAS GKYANTLHLK GIILIHPFFG GESRTSSEKQ QHHTKSSALT
LSASDAYWRL ALPRGASRDH PWCNPLMSSA GAKLPTTMVF MAEFDILKER NLEMCKVMRS
HGKRVEGIVH GGVGHAFHIL DNSSVSRDRI HDMMCRLHNF IHPS
