CXE4_ARATH
ID CXE4_ARATH Reviewed; 374 AA.
AC Q9FX93; Q8LF34;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Probable carboxylesterase 4, mitochondrial;
DE AltName: Full=AtCXE4;
DE EC=3.1.1.1;
DE Flags: Precursor;
GN Name=CXE4; OrderedLocusNames=At1g49650; ORFNames=F14J22.21;
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=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 (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP CYS-52.
RX PubMed=25732537; DOI=10.1093/jxb/erv064;
RA Carrie C., Venne A.S., Zahedi R.P., Soll J.;
RT "Identification of cleavage sites and substrate proteins for two
RT mitochondrial intermediate peptidases in Arabidopsis thaliana.";
RL J. Exp. Bot. 66:2691-2708(2015).
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:25732537}.
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}.
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DR EMBL; AC011807; AAG13051.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32455.1; -; Genomic_DNA.
DR EMBL; BT029001; ABI93910.1; -; mRNA.
DR EMBL; AY085072; AAM61628.1; -; mRNA.
DR RefSeq; NP_564550.1; NM_103853.5.
DR AlphaFoldDB; Q9FX93; -.
DR SMR; Q9FX93; -.
DR STRING; 3702.AT1G49650.1; -.
DR ESTHER; arath-Q8LF34; Plant_carboxylesterase.
DR PaxDb; Q9FX93; -.
DR PRIDE; Q9FX93; -.
DR ProteomicsDB; 220515; -.
DR EnsemblPlants; AT1G49650.1; AT1G49650.1; AT1G49650.
DR GeneID; 841389; -.
DR Gramene; AT1G49650.1; AT1G49650.1; AT1G49650.
DR KEGG; ath:AT1G49650; -.
DR Araport; AT1G49650; -.
DR TAIR; locus:2012131; AT1G49650.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_012494_22_0_1; -.
DR InParanoid; Q9FX93; -.
DR OMA; PVEWINK; -.
DR OrthoDB; 1263520at2759; -.
DR PhylomeDB; Q9FX93; -.
DR BioCyc; ARA:AT1G49650-MON; -.
DR PRO; PR:Q9FX93; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FX93; baseline and differential.
DR Genevisible; Q9FX93; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
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 Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Mitochondrion; Reference proteome; Serine esterase;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25732537"
FT CHAIN 53..374
FT /note="Probable carboxylesterase 4, mitochondrial"
FT /id="PRO_0000402550"
FT MOTIF 135..137
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 219
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 317
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 349
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT CONFLICT 196
FT /note="C -> D (in Ref. 4; AAM61628)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="R -> K (in Ref. 4; AAM61628)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="V -> I (in Ref. 4; AAM61628)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="N -> D (in Ref. 4; AAM61628)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="D -> E (in Ref. 4; AAM61628)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="A -> E (in Ref. 4; AAM61628)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="F -> L (in Ref. 4; AAM61628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 41693 MW; 1C02DE49FF97E071 CRC64;
MLRRITCSSS LASPSLFLRF FRQLPRSYSS PTTIAVSGRN IRRLSTPTTL RCICSHSSSE
IISEHPPFVR VYKDGRIERL SGTETVPASL NPRNDVVSKD VVYSPGHNLS VRLFLPHKST
QLAAGNKLPL LIYFHGGAWI NESPFSPIYH NFLTEVVKSA NCLAVSVQYR RAPEDPVPAA
YEDTWSAIQW IFSHSCGSGE EDWINKYADF ERVFLAGDSA GGNISHHMAM RAGKEKLKPR
IKGTVIVHPA IWGKDPVDEH DVQDREIRDG VAEVWEKIVS PNSVDGADDP WFNVVGSGSN
FSGMGCDKVL VEVAGKDVFW RQGLAYAAKL KKSGWKGEVE VIEEEDEEHC FHLLNPSSEN
APSFMKRFVE FITG
