位置:首页 > 蛋白库 > CXE2_ARATH
CXE2_ARATH
ID   CXE2_ARATH              Reviewed;         314 AA.
AC   Q9SX78; Q8LG06;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Probable carboxylesterase 2;
DE   AltName: Full=AtCXE2;
DE            EC=3.1.1.1;
GN   Name=CXE2; OrderedLocusNames=At1g47480; ORFNames=F16N3.25;
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].
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   [4]
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 and flowers.
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; AC007519; AAD46039.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE32171.1; -; Genomic_DNA.
DR   EMBL; AY084535; AAM61103.1; -; mRNA.
DR   PIR; A96515; A96515.
DR   RefSeq; NP_564507.1; NM_103640.3.
DR   AlphaFoldDB; Q9SX78; -.
DR   SMR; Q9SX78; -.
DR   STRING; 3702.AT1G47480.1; -.
DR   ESTHER; arath-F16N3.25; Plant_carboxylesterase.
DR   PaxDb; Q9SX78; -.
DR   PRIDE; Q9SX78; -.
DR   ProteomicsDB; 220377; -.
DR   EnsemblPlants; AT1G47480.1; AT1G47480.1; AT1G47480.
DR   GeneID; 841155; -.
DR   Gramene; AT1G47480.1; AT1G47480.1; AT1G47480.
DR   KEGG; ath:AT1G47480; -.
DR   Araport; AT1G47480; -.
DR   TAIR; locus:2015413; AT1G47480.
DR   eggNOG; KOG1515; Eukaryota.
DR   HOGENOM; CLU_012494_22_0_1; -.
DR   InParanoid; Q9SX78; -.
DR   OMA; NISHFMA; -.
DR   OrthoDB; 1263520at2759; -.
DR   PhylomeDB; Q9SX78; -.
DR   BioCyc; ARA:AT1G47480-MON; -.
DR   PRO; PR:Q9SX78; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SX78; baseline and differential.
DR   Genevisible; Q9SX78; 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; IPR002168; Lipase_GDXG_HIS_AS.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Reference proteome; Serine esterase.
FT   CHAIN           1..314
FT                   /note="Probable carboxylesterase 2"
FT                   /id="PRO_0000402548"
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        158
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   CONFLICT        133..134
FT                   /note="KN -> NT (in Ref. 3; AAM61103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="L -> I (in Ref. 3; AAM61103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178
FT                   /note="L -> V (in Ref. 3; AAM61103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205
FT                   /note="R -> M (in Ref. 3; AAM61103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220
FT                   /note="E -> K (in Ref. 3; AAM61103)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        264
FT                   /note="Y -> F (in Ref. 3; AAM61103)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   314 AA;  35255 MW;  F650CA0F5D2A4BA8 CRC64;
     MESTKKQVSL ELLPWLVVHT DGTVERLAGT EVCPPGLDPI TGVFSKDIII EPKTGLSARI
     YRPFSIQPGQ KIPLMLYFHG GAFLISSTSF PSYHTSLNKI VNQANVIAVS VNYRLAPEHP
     LPTAYEDSWT ALKNIQAINE PWINDYADLD SLFLVGDSAG ANISHHLAFR AKQSDQTLKI
     KGIGMIHPYF WGTQPIGAEI KDEARKQMVD GWWEFVCPSE KGSDDPWINP FADGSPDLGG
     LGCERVMITV AEKDILNERG KMYYERLVKS EWKGKVEIME TKEKDHVFHI FEPDCDEAME
     MVRCLALFIN QVEA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024