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CXE11_ARATH
ID   CXE11_ARATH             Reviewed;         460 AA.
AC   Q9LK21; Q6NKX4;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Probable carboxylesterase 11;
DE   AltName: Full=AtCXE11;
DE            EC=3.1.1.1;
GN   Name=CXE11; OrderedLocusNames=At3g27320; ORFNames=K17E12.14;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA   Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA   Shinozaki K., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
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).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LK21-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LK21-2; Sequence=VSP_040307;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC       siliques. {ECO:0000269|PubMed:14738307}.
CC   -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BX824353; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; AP000381; BAB02127.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77294.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77295.1; -; Genomic_DNA.
DR   EMBL; BT012569; AAS99713.1; -; mRNA.
DR   EMBL; AK176881; BAD44644.1; -; mRNA.
DR   EMBL; BX824353; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001030781.1; NM_001035704.2. [Q9LK21-2]
DR   RefSeq; NP_189367.1; NM_113646.4. [Q9LK21-1]
DR   AlphaFoldDB; Q9LK21; -.
DR   SMR; Q9LK21; -.
DR   STRING; 3702.AT3G27320.1; -.
DR   ESTHER; arath-CXE11; Plant_carboxylesterase.
DR   MEROPS; S09.A05; -.
DR   iPTMnet; Q9LK21; -.
DR   PaxDb; Q9LK21; -.
DR   PRIDE; Q9LK21; -.
DR   ProteomicsDB; 220511; -. [Q9LK21-1]
DR   EnsemblPlants; AT3G27320.1; AT3G27320.1; AT3G27320. [Q9LK21-1]
DR   EnsemblPlants; AT3G27320.2; AT3G27320.2; AT3G27320. [Q9LK21-2]
DR   GeneID; 822351; -.
DR   Gramene; AT3G27320.1; AT3G27320.1; AT3G27320. [Q9LK21-1]
DR   Gramene; AT3G27320.2; AT3G27320.2; AT3G27320. [Q9LK21-2]
DR   KEGG; ath:AT3G27320; -.
DR   Araport; AT3G27320; -.
DR   TAIR; locus:2086503; AT3G27320.
DR   eggNOG; KOG1515; Eukaryota.
DR   InParanoid; Q9LK21; -.
DR   OMA; SMCILAW; -.
DR   PhylomeDB; Q9LK21; -.
DR   PRO; PR:Q9LK21; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LK21; baseline and differential.
DR   Genevisible; Q9LK21; 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   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Reference proteome; Serine esterase.
FT   CHAIN           1..460
FT                   /note="Probable carboxylesterase 11"
FT                   /id="PRO_0000402556"
FT   REGION          26..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           173..175
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   COMPBIAS        26..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT   VAR_SEQ         96..127
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3, ECO:0000303|Ref.4"
FT                   /id="VSP_040307"
FT   CONFLICT        218
FT                   /note="A -> G (in Ref. 3; AAS99713 and 4; BAD44644)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   460 AA;  50531 MW;  F6E0637960621478 CRC64;
     MPSVGVKLYS VFFKFLLKHR LQNRIQSSGD ESSSDPFGVT TRPEESVAAP NPLFTDGVAT
     KDIHIDPLTS LSVRIFLPES ALTPLEPSTS ACVYSGKART LNNIAGSDLL SRRNSLGSSN
     SLLSHKVESR RNSYGYTTGS SSPEAGSSDV YRGYAPSSSG GNSRKLPVML QFHGGGWVSG
     SNDSVANDFF CRRMAKHCDI IVLAVGYRLA PENRYPAACE DGFKVLKWLG KQANLAECNK
     SMGNSRRPGG EVKKSEVNKH IVDAFGASLV EPWLANHADP SRCVLLGVSC GANIADYVAR
     KAIEVGQNLD PVKVVAQVLM YPFFIGSVPT QSEIKQANSY FYDKPMCILA WKLFLPEEEF
     SLDHQAANPL VPGRSPPLKF MPPTLTIVAE HDWMRDRAIA YSEELRKVNV DAPVLEYKDA
     VHEFATLDML LRTPQAQACA EDIAIWAKKY ISLRGHEFSY
 
 
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