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GDL43_ARATH
ID   GDL43_ARATH             Reviewed;         360 AA.
AC   Q9SIQ3; Q8LFE6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=GDSL esterase/lipase At2g31540;
DE            EC=3.1.1.-;
DE   AltName: Full=Extracellular lipase At2g31540;
DE   Flags: Precursor;
GN   OrderedLocusNames=At2g31540; ORFNames=T9H9.6;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   REVIEW.
RX   PubMed=15522763; DOI=10.1016/j.plipres.2004.09.002;
RA   Akoh C.C., Lee G.-C., Liaw Y.-C., Huang T.-H., Shaw J.-F.;
RT   "GDSL family of serine esterases/lipases.";
RL   Prog. Lipid Res. 43:534-552(2004).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=18819574; DOI=10.3923/pjbs.2008.763.767;
RA   Ling H.;
RT   "Sequence analysis of GDSL lipase gene family in Arabidopsis thaliana.";
RL   Pak. J. Biol. Sci. 11:763-767(2008).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AC007071; AAD24833.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08558.1; -; Genomic_DNA.
DR   EMBL; AY084895; AAM61458.1; -; mRNA.
DR   PIR; A84722; A84722.
DR   RefSeq; NP_180712.1; NM_128711.2.
DR   AlphaFoldDB; Q9SIQ3; -.
DR   SMR; Q9SIQ3; -.
DR   PaxDb; Q9SIQ3; -.
DR   PRIDE; Q9SIQ3; -.
DR   ProteomicsDB; 247093; -.
DR   EnsemblPlants; AT2G31540.1; AT2G31540.1; AT2G31540.
DR   GeneID; 817712; -.
DR   Gramene; AT2G31540.1; AT2G31540.1; AT2G31540.
DR   KEGG; ath:AT2G31540; -.
DR   Araport; AT2G31540; -.
DR   TAIR; locus:2065883; AT2G31540.
DR   eggNOG; ENOG502QSNM; Eukaryota.
DR   HOGENOM; CLU_015101_0_1_1; -.
DR   InParanoid; Q9SIQ3; -.
DR   OMA; FTHYYRS; -.
DR   OrthoDB; 704138at2759; -.
DR   PhylomeDB; Q9SIQ3; -.
DR   BioCyc; ARA:AT2G31540-MON; -.
DR   PRO; PR:Q9SIQ3; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SIQ3; baseline and differential.
DR   Genevisible; Q9SIQ3; AT.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd01837; SGNH_plant_lipase_like; 1.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR035669; SGNH_plant_lipase-like.
DR   Pfam; PF00657; Lipase_GDSL; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Lipid degradation; Lipid metabolism;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..360
FT                   /note="GDSL esterase/lipase At2g31540"
FT                   /id="PRO_0000367384"
FT   ACT_SITE        42
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        334
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        337
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        25
FT                   /note="A -> T (in Ref. 3; AAM61458)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        314
FT                   /note="S -> G (in Ref. 3; AAM61458)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        331
FT                   /note="L -> M (in Ref. 3; AAM61458)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        349
FT                   /note="L -> R (in Ref. 3; AAM61458)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  40121 MW;  FB01443FB79BC626 CRC64;
     MSTSKAITLT LFIATTLLAP CNAAANATTK PLFPAILIFG DSTVDTGNNN YPLPTIFRAE
     HFPYGMDLPD GKANGRFSNG KLISDIIATK LNIKEFIPPF LQPNLSDQDI LTGVCFASAG
     AGYDDLTSLS TQAIRVSEQP NMFKSYIARL KGIVGDKKAM EIINNAFVVV SAGPNDFILN
     YYEIPSRRLE YPFISGYQDF ILKRLENFVR ELYSLGVRNV LVGGLPPMGC LPIHMTAKFR
     NIFRFCLEHH NKDSVLYNEK LQNLLPQIEA SLPGSKFLYA DVYNPMMEMI QNPSKYGFKE
     TKRGCCGTGF LETSFMCNVF SPVCQNRSEF LFFDSIHPSE ATYNVIGNLL DPLIRGKFQA
 
 
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