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GDL86_ARATH
ID   GDL86_ARATH             Reviewed;         375 AA.
AC   Q9FJ40; Q8LFP6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=GDSL esterase/lipase At5g45960;
DE            EC=3.1.1.-;
DE   AltName: Full=Extracellular lipase At5g45960;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g45960; ORFNames=K15I22.16;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
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; AB016870; BAB09324.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95320.1; -; Genomic_DNA.
DR   EMBL; AY084721; AAM61295.1; -; mRNA.
DR   RefSeq; NP_199408.1; NM_123964.4.
DR   AlphaFoldDB; Q9FJ40; -.
DR   SMR; Q9FJ40; -.
DR   PaxDb; Q9FJ40; -.
DR   PRIDE; Q9FJ40; -.
DR   ProteomicsDB; 221994; -.
DR   EnsemblPlants; AT5G45960.1; AT5G45960.1; AT5G45960.
DR   GeneID; 834636; -.
DR   Gramene; AT5G45960.1; AT5G45960.1; AT5G45960.
DR   KEGG; ath:AT5G45960; -.
DR   Araport; AT5G45960; -.
DR   TAIR; locus:2152435; AT5G45960.
DR   eggNOG; ENOG502QUD3; Eukaryota.
DR   HOGENOM; CLU_015101_0_1_1; -.
DR   InParanoid; Q9FJ40; -.
DR   OMA; RIAYMDI; -.
DR   OrthoDB; 704138at2759; -.
DR   PhylomeDB; Q9FJ40; -.
DR   BioCyc; ARA:AT5G45960-MON; -.
DR   PRO; PR:Q9FJ40; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJ40; baseline and differential.
DR   Genevisible; Q9FJ40; 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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..375
FT                   /note="GDSL esterase/lipase At5g45960"
FT                   /id="PRO_0000367426"
FT   ACT_SITE        54
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        348
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        351
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        8
FT                   /note="F -> S (in Ref. 3; AAM61295)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="N -> D (in Ref. 3; AAM61295)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   375 AA;  42482 MW;  5D69953AC1137684 CRC64;
     MRSHHRHFSS YVSFILFLFL FFISFSSSTS KLEPAKSEPK RKHSVSAILV FGDSTVDPGN
     NNYIDTVFKC NFPPYGLDFR NKTPTGRFCN GRLVTDFIAS YIGVKENVPP YLDPNLGINE
     LISGVSFASA GSGYDPLTPT ITNVIDIPTQ LEYFREYKRK LEGKMGKQEM EKHIEEAMFC
     VSAGTNDFVI NYFTIPIRRK TFTIEAYQQF VISNLKQFIQ GLWKEGARKI TVAGLPPIGC
     LPIVITLFSG EALTNRRCID RFSTVATNYN FLLQKQLALM QVGLAHLGSK IFYLDVYNPV
     YEVIRDPRKF GFEEVFSGCC GSGYLEASFL CNPKSYVCPN TSAYVFFDSI HPSEKTYFSL
     FRSLRPIYDS ILGSF
 
 
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