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GDL80_ARATH
ID   GDL80_ARATH             Reviewed;         356 AA.
AC   Q9FHQ1; Q8LF30;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=GDSL esterase/lipase At5g37690;
DE            EC=3.1.1.-;
DE   AltName: Full=Extracellular lipase At5g37690;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g37690; ORFNames=K12B20.17;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT   features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT   clones.";
RL   DNA Res. 6:183-195(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; AB018107; BAB08315.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94220.1; -; Genomic_DNA.
DR   EMBL; AY085078; AAM61634.1; -; mRNA.
DR   RefSeq; NP_198585.2; NM_123128.3.
DR   AlphaFoldDB; Q9FHQ1; -.
DR   SMR; Q9FHQ1; -.
DR   STRING; 3702.AT5G37690.1; -.
DR   PaxDb; Q9FHQ1; -.
DR   PRIDE; Q9FHQ1; -.
DR   ProteomicsDB; 221990; -.
DR   DNASU; 833748; -.
DR   EnsemblPlants; AT5G37690.1; AT5G37690.1; AT5G37690.
DR   GeneID; 833748; -.
DR   Gramene; AT5G37690.1; AT5G37690.1; AT5G37690.
DR   KEGG; ath:AT5G37690; -.
DR   Araport; AT5G37690; -.
DR   TAIR; locus:2151744; AT5G37690.
DR   eggNOG; ENOG502QW3W; Eukaryota.
DR   HOGENOM; CLU_015101_0_0_1; -.
DR   InParanoid; Q9FHQ1; -.
DR   OMA; YLTYCLA; -.
DR   OrthoDB; 704138at2759; -.
DR   PhylomeDB; Q9FHQ1; -.
DR   BioCyc; ARA:AT5G37690-MON; -.
DR   PRO; PR:Q9FHQ1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FHQ1; baseline and differential.
DR   Genevisible; Q9FHQ1; 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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..356
FT                   /note="GDSL esterase/lipase At5g37690"
FT                   /id="PRO_0000367420"
FT   ACT_SITE        34
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        322
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        325
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        14
FT                   /note="T -> A (in Ref. 3; AAM61634)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="V -> I (in Ref. 3; AAM61634)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="Missing (in Ref. 3; AAM61634)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   356 AA;  39211 MW;  EC3878F13D84A7D5 CRC64;
     MMILRLALAI VISTYATAQP ASTSSLVTYI FGDSLTEVGN NNFLQYSLAR ADFPYYGVDF
     SGGKATGRFT NGRTIGDIIS TKLGILSPPP YLSLSQNDDA FLSGINYASG GAGILNETGI
     YFIQRLTFND QINCFKKTKE VIRAKIGDGA ANKHVNDAMY FIGLGSNDYV NNFLQPFMAD
     GQQYTHDEFV ELLTSTLHNQ LTTIYKLGAR KVIFHGLGPL GCIPSQRVKS KTRMCLNRVN
     EWVLEFNSRT KKLLIDLNKR LPGAKFSFAD TYPAVLDLIN NPTHYGFKIA NTSCCNVDTS
     VGGLCLPNSK MCKNRQDFVF WDAFHPSDSA NQILADHLFS SLLSSSSPSP APKPRQ
 
 
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