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BGL19_ARATH
ID   BGL19_ARATH             Reviewed;         527 AA.
AC   Q9LIF9; Q93Z07;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Beta-glucosidase 19;
DE            Short=AtBGLU19;
DE            EC=3.2.1.21;
DE   Flags: Precursor;
GN   Name=BGLU19; OrderedLocusNames=At3g21370; ORFNames=MHC9.5;
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].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
RA   Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
RA   Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.;
RT   "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT   family 1.";
RL   Plant Mol. Biol. 55:343-367(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; AP001305; BAB03050.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76501.1; -; Genomic_DNA.
DR   EMBL; AY058865; AAL24252.1; -; mRNA.
DR   EMBL; AY064046; AAL36402.1; -; mRNA.
DR   EMBL; AY096383; AAM20024.1; -; mRNA.
DR   RefSeq; NP_188774.2; NM_113032.4.
DR   AlphaFoldDB; Q9LIF9; -.
DR   SMR; Q9LIF9; -.
DR   BioGRID; 7023; 2.
DR   IntAct; Q9LIF9; 1.
DR   STRING; 3702.AT3G21370.1; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   iPTMnet; Q9LIF9; -.
DR   PaxDb; Q9LIF9; -.
DR   PRIDE; Q9LIF9; -.
DR   ProteomicsDB; 240395; -.
DR   EnsemblPlants; AT3G21370.1; AT3G21370.1; AT3G21370.
DR   GeneID; 821691; -.
DR   Gramene; AT3G21370.1; AT3G21370.1; AT3G21370.
DR   KEGG; ath:AT3G21370; -.
DR   Araport; AT3G21370; -.
DR   TAIR; locus:2089433; AT3G21370.
DR   eggNOG; KOG0626; Eukaryota.
DR   HOGENOM; CLU_001859_1_0_1; -.
DR   InParanoid; Q9LIF9; -.
DR   OMA; QPNTAKM; -.
DR   OrthoDB; 408001at2759; -.
DR   PhylomeDB; Q9LIF9; -.
DR   BioCyc; ARA:AT3G21370-MON; -.
DR   PRO; PR:Q9LIF9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LIF9; baseline and differential.
DR   Genevisible; Q9LIF9; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0019762; P:glucosinolate catabolic process; IBA:GO_Central.
DR   GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosidase;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..527
FT                   /note="Beta-glucosidase 19"
FT                   /id="PRO_0000389581"
FT   MOTIF           524..527
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   ACT_SITE        201
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        418
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         469
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         476..477
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        495
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        220..231
FT                   /evidence="ECO:0000250"
FT   CONFLICT        349
FT                   /note="F -> L (in Ref. 3; AAL24252)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   527 AA;  60015 MW;  A9EB34BC818BF88A CRC64;
     MKIPLLGLLL LISLVGSPTR AEEGPVCPKT ETLSRASFPE GFMFGTATAA FQVEGAVNEG
     CRGPSLWDIY TKKFPHRVKN HNADEAVDFY HRYKEDIQLM KKLNTDGFRL SISWPRIFPH
     GRMEKGISKE GVQFYHDLID ELLKNDITPL VTVFHWDTPA DLEDEYGGFL SERIVPDFVE
     YANFTFHEYG DKVKNWITFN EPWVFSRSGY DVGKKAPGRC SPYVKEFGKL CQDGRSGFEP
     YVVSHNLLVG HAEAVDAFRK CEKCKGGKIG IAHSPAWFEP EDVEGGQATV NRVLDFVIGW
     HLDPTTFGDY PQSMKDAVGS RLPRFTKAQK AKLKDSTDFV GINYYTSFFA KADQKVDSRN
     PTWATDALVE FEPKTVDGSI KIGSQPNTAK MAVYAKGLRK LMKYIKDRYN SPEIIITENG
     YGEDLGDKDT DLSVALNDHN RKYYLQRHLL ALNEAICEDK VNVTSYFLWS LMDNFEWQDG
     YTARFGVYYI DFKNNLTRME KESAKWLSEF LKPGLKPSKS SKLHEEL
 
 
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