E133_ARATH
ID E133_ARATH Reviewed; 501 AA.
AC Q9ZU91;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase 3;
DE EC=3.2.1.39;
DE AltName: Full=(1->3)-beta-glucan endohydrolase 3;
DE Short=(1->3)-beta-glucanase 3;
DE AltName: Full=Beta-1,3-endoglucanase 3;
DE Short=Beta-1,3-glucanase 3;
DE Flags: Precursor;
GN OrderedLocusNames=At2g01630; ORFNames=T8O11.20;
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.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC beta-D-glucans.; EC=3.2.1.39;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9ZU91-1; Sequence=Displayed;
CC -!- PTM: Contains two additional disulfide bonds. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR EMBL; AC006069; AAD12708.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC05475.1; -; Genomic_DNA.
DR EMBL; AY085500; AAM62724.1; -; mRNA.
DR PIR; B84427; B84427.
DR RefSeq; NP_565269.1; NM_126224.2. [Q9ZU91-1]
DR AlphaFoldDB; Q9ZU91; -.
DR SMR; Q9ZU91; -.
DR STRING; 3702.AT2G01630.1; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; Q9ZU91; -.
DR PRIDE; Q9ZU91; -.
DR ProteomicsDB; 222026; -. [Q9ZU91-1]
DR EnsemblPlants; AT2G01630.1; AT2G01630.1; AT2G01630. [Q9ZU91-1]
DR GeneID; 814692; -.
DR Gramene; AT2G01630.1; AT2G01630.1; AT2G01630. [Q9ZU91-1]
DR KEGG; ath:AT2G01630; -.
DR Araport; AT2G01630; -.
DR TAIR; locus:2065403; AT2G01630.
DR eggNOG; ENOG502QUUJ; Eukaryota.
DR InParanoid; Q9ZU91; -.
DR OrthoDB; 966331at2759; -.
DR PhylomeDB; Q9ZU91; -.
DR BioCyc; ARA:AT2G01630-MON; -.
DR PRO; PR:Q9ZU91; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU91; baseline and differential.
DR Genevisible; Q9ZU91; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR044965; Glyco_hydro_17_plant.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012946; X8.
DR PANTHER; PTHR32227; PTHR32227; 1.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Plant defense;
KW Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..470
FT /note="Glucan endo-1,3-beta-glucosidase 3"
FT /id="PRO_0000011886"
FT PROPEP 471..501
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000011887"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT LIPID 470
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 361..424
FT /evidence="ECO:0000250"
SQ SEQUENCE 501 AA; 53992 MW; 3858B1C25FD37920 CRC64;
MAALLLLFLF LFASSALSQD SLIGVNIGTE VTNMPSPTQV VALLKSQNIN RVRLYDADRS
MLLAFAHTGV QVIISVPNDQ LLGISQSNAT AANWVTRNVA AYYPATNITT IAVGSEVLTS
LTNAASVLVS ALKYIQAALV TANLDRQIKV STPHSSTIIL DSFPPSQAFF NKTWDPVIVP
LLKFLQSTGS PLLLNVYPYF DYVQSNGVIP LDYALFQPLQ ANKEAVDANT LLHYTNVFDA
IVDAAYFAMS YLNFTNIPIV VTESGWPSKG GPSEHDATVE NANTYNSNLI QHVINKTGTP
KHPGTAVTTY IYELYNEDTR PGPVSEKNWG LFYTNGTPVY TLRLAGAGAI LANDTTNQTF
CIAKEKVDRK MLQAALDWAC GPGKVDCSAL MQGESCYEPD DVVAHSTYAF NAYYQKMGKA
SGSCDFKGVA TVTTTDPSRG TCVFPGSAKS NQTLGNNTSA LAPSANSTTS GCIPKYYHHP
HASFGDLTLL SLLLIIALVF L
