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   27-MAR-2024, entry version 147.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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.Q9ZU91; -.
DR   CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PaxDb; 3702-AT2G01630-1; -.
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; AT2G01630; -.
DR   eggNOG; ENOG502QUUJ; Eukaryota.
DR   InParanoid; Q9ZU91; -.
DR   OrthoDB; 1211890at2759; -.
DR   PhylomeDB; Q9ZU91; -.
DR   BioCyc; ARA:AT2G01630-MONOMER; -.
DR   PRO; PR:Q9ZU91; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9ZU91; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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   Gene3D; 1.20.58.1040; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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:SF366; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE 3; 1.
DR   PANTHER; PTHR32227; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE BG1-RELATED-RELATED; 1.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   Pfam; PF07983; X8; 1.
DR   SMART; SM00768; X8; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
DR   Genevisible; Q9ZU91; AT.
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
//