ID   E131_ARATH              Reviewed;         511 AA.
AC   O65399; F4IAH7; Q84W37;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 3.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase 1;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase 1;
DE            Short=(1->3)-beta-glucanase 1;
DE   AltName: Full=Beta-1,3-endoglucanase 1;
DE            Short=Beta-1,3-glucanase 1;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g11820; ORFNames=F12F1.33, F25C20_1;
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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).
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=O65399-1; Sequence=Displayed;
CC   -!- PTM: Contains two additional disulfide bonds. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC17632.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAO42272.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact leading to a deletion into the sequence.; Evidence={ECO:0000305};
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DR   EMBL; AC002131; AAC17632.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC007296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002684; AEE28791.1; -; Genomic_DNA.
DR   EMBL; BT004271; AAO42272.1; ALT_SEQ; mRNA.
DR   PIR; E86252; E86252.
DR   RefSeq; NP_001184967.1; NM_001198038.2. [O65399-1]
DR   RefSeq; NP_001323381.1; NM_001332003.1.
DR   AlphaFoldDB; O65399; -.
DR   SMR; O65399; -.
DR   STRING; 3702.O65399; -.
DR   CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PaxDb; 3702-AT1G11820-2; -.
DR   ProteomicsDB; 221953; -. [O65399-1]
DR   EnsemblPlants; AT1G11820.2; AT1G11820.2; AT1G11820. [O65399-1]
DR   GeneID; 837730; -.
DR   Gramene; AT1G11820.2; AT1G11820.2; AT1G11820. [O65399-1]
DR   KEGG; ath:AT1G11820; -.
DR   Araport; AT1G11820; -.
DR   TAIR; AT1G11820; -.
DR   eggNOG; ENOG502QTII; Eukaryota.
DR   HOGENOM; CLU_024953_3_3_1; -.
DR   InParanoid; O65399; -.
DR   OrthoDB; 1211890at2759; -.
DR   BioCyc; ARA:AT1G11820-MONOMER; -.
DR   PRO; PR:O65399; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O65399; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:SF120; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE 1; 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; O65399; 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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..485
FT                   /note="Glucan endo-1,3-beta-glucosidase 1"
FT                   /id="PRO_0000011884"
FT   PROPEP          486..511
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000011885"
FT   ACT_SITE        137
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        284
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   LIPID           485
FT                   /note="GPI-anchor amidated alanine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        480
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        382..445
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   511 AA;  55630 MW;  1C29693D4F94E8C4 CRC64;
     MAFTSMVSTV PVLFFFFTLL LISANSSSLS HNIKVQEQDK DPFVGFNIGT DVSNLLSPTE
     LVKFLQAQKV NHVRLYDADP ELLKALAKTK VRVIISVPNN QLLAIGSSNS TAASWIGRNV
     VAYYPETLIT AISVGDEVLT TVPSSAPLLL PAIESLYNAL VASNLHTQIK VSTPHAASIM
     LDTFPPSQAY FNQTWHSIMV PLLQFLSKTG SPLMMNLYPY YVYMQNKGVV PLDNCLFEPL
     TPSKEMVDPN TLLHYTNVLD AMVDAAYVSM KNLNVSDVAV LVTESGWPSK GDSKEPYATI
     DNADTYNSNL IKHVFDRTGT PLHPEMTSSV YIYELFNEDL RAPPVSEASW GLFYGNSTPV
     YLLHVSGSGT FLANDTTNQT YCIAMDGVDA KTLQAALDWA CGPGRSNCSE IQPGESCYQP
     NNVKGHASFA FNSYYQKEGR ASGSCDFKGV AMITTTDPSH GSCIFPGSKK VGNRTQTVVN
     STEVAAGEAT SRSLSRGFCV TIMILVTFSI L
//