ID   E139_ARATH              Reviewed;         476 AA.
AC   Q9FGH4;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   02-SEP-2026, entry version 141.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase 9;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase 9;
DE            Short=(1->3)-beta-glucanase 9;
DE   AltName: Full=Beta-1,3-endoglucanase 9;
DE            Short=Beta-1,3-glucanase 9;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g58480; ORFNames=MQJ2.8;
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;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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: Secreted, cell wall {ECO:0000305}. Cell membrane;
CC       Lipid-anchor, GPI-anchor; Extracellular side.
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; AB025632; BAB10263.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97058.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7056993.1; -; Genomic_DNA.
DR   EMBL; BT005117; AAO50650.1; -; mRNA.
DR   EMBL; BT003904; AAO41952.1; -; mRNA.
DR   RefSeq; NP_200656.2; NM_125234.4.
DR   AlphaFoldDB; Q9FGH4; -.
DR   SMR; Q9FGH4; -.
DR   FunCoup; Q9FGH4; 75.
DR   STRING; 3702.Q9FGH4; -.
DR   GlyGen; Q9FGH4; 9 sites.
DR   PaxDb; 3702-Q9FGH4; -.
DR   ProteomicsDB; 222009; -.
DR   GeneID; 835961; -.
DR   KEGG; ath:AT5G58480; -.
DR   Araport; AT5G58480; -.
DR   TAIR; AT5G58480; -.
DR   eggNOG; ENOG502QTM2; Eukaryota.
DR   HOGENOM; CLU_024953_2_0_1; -.
DR   InParanoid; Q9FGH4; -.
DR   OMA; GEQFHPF; -.
DR   OrthoDB; 1293114at2759; -.
DR   PhylomeDB; Q9FGH4; -.
DR   BioCyc; ARA:AT5G58480-MONOMER; -.
DR   PRO; PR:Q9FGH4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FGH4; baseline and differential.
DR   GO; GO:0016020; C:membrane; TAS: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   FunFam; 3.20.20.80:FF:000008; Glucan endo-1,3-beta-glucosidase 5; 1.
DR   FunFam; 1.20.58.1040:FF:000002; Glucan endo-1,3-beta-glucosidase 8; 1.
DR   Gene3D; 1.20.58.1040; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR044965; Glyco_hydro_17_plant.
DR   InterPro; IPR012946; X8.
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.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW   Plant defense; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..453
FT                   /note="Glucan endo-1,3-beta-glucosidase 9"
FT                   /id="PRO_0000251265"
FT   PROPEP          454..476
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000251266"
FT   ACT_SITE        122
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   LIPID           453
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        101
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
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        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        364..424
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   476 AA;  52370 MW;  00CC6739B10CBB20 CRC64;
     MARRLFLLLL AVTAGLSLTG TTVRAVGINW GTEASHPLPP SKVVELLKSN GIVKVKLFDA
     DPKVLRALSG SNIGVTIGIQ NSMLKSLNAS VKVAESWVHD NVTRYFNGGN RVRIEYVAVG
     EEPFLQSYGN QYKPFVIGAA MNIQNALVKA NLANEVKVVV PSSFDSFLSE SGRPSSGHFR
     ADLNKTMIEL LSFLTKHHSP FFVTISPFLS FHQNKNISLD FSLFKETAKA HKDGRKTYRN
     SFDLSYDTLV SALFTIGFSE VDIVVSKIGW PTDGAENATS LTAEAFFKGL IVHLEKKTAS
     LPRPPVETYI ESLLDEDQRN LSAGNFERHW GVFTFDGQAK YNFSFNHKNQ VNAQNVQYLP
     PKWCVVNNNK DLSNASARAL EACAVADCTS ILPGGSCSGI RWPGNVSYAF NSLYQQNDHS
     AESCNFGGLG LITTVDPSED NCRFSIQLDT SHSSSQTPNF FQSWPLLLLF LLSGLF
//