E139_ARATH
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 03-AUG-2022, entry version 127.
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 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; 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 STRING; 3702.AT5G58480.1; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; Q9FGH4; -.
DR PRIDE; Q9FGH4; -.
DR ProteomicsDB; 222009; -.
DR EnsemblPlants; AT5G58480.1; AT5G58480.1; AT5G58480.
DR GeneID; 835961; -.
DR Gramene; AT5G58480.1; AT5G58480.1; AT5G58480.
DR KEGG; ath:AT5G58480; -.
DR Araport; AT5G58480; -.
DR TAIR; locus:2171253; AT5G58480.
DR eggNOG; ENOG502QTM2; Eukaryota.
DR HOGENOM; CLU_024953_2_0_1; -.
DR InParanoid; Q9FGH4; -.
DR OMA; GEQFHPF; -.
DR OrthoDB; 966331at2759; -.
DR PhylomeDB; Q9FGH4; -.
DR BioCyc; ARA:AT5G58480-MON; -.
DR PRO; PR:Q9FGH4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGH4; baseline and differential.
DR Genevisible; Q9FGH4; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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.
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
