E138_ARATH
ID E138_ARATH Reviewed; 481 AA.
AC Q6NKW9; Q67XG3; Q9XIR7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase 8;
DE EC=3.2.1.39;
DE AltName: Full=(1->3)-beta-glucan endohydrolase 8;
DE Short=(1->3)-beta-glucanase 8;
DE AltName: Full=Beta-1,3-endoglucanase 8;
DE Short=Beta-1,3-glucanase 8;
DE Flags: Precursor;
GN OrderedLocusNames=At1g64760; ORFNames=F13O11.7;
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 [MRNA].
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RL Submitted (MAR-2005) 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: 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD38251.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC006193; AAD38251.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE34283.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34284.1; -; Genomic_DNA.
DR EMBL; BT012574; AAS99718.1; -; mRNA.
DR EMBL; AK220635; BAD95084.1; -; mRNA.
DR EMBL; AK176856; BAD44619.1; -; mRNA.
DR EMBL; AK175510; BAD43273.1; -; mRNA.
DR PIR; G96670; G96670.
DR RefSeq; NP_001031232.1; NM_001036155.3.
DR RefSeq; NP_176656.1; NM_105150.3.
DR AlphaFoldDB; Q6NKW9; -.
DR SMR; Q6NKW9; -.
DR STRING; 3702.AT1G64760.2; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; Q6NKW9; -.
DR PRIDE; Q6NKW9; -.
DR ProteomicsDB; 222028; -.
DR EnsemblPlants; AT1G64760.1; AT1G64760.1; AT1G64760.
DR EnsemblPlants; AT1G64760.2; AT1G64760.2; AT1G64760.
DR GeneID; 842784; -.
DR Gramene; AT1G64760.1; AT1G64760.1; AT1G64760.
DR Gramene; AT1G64760.2; AT1G64760.2; AT1G64760.
DR KEGG; ath:AT1G64760; -.
DR Araport; AT1G64760; -.
DR TAIR; locus:2010916; AT1G64760.
DR eggNOG; ENOG502QQQS; Eukaryota.
DR HOGENOM; CLU_024953_2_0_1; -.
DR InParanoid; Q6NKW9; -.
DR OMA; MYYQAQN; -.
DR OrthoDB; 966331at2759; -.
DR PhylomeDB; Q6NKW9; -.
DR BioCyc; ARA:AT1G64760-MON; -.
DR PRO; PR:Q6NKW9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NKW9; baseline and differential.
DR Genevisible; Q6NKW9; 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:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; 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 GO; GO:0009664; P:plant-type cell wall organization; IMP:TAIR.
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 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..33
FT /evidence="ECO:0000255"
FT CHAIN 34..455
FT /note="Glucan endo-1,3-beta-glucosidase 8"
FT /id="PRO_0000251255"
FT PROPEP 456..481
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000251256"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT LIPID 455
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 367..428
FT /evidence="ECO:0000250"
FT CONFLICT 95
FT /note="W -> L (in Ref. 3; AAS99718 and 4; BAD95084)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="N -> H (in Ref. 3; AAS99718 and 4; BAD95084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 52281 MW; 01A7938FBF3C65F0 CRC64;
MSNLLALVVG FVIVIGHLGI LVNGLGVNWG TMATHKLPPK TVVQMLKDNN INKVKLFDAD
ETTMGALAGS GLEVMVAIPN DQLKVMTSYD RAKDWVRKNV TRYNFDGGVN ITFVAVGNEP
FLKSYNGSFI NLTFPALANI QNALNEAGLG NSVKATVPLN ADVYDSPASN PVPSAGRFRP
DIIGQMTQIV DFLGKNNAPI TINIYPFLSL YGNDDFPLNY AFFDGAEPIN DNGIDYTNVF
DANFDTLVSS LKAVGHGDMP IIVGEVGWPT EGDKHANAGS AYRFYNGLLP RLGTNKGTPL
RPTYIEVYLF GLLDEDAKSI APGPFERHWG IFKFDGQPKF PIDLSGQGQS KFLIGAQNVP
YLPNKWCTFN PEAKDLTKLA ANIDYACTFS DCTALGYGSS CNTLDANGNA SYAFNMFFQV
KNQDESACYF QGLATITTQN ISQGQCNFPI QIVASSASSF SCSSYSLVVL IVWFLLSGMM
F
