E132_ARATH
ID E132_ARATH Reviewed; 505 AA.
AC Q9C7U5;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase 2;
DE EC=3.2.1.39;
DE AltName: Full=(1->3)-beta-glucan endohydrolase 2;
DE Short=(1->3)-beta-glucanase 2;
DE AltName: Full=Beta-1,3-endoglucanase 2;
DE Short=Beta-1,3-glucanase 2;
DE Flags: Precursor;
GN OrderedLocusNames=At1g66250; ORFNames=T6J19.7;
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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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 -!- PTM: Contains two additional disulfide bonds. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51762.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC066691; AAG51762.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34485.1; -; Genomic_DNA.
DR EMBL; BX814184; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; E96687; E96687.
DR RefSeq; NP_176799.2; NM_105296.3.
DR AlphaFoldDB; Q9C7U5; -.
DR SMR; Q9C7U5; -.
DR STRING; 3702.AT1G66250.1; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; Q9C7U5; -.
DR PRIDE; Q9C7U5; -.
DR ProteomicsDB; 221954; -.
DR EnsemblPlants; AT1G66250.1; AT1G66250.1; AT1G66250.
DR GeneID; 842942; -.
DR Gramene; AT1G66250.1; AT1G66250.1; AT1G66250.
DR KEGG; ath:AT1G66250; -.
DR Araport; AT1G66250; -.
DR TAIR; locus:2205298; AT1G66250.
DR eggNOG; ENOG502QUUJ; Eukaryota.
DR HOGENOM; CLU_024953_3_3_1; -.
DR InParanoid; Q9C7U5; -.
DR OMA; ARYLNNN; -.
DR OrthoDB; 966331at2759; -.
DR PhylomeDB; Q9C7U5; -.
DR BioCyc; ARA:AT1G66250-MON; -.
DR PRO; PR:Q9C7U5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7U5; baseline and differential.
DR Genevisible; Q9C7U5; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA: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 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.
DR PROSITE; PS00587; GLYCOSYL_HYDROL_F17; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Glycosidase; GPI-anchor;
KW Hydrolase; Lipoprotein; Membrane; Plant defense; Reference proteome;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..477
FT /note="Glucan endo-1,3-beta-glucosidase 2"
FT /id="PRO_0000252330"
FT PROPEP 478..505
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000252331"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 272
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT LIPID 477
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 369..432
FT /evidence="ECO:0000250"
SQ SEQUENCE 505 AA; 54206 MW; 1A1CC342B307F29F CRC64;
MASLLHLLLL SLSLLVLASA SPSPPADEGS YIGVNIGTDL SDMPHPTQVV ALLKAQEIRH
IRLYNADPGL LIALANTGIK VIISIPNDQL LGIGQSNSTA ANWVKRNVIA HYPATMITAV
SVGSEVLTSL SNAAPVLVSA IKNVHAALLS ANLDKLIKVS TPLSTSLILD PFPPSQAFFN
RSLNAVIVPL LSFLQSTNSY LMVNVYPYID YMQSNGVIPL DYALFKPIPP NKEAVDANTL
VRYSNAFDAM VDATYFAMAF LNFTNIPVLV TESGWPSKGE TNEPDATLDN ANTYNSNLIR
HVLNKTGTPK RPGIAVSTYI YELYNEDTKA GLSEKNWGLF NANGEPVYVL RLTNSGSVLA
NDTTNQTYCT AREGADTKML QAALDWACGP GKIDCSPIKQ GETCYEPDNV VAHANYAFDT
YYHQTGNNPD ACNFNGVASI TTTDPSHGTC VFAGSRGNGR NGTSVNITAP SANSTTSSGI
RSDLYYSRGI WSILTVMILN VANIL
