E131_ARATH
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 03-AUG-2022, entry version 131.
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.AT1G11820.2; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; O65399; -.
DR PRIDE; O65399; -.
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; locus:2027317; AT1G11820.
DR eggNOG; ENOG502QTII; Eukaryota.
DR HOGENOM; CLU_024953_3_3_1; -.
DR InParanoid; O65399; -.
DR OrthoDB; 966331at2759; -.
DR BioCyc; ARA:AT1G11820-MON; -.
DR PRO; PR:O65399; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O65399; baseline and differential.
DR Genevisible; O65399; AT.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; 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 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
