E1313_ARATH
ID E1313_ARATH Reviewed; 506 AA.
AC Q9FJU9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase 13;
DE EC=3.2.1.39;
DE AltName: Full=(1->3)-beta-glucan endohydrolase 13;
DE Short=(1->3)-beta-glucanase 13;
DE AltName: Full=Beta-1,3-endoglucanase 13;
DE Short=Beta-1,3-glucanase 13;
DE Flags: Precursor;
GN OrderedLocusNames=At5g56590; ORFNames=MIK19.3;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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; AB013392; BAB09876.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96784.1; -; Genomic_DNA.
DR EMBL; AY133637; AAM91467.1; -; mRNA.
DR EMBL; AY075591; AAL91612.1; -; mRNA.
DR RefSeq; NP_200470.1; NM_125042.4.
DR AlphaFoldDB; Q9FJU9; -.
DR SMR; Q9FJU9; -.
DR STRING; 3702.AT5G56590.1; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; Q9FJU9; -.
DR PRIDE; Q9FJU9; -.
DR ProteomicsDB; 222006; -.
DR EnsemblPlants; AT5G56590.1; AT5G56590.1; AT5G56590.
DR GeneID; 835760; -.
DR Gramene; AT5G56590.1; AT5G56590.1; AT5G56590.
DR KEGG; ath:AT5G56590; -.
DR Araport; AT5G56590; -.
DR TAIR; locus:2164991; AT5G56590.
DR eggNOG; ENOG502QQHU; Eukaryota.
DR HOGENOM; CLU_024953_3_4_1; -.
DR InParanoid; Q9FJU9; -.
DR OMA; AMQNVFT; -.
DR OrthoDB; 966331at2759; -.
DR PhylomeDB; Q9FJU9; -.
DR BioCyc; ARA:AT5G56590-MON; -.
DR PRO; PR:Q9FJU9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJU9; baseline and differential.
DR Genevisible; Q9FJU9; 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:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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: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.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..471
FT /note="Glucan endo-1,3-beta-glucosidase 13"
FT /id="PRO_0000251273"
FT PROPEP 472..506
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000251274"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT LIPID 471
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
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 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 370..433
FT /evidence="ECO:0000250"
SQ SEQUENCE 506 AA; 55604 MW; DC314FEF619BE810 CRC64;
MARDFKLIFS ISILLLLLDC CYGGKVGVCY GRSADDLPTP SKVVQLIQQH NIKYVRIYDY
NSQVLKAFGN TSIELMIGVP NSDLNAFSQS QSNVDTWLKN SVLPYYPTTK ITYITVGAES
TDDPHINASS FVVPAMQNVL TALRKVGLSR RIKVSTTLSL GILSRSFPPS AGAFNSSYAY
FLRPMLEFLA ENKSPFMIDL YPYYAYRDSP NNVSLDYVLF ESSSEVIDPN TGLLYKNMFD
AQVDALYYAL TALNFRTIKI MVTETGWPTK GSPKEKAAAS SDNAETYNSN IIRHVVTNQG
TPAKPGEAMN VYIFSLFNEN RKAGLDSERN WGLFYPDQTS VYQLDFTGKS NGFHSNSSGT
NSSGSSNSWC IASSKASERD LKGALDWACG PGNVDCTAIQ PSQPCFQPDT LVSHASFVFN
SYFQQNRATD VACSFGGAGV KVNKDPSYDK CIYITAGGNK TKATNATALT SSASTPRGNE
LLQWILKLCL MISLFFSLQT MNSQAL
