E134_ARATH
ID E134_ARATH Reviewed; 505 AA.
AC Q94CD8; B9DGU2; Q9LJD6;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase 4;
DE EC=3.2.1.39;
DE AltName: Full=(1->3)-beta-glucan endohydrolase 4;
DE Short=(1->3)-beta-glucanase 4;
DE AltName: Full=Beta-1,3-endoglucanase 4;
DE Short=Beta-1,3-glucanase 4;
DE Flags: Precursor;
GN OrderedLocusNames=At3g13560; ORFNames=MRP15.22;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
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=BAB01763.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000603; BAB01763.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75372.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75373.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75374.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64915.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64916.1; -; Genomic_DNA.
DR EMBL; AY034940; AAK59446.1; -; mRNA.
DR EMBL; AY063117; AAL34291.1; -; mRNA.
DR EMBL; AK317283; BAH19959.1; -; mRNA.
DR RefSeq; NP_001326916.1; NM_001338056.1.
DR RefSeq; NP_001326917.1; NM_001338055.1.
DR RefSeq; NP_187965.1; NM_112202.5.
DR RefSeq; NP_974302.1; NM_202573.3.
DR RefSeq; NP_974303.1; NM_202574.3.
DR AlphaFoldDB; Q94CD8; -.
DR SMR; Q94CD8; -.
DR STRING; 3702.AT3G13560.2; -.
DR CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; Q94CD8; -.
DR PRIDE; Q94CD8; -.
DR ProteomicsDB; 222007; -.
DR EnsemblPlants; AT3G13560.1; AT3G13560.1; AT3G13560.
DR EnsemblPlants; AT3G13560.2; AT3G13560.2; AT3G13560.
DR EnsemblPlants; AT3G13560.3; AT3G13560.3; AT3G13560.
DR EnsemblPlants; AT3G13560.4; AT3G13560.4; AT3G13560.
DR EnsemblPlants; AT3G13560.5; AT3G13560.5; AT3G13560.
DR GeneID; 820558; -.
DR Gramene; AT3G13560.1; AT3G13560.1; AT3G13560.
DR Gramene; AT3G13560.2; AT3G13560.2; AT3G13560.
DR Gramene; AT3G13560.3; AT3G13560.3; AT3G13560.
DR Gramene; AT3G13560.4; AT3G13560.4; AT3G13560.
DR Gramene; AT3G13560.5; AT3G13560.5; AT3G13560.
DR KEGG; ath:AT3G13560; -.
DR Araport; AT3G13560; -.
DR TAIR; locus:2092855; AT3G13560.
DR eggNOG; ENOG502QS8U; Eukaryota.
DR HOGENOM; CLU_024953_3_3_1; -.
DR InParanoid; Q94CD8; -.
DR OMA; NFNSTAM; -.
DR OrthoDB; 966331at2759; -.
DR PhylomeDB; Q94CD8; -.
DR BioCyc; ARA:AT3G13560-MON; -.
DR PRO; PR:Q94CD8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94CD8; baseline and differential.
DR Genevisible; Q94CD8; 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:0005829; C:cytosol; HDA: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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..474
FT /note="Glucan endo-1,3-beta-glucosidase 4"
FT /id="PRO_0000011888"
FT PROPEP 475..505
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000011889"
FT ACT_SITE 119
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT LIPID 474
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
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 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 363..426
FT /evidence="ECO:0000250"
SQ SEQUENCE 505 AA; 54416 MW; 4C6CA8CA9952B671 CRC64;
MLLPRWFAEA LLLLLSILAC SNAAFIGVNI GTDLTNMPPP SDIVTLLKSQ QITHVRLYDA
NSHMLKAFAN TSIEVMVGVT NEEILKIGRF PSAAAAWVNK NVAAYIPSTN ITAIAVGSEV
LTTIPHVAPI LASALNNIHK ALVASNLNFK VKVSSPMSMD IMPKPFPPST STFSPSWNTT
VYQLLQFLKN TGSFFMLNAY PYYGYTTANG IFPLDYALFK QLSPVKQIVD PNTLLHYNSM
FDAMVDAAYY SMEALNFSKI PVVVTETGWP SSGGSDEAAA TVANAETFNT NLIKRVLNNS
GPPSQPDIPI NTYIYELYNE DKRSGPVSER NWGILFPNGT SVYPLSLSGG SSSAALNGSS
MFCVAKADAD DDKLVDGLNW ACGQGRANCA AIQPGQPCYL PNDVKSHASF AFNDYYQKMK
SAGGTCDFDG TAITTTRDPS YRTCAYTGSL NANATNGNFP PDALGPASPL GGNANARIIF
SYHLPILAPL ALTLLQLLLQ HDRLL
