E1314_ARATH
ID E1314_ARATH Reviewed; 392 AA.
AC Q9ZQG9; Q2V449; Q3EBS8; Q8VWJ3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase 14;
DE EC=3.2.1.39;
DE AltName: Full=(1->3)-beta-glucan endohydrolase 14;
DE Short=(1->3)-beta-glucanase 14;
DE AltName: Full=Beta-1,3-endoglucanase 14;
DE Short=Beta-1,3-glucanase 14;
DE Flags: Precursor;
GN OrderedLocusNames=At2g27500; ORFNames=F10A12.18;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] (ISOFORM 1).
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] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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: [Isoform 1]: Cell membrane {ECO:0000305}; Lipid-
CC anchor, GPI-anchor {ECO:0000305}; Extracellular side {ECO:0000305}.
CC Secreted, cell wall {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted, cell wall {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ZQG9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZQG9-2; Sequence=VSP_020755;
CC Name=3;
CC IsoId=Q9ZQG9-3; Sequence=VSP_020754;
CC -!- MISCELLANEOUS: [Isoform 2]: Has no GPI-anchor. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Has no GPI-anchor. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC006232; AAD15611.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08004.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08005.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08006.1; -; Genomic_DNA.
DR EMBL; AY096525; AAM20175.1; -; mRNA.
DR EMBL; AY065273; AAL38749.1; -; mRNA.
DR EMBL; AY065085; AAL38261.1; -; mRNA.
DR EMBL; AY084587; AAM61152.1; -; mRNA.
DR PIR; F84673; F84673.
DR RefSeq; NP_001031432.1; NM_001036355.1. [Q9ZQG9-3]
DR RefSeq; NP_565652.1; NM_128310.4. [Q9ZQG9-1]
DR RefSeq; NP_973548.1; NM_201819.2. [Q9ZQG9-2]
DR AlphaFoldDB; Q9ZQG9; -.
DR SMR; Q9ZQG9; -.
DR STRING; 3702.AT2G27500.1; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; Q9ZQG9; -.
DR PRIDE; Q9ZQG9; -.
DR ProteomicsDB; 222025; -. [Q9ZQG9-1]
DR EnsemblPlants; AT2G27500.1; AT2G27500.1; AT2G27500. [Q9ZQG9-1]
DR EnsemblPlants; AT2G27500.2; AT2G27500.2; AT2G27500. [Q9ZQG9-2]
DR EnsemblPlants; AT2G27500.3; AT2G27500.3; AT2G27500. [Q9ZQG9-3]
DR GeneID; 817295; -.
DR Gramene; AT2G27500.1; AT2G27500.1; AT2G27500. [Q9ZQG9-1]
DR Gramene; AT2G27500.2; AT2G27500.2; AT2G27500. [Q9ZQG9-2]
DR Gramene; AT2G27500.3; AT2G27500.3; AT2G27500. [Q9ZQG9-3]
DR KEGG; ath:AT2G27500; -.
DR Araport; AT2G27500; -.
DR TAIR; locus:2038583; AT2G27500.
DR eggNOG; ENOG502QQ1M; Eukaryota.
DR InParanoid; Q9ZQG9; -.
DR OMA; CINSNVT; -.
DR PhylomeDB; Q9ZQG9; -.
DR BioCyc; ARA:AT2G27500-MON; -.
DR PRO; PR:Q9ZQG9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQG9; baseline and differential.
DR Genevisible; Q9ZQG9; AT.
DR GO; GO:0046658; C:anchored component of plasma membrane; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; 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 PANTHER; PTHR32227; PTHR32227; 1.
DR Pfam; PF00332; Glyco_hydro_17; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cell wall;
KW Cell wall biogenesis/degradation; Cytoplasm; Glycoprotein; Glycosidase;
KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Plant defense;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..359
FT /note="Glucan endo-1,3-beta-glucosidase 14"
FT /id="PRO_0000251275"
FT PROPEP 360..392
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000251276"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 267
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT LIPID 359
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_020754"
FT VAR_SEQ 366..392
FT /note="ILNLWRVVMGLAVAWFILDMGDKMRMR -> VNSSFHFLYLHF (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_020755"
SQ SEQUENCE 392 AA; 44074 MW; 67206B809BB7322A CRC64;
MATHSLSFFF RVLLLLFLTL SERIKGQGVG INYGQIANNL PSPARVAVLL RSLNITRVKL
YDADPNVLFS FSNSQVDFMI GLGNEYLQNM STDPTKAQDW LQQRLEPHIS KTRITSIVVG
NEIFKTNDHV LIQSLLPAMK SVYAALTNLG LEKQVTVTSA HSLDILSTSY PPSSGSFKEE
FIQYLQPLLD FHSQIESPFL INAYPFFAYK DSPKEVPLEY VLFQPNQGMV DPNTNLHYDN
MLFAQVDALY SAIKTLGHTD IEVRISETGW PSKGDENEIG ASPENAALYN GNLLKLIQQR
KGTPAKQSVP IDVYVFALFN ENLKPGPVSE RNYGLFYPDG KPVYNVGMQG YLPDIIYTSR
ATTIKILNLW RVVMGLAVAW FILDMGDKMR MR
