E1311_ARATH
ID E1311_ARATH Reviewed; 426 AA.
AC Q8L868; Q9MAQ2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase 11;
DE EC=3.2.1.39;
DE AltName: Full=(1->3)-beta-glucan endohydrolase 11;
DE Short=(1->3)-beta-glucanase 11;
DE AltName: Full=Beta-1,3-endoglucanase 11;
DE Short=Beta-1,3-glucanase 11;
DE Flags: Precursor;
GN OrderedLocusNames=At1g32860; ORFNames=F9L11.6;
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: Secreted, cell wall {ECO:0000305}. Cell membrane;
CC Lipid-anchor, GPI-anchor; Extracellular side.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF31288.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006424; AAF31288.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31533.1; -; Genomic_DNA.
DR EMBL; AY120710; AAM53268.1; -; mRNA.
DR EMBL; BT000048; AAN15367.1; -; mRNA.
DR PIR; D86453; D86453.
DR RefSeq; NP_174563.2; NM_103020.3.
DR AlphaFoldDB; Q8L868; -.
DR SMR; Q8L868; -.
DR STRING; 3702.AT1G32860.1; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR PaxDb; Q8L868; -.
DR PRIDE; Q8L868; -.
DR ProteomicsDB; 222005; -.
DR EnsemblPlants; AT1G32860.1; AT1G32860.1; AT1G32860.
DR GeneID; 840180; -.
DR Gramene; AT1G32860.1; AT1G32860.1; AT1G32860.
DR KEGG; ath:AT1G32860; -.
DR Araport; AT1G32860; -.
DR TAIR; locus:2037905; AT1G32860.
DR eggNOG; ENOG502QR6V; Eukaryota.
DR HOGENOM; CLU_024953_1_2_1; -.
DR InParanoid; Q8L868; -.
DR OMA; NCNLMKL; -.
DR OrthoDB; 966331at2759; -.
DR PhylomeDB; Q8L868; -.
DR BioCyc; ARA:AT1G32860-MON; -.
DR PRO; PR:Q8L868; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L868; baseline and differential.
DR Genevisible; Q8L868; 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: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 Cell membrane; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Plant defense;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..398
FT /note="Glucan endo-1,3-beta-glucosidase 11"
FT /id="PRO_0000251269"
FT PROPEP 399..426
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000251270"
FT REGION 360..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
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 398
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 426 AA; 45421 MW; E40288A0C0543540 CRC64;
MELTSFHRSS LLFLISLTLI ILPTTTTSIG VNYGQIGDNL PSPTDVIPLI KSIGATKVKL
YDANPQILKA FSNTGIEFII GLGNEYLSKM KDPSKALTWI KQNVTPFLPA TNITCITIGN
EILALNDSSL TTNLLPAMQG VHSALITAGL SDQISVTTAH SLSILKSSFP PSAGEFQPDL
LDSLTPILEF HRKTDSPFLI NAYPFFAYKG NPKEVPLDFV LFQPNQGIVD PATGFHYDNM
LFAQIDAVYS ALAAAGFKSL RVEISETGWP SKGDDDEVGA TPENAKRYNG NLIKMMMSGK
KTKTPLKPNN DLSIYVFALF NENLKPGPTS ERNYGLFKPD GTQAYSLGFA LNDVVRGASG
GGTGGGNSSS GGGRDKSPVF PVSPVAPDSA STGYLAISAS PVTGKRKGKG AILSLVVSML
LARHLL
