BGL23_ARATH
ID BGL23_ARATH Reviewed; 524 AA.
AC Q9SR37; B9DH17; O24433; Q42585; Q56YN0;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Beta-glucosidase 23;
DE Short=AtBGLU23;
DE EC=3.2.1.21;
DE AltName: Full=Protein PHOSPHATE STARVATION-RESPONSE 3.1;
DE Flags: Precursor;
GN Name=BGLU23; Synonyms=PSR3.1, PYK10; OrderedLocusNames=At3g09260;
GN ORFNames=F3L24.13;
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 [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Root;
RA Malboobi M.A., Tremblay L., Lefebvre D.D.;
RT "Identification and nucleotide sequences of cDNA clones of phosphate-
RT starvation inducible beta-glucosidase genes of Brassicaceae.";
RL (er) Plant Gene Register PGR96-114(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24;
RX PubMed=11448764; DOI=10.1016/s0168-9452(01)00412-5;
RA Nitz I., Berkefeld H., Puzio P.S., Grundler F.M.;
RT "Pyk10, a seedling and root specific gene and promoter from Arabidopsis
RT thaliana.";
RL Plant Sci. 161:337-346(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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).
RN [8]
RP PROTEIN SEQUENCE OF 25-41, AND SUBCELLULAR LOCATION.
RX PubMed=12581307; DOI=10.1046/j.1365-313x.2003.01636.x;
RA Matsushima R., Kondo M., Nishimura M., Hara-Nishimura I.;
RT "A novel ER-derived compartment, the ER body, selectively accumulates a
RT beta-glucosidase with an ER-retention signal in Arabidopsis.";
RL Plant J. 33:493-502(2003).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15155889; DOI=10.1105/tpc.021154;
RA Matsushima R., Fukao Y., Nishimura M., Hara-Nishimura I.;
RT "NAI1 gene encodes a basic-helix-loop-helix-type putative transcription
RT factor that regulates the formation of an endoplasmic reticulum-derived
RT structure, the ER body.";
RL Plant Cell 16:1536-1549(2004).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15604686; DOI=10.1007/s11103-004-0790-1;
RA Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R.,
RA Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A.;
RT "Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase
RT family 1.";
RL Plant Mol. Biol. 55:343-367(2004).
RN [11]
RP FUNCTION, INDUCTION, ACTIVITY REGULATION, SUBUNIT, DISULFIDE BOND,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PBP1.
RC STRAIN=cv. Columbia;
RX PubMed=15919674; DOI=10.1093/pcp/pci126;
RA Nagano A.J., Matsushima R., Hara-Nishimura I.;
RT "Activation of an ER-body-localized beta-glucosidase via a cytosolic
RT binding partner in damaged tissues of Arabidopsis thaliana.";
RL Plant Cell Physiol. 46:1140-1148(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [13]
RP IDENTIFICATION IN THE PYK10 COMPLEX.
RX PubMed=18467340; DOI=10.1093/pcp/pcn075;
RA Nagano A.J., Fukao Y., Fujiwara M., Nishimura M., Hara-Nishimura I.;
RT "Antagonistic jacalin-related lectins regulate the size of ER body-type
RT beta-glucosidase complexes in Arabidopsis thaliana.";
RL Plant Cell Physiol. 49:969-980(2008).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18248598; DOI=10.1111/j.1365-313x.2008.03424.x;
RA Sherameti I., Venus Y., Drzewiecki C., Tripathi S., Dan V.M., Nitz I.,
RA Varma A., Grundler F.M., Oelmueller R.;
RT "PYK10, a beta-glucosidase located in the endoplasmatic reticulum, is
RT crucial for the beneficial interaction between Arabidopsis thaliana and the
RT endophytic fungus Piriformospora indica.";
RL Plant J. 54:428-439(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=19147648; DOI=10.1093/pcp/pcp007;
RA Ogasawara K., Yamada K., Christeller J.T., Kondo M., Hatsugai N.,
RA Hara-Nishimura I., Nishimura M.;
RT "Constitutive and inducible ER bodies of Arabidopsis thaliana accumulate
RT distinct beta-glucosidases.";
RL Plant Cell Physiol. 50:480-488(2009).
RN [17]
RP MUTAGENESIS OF CYS-29, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=19906837; DOI=10.1093/pcp/pcp157;
RA Nagano A.J., Maekawa A., Nakano R.T., Miyahara M., Higaki T., Kutsuna N.,
RA Hasezawa S., Hara-Nishimura I.;
RT "Quantitative analysis of ER body morphology in an Arabidopsis mutant.";
RL Plant Cell Physiol. 50:2015-2022(2009).
RN [18]
RP INTERACTION WITH AMSH3.
RX PubMed=20543027; DOI=10.1105/tpc.110.075952;
RA Isono E., Katsiarimpa A., Mueller I.K., Anzenberger F., Stierhof Y.-D.,
RA Geldner N., Chory J., Schwechheimer C.;
RT "The deubiquitinating enzyme AMSH3 is required for intracellular
RT trafficking and vacuole biogenesis in Arabidopsis thaliana.";
RL Plant Cell 22:1826-1837(2010).
RN [19]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, INDUCTION, AND ACTIVITY REGULATION.
RX PubMed=19965874; DOI=10.1093/pcp/pcp174;
RA Ahn Y.O., Shimizu B., Sakata K., Gantulga D., Zhou C., Zhou Z., Bevan D.R.,
RA Esen A.;
RT "Scopolin-hydrolyzing beta-glucosidases in roots of Arabidopsis.";
RL Plant Cell Physiol. 51:132-143(2010).
CC -!- FUNCTION: Beta-D-glucosidase active on scopolin > esculin >> 4-MU-
CC glucoside >> DIMBOA-glucoside. No activity with pNP-glucoside, oNP-
CC glucoside and sinigrin as substrates. May possess beta-D-fucosidase
CC activity. Required for the beneficial interaction with the endophytic
CC fungus P.indica. May participate in the control of root colonization by
CC P.indica by repressing defense responses and modulating other responses
CC required for a mutualistic interaction. {ECO:0000269|PubMed:15155889,
CC ECO:0000269|PubMed:15919674, ECO:0000269|PubMed:18248598,
CC ECO:0000269|PubMed:19965874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC with release of beta-D-glucose.; EC=3.2.1.21;
CC Evidence={ECO:0000269|PubMed:19965874};
CC -!- ACTIVITY REGULATION: Activated by tissue damage and upon binding to
CC PBP1 or PBP2. {ECO:0000269|PubMed:15919674,
CC ECO:0000269|PubMed:19965874}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.81 mM for scopolin (with recombinant enzyme)
CC {ECO:0000269|PubMed:19965874};
CC KM=0.73 mM for scopolin (with native enzyme)
CC {ECO:0000269|PubMed:19965874};
CC KM=9.7 mM for esculin (with recombinant enzyme)
CC {ECO:0000269|PubMed:19965874};
CC KM=5.8 mM for esculin (with native enzyme)
CC {ECO:0000269|PubMed:19965874};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:19965874};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:19965874};
CC -!- SUBUNIT: Homodimers. Binds to the deubiquitinating enzyme AMSH3. The
CC inactive form interacts with PBP1/JAL30 to form the PYK10 complex, at
CC least composed of PYK10/BGLU23, BGLU21, BGLU22, JAL22, JAL23,
CC PBP1/JAL30, PBP2/JAL31, JAL32, JAL33, JAL34, JAL35, GLL22 and GLL23.
CC {ECO:0000269|PubMed:15919674, ECO:0000269|PubMed:18467340,
CC ECO:0000269|PubMed:19906837, ECO:0000269|PubMed:20543027}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:12581307,
CC ECO:0000269|PubMed:15155889, ECO:0000269|PubMed:15919674,
CC ECO:0000269|PubMed:18248598, ECO:0000269|PubMed:19147648}. Note=Located
CC in ER bodies.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in roots.
CC {ECO:0000269|PubMed:11448764, ECO:0000269|PubMed:19965874}.
CC -!- INDUCTION: Up-regulated by wounding, 2,4-D and methyl jasmonate (MeJA).
CC Down-regulated by salt and mannitol. {ECO:0000269|PubMed:15919674,
CC ECO:0000269|PubMed:19965874}.
CC -!- PTM: Forms interchain disulfide bonds.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB38783.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD94012.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U72153; AAB38783.1; ALT_FRAME; mRNA.
DR EMBL; X89413; CAA61592.1; -; mRNA.
DR EMBL; AJ243490; CAB50792.1; -; Genomic_DNA.
DR EMBL; AC011436; AAF14024.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74744.1; -; Genomic_DNA.
DR EMBL; AF386967; AAK62412.1; -; mRNA.
DR EMBL; AY136440; AAM97105.1; -; mRNA.
DR EMBL; AY140060; AAM98201.1; -; mRNA.
DR EMBL; BT000230; AAN15549.1; -; mRNA.
DR EMBL; AK221291; BAD94012.1; ALT_INIT; mRNA.
DR EMBL; AK226844; BAE98937.1; -; mRNA.
DR EMBL; AK230345; BAF02144.1; -; mRNA.
DR EMBL; AK317362; BAH20034.1; -; mRNA.
DR EMBL; AK317443; BAH20110.1; -; mRNA.
DR PIR; S57621; S57621.
DR RefSeq; NP_187537.1; NM_111760.3.
DR AlphaFoldDB; Q9SR37; -.
DR SMR; Q9SR37; -.
DR BioGRID; 5416; 6.
DR STRING; 3702.AT3G09260.1; -.
DR CAZy; GH1; Glycoside Hydrolase Family 1.
DR MetOSite; Q9SR37; -.
DR SwissPalm; Q9SR37; -.
DR PaxDb; Q9SR37; -.
DR PRIDE; Q9SR37; -.
DR ProteomicsDB; 240418; -.
DR EnsemblPlants; AT3G09260.1; AT3G09260.1; AT3G09260.
DR GeneID; 820082; -.
DR Gramene; AT3G09260.1; AT3G09260.1; AT3G09260.
DR KEGG; ath:AT3G09260; -.
DR Araport; AT3G09260; -.
DR TAIR; locus:2083524; AT3G09260.
DR eggNOG; KOG0626; Eukaryota.
DR HOGENOM; CLU_001859_1_0_1; -.
DR InParanoid; Q9SR37; -.
DR OMA; IGYCAWS; -.
DR OrthoDB; 408001at2759; -.
DR PhylomeDB; Q9SR37; -.
DR BioCyc; ARA:AT3G09260-MON; -.
DR BRENDA; 3.2.1.21; 399.
DR PRO; PR:Q9SR37; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR37; baseline and differential.
DR Genevisible; Q9SR37; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0010168; C:ER body; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008422; F:beta-glucosidase activity; IDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0015928; F:fucosidase activity; TAS:TAIR.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0019137; F:thioglucosidase activity; IDA:TAIR.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0070417; P:cellular response to cold; IEP:TAIR.
DR GO; GO:0080119; P:ER body organization; IMP:TAIR.
DR GO; GO:0019762; P:glucosinolate catabolic process; IDA:TAIR.
DR GO; GO:0019760; P:glucosinolate metabolic process; IDA:TAIR.
DR GO; GO:0042344; P:indole glucosinolate catabolic process; IDA:TAIR.
DR GO; GO:0042343; P:indole glucosinolate metabolic process; IDA:TAIR.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IBA:GO_Central.
DR GO; GO:0009610; P:response to symbiotic fungus; IMP:TAIR.
DR InterPro; IPR001360; Glyco_hydro_1.
DR InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10353; PTHR10353; 1.
DR Pfam; PF00232; Glyco_hydro_1; 1.
DR PRINTS; PR00131; GLHYDRLASE1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:12581307"
FT CHAIN 25..524
FT /note="Beta-glucosidase 23"
FT /id="PRO_0000389585"
FT MOTIF 521..524
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 418
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 475..476
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 222..230
FT /evidence="ECO:0000250"
FT MUTAGEN 29
FT /note="C->Y: In leb-1; loss of homodimerization resulting
FT in fewer and larger ER bodies."
FT /evidence="ECO:0000269|PubMed:19906837"
FT CONFLICT 208
FT /note="S -> L (in Ref. 2; CAB50792/CAA61592)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="C -> S (in Ref. 1; AAB38783)"
FT /evidence="ECO:0000305"
FT CONFLICT 400
FT /note="S -> G (in Ref. 6; BAD94012)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="K -> E (in Ref. 7; BAH20034)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 59721 MW; 4758EA7A9B8336E1 CRC64;
MVLQKLPLIG LLLLLTIVAS PANADGPVCP PSNKLSRASF PEGFLFGTAT AAYQVEGAIN
ETCRGPALWD IYCRRYPERC NNDNGDVAVD FFHRYKEDIQ LMKNLNTDAF RMSIAWPRIF
PHGRKEKGVS QAGVQFYHDL IDELIKNGIT PFVTVFHWDT PQDLEDEYGG FLSERIVKDF
REYADFVFQE YGGKVKHWIT FNEPWVFSHA GYDVGKKAPG RCSSYVNAKC QDGRSGYEAY
LVTHNLLISH AEAVEAYRKC EKCKGGKIGI AHSPAWFEAH DLADSQDGAS IDRALDFILG
WHLDTTTFGD YPQIMKDIVG HRLPKFTTEQ KAKLKASTDF VGLNYYTSVF SNHLEKPDPS
KPRWMQDSLI TWESKNAQNY AIGSKPLTAA LNVYSRGFRS LLKYIKDKYA NPEIMIMENG
YGEELGASDS VAVGTADHNR KYYLQRHLLS MQEAVCIDKV NVTGYFVWSL LDNFEWQDGY
KNRFGLYYVD FKNNLTRYEK ESGKYYKDFL SQGVRPSALK KDEL
