P37702 (BGL38_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Myrosinase 1
EC=3.2.1.147

Alternative name(s):
Beta-glucosidase 38
Short name=AtBGLU38
EC=3.2.1.21
Sinigrinase 1
Thioglucosidase 1

Gene names

Name:	TGG1
Synonyms:	BGLU38
Ordered Locus Names:	At5g26000
ORF Names:	T1N24.7

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	541 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Degradation of glucosinolates (glucose residue linked by a thioglucoside bound to an amino acid derivative) to glucose, sulfate and any of the products: thiocyanates, isothiocyanates, nitriles, epithionitriles or oxazolidine-2-thiones. These toxic degradation products can deter insect herbivores. Seems to function in abscisic acid (ABA) and methyl jasmonate (MeJA) signaling in guard cells. Functionally redundant with TGG2. Hydrolyzes sinigrin and, with lower efficiency, p-nitrophenyl beta-D-glucoside. Ref.7 Ref.12 Ref.13 Ref.14
Catalytic activity	A thioglucoside + H2O = a sugar + a thiol. Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.
Subunit structure	Homodimer By similarity.
Subcellular location	Vacuole By similarity.
Tissue specificity	Expressed in guard cells, phloem-associated cells and myrosin cells. Ref.10
Miscellaneous	It seems that the absence of a catalytic proton donor in plant myrosinases is not impairing the hydrolysis of glucosinolates.
Sequence similarities	Belongs to the glycosyl hydrolase 1 family.
Biophysicochemical properties	Kinetic parameters: KM=45 µM for sinigrin (at pH 4.5) Ref.13 KM=34 mM for p-nitrophenyl beta-D-glucoside (at pH 4.5) Vmax=2.3 µmol/min/mg enzyme with sinigrin as substrate (at pH 4.5) Vmax=1.2 µmol/min/mg enzyme with p-nitrophenyl beta-D-glucoside as substrate (at pH 4.5)

Ontologies

Keywords
Biological process	Abscisic acid signaling pathway Plant defense
Cellular component	Vacuole
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	abscisic acid mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro defense response to insect Inferred from mutant phenotype Ref.12. Source: UniProtKB glucosinolate catabolic process Inferred from mutant phenotype Ref.12. Source: TAIR regulation of stomatal movement Inferred from mutant phenotype Ref.14. Source: UniProtKB response to abscisic acid stimulus Inferred from mutant phenotype Ref.14. Source: UniProtKB
Cellular_component	apoplast Inferred from direct assay PubMed 18538804. Source: TAIR chloroplast Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR cytosolic ribosome Inferred from direct assay PubMed 15821981. Source: TAIR peroxisome Inferred from direct assay PubMed 17951448. Source: TAIR plant-type cell wall Inferred from direct assay PubMed 17526915. Source: TAIR thylakoid Inferred from direct assay PubMed 16648217. Source: TAIR vacuole Inferred from direct assay PubMed 15539469. Source: TAIR
Molecular_function	beta-glucosidase activity Inferred from direct assay Ref.13. Source: TAIR metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW thioglucosidase activity Inferred from mutant phenotype Ref.12. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P37702-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P37702-2)

The sequence of this isoform differs from the canonical sequence as follows:
     457-541: Missing.

Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 541	522	Myrosinase 1		PRO_0000011773
Regions
	Region	475 – 476	2	Substrate binding By similarity
Sites
	Active site	420	1	Nucleophile By similarity
	Metal binding	74	1	Zinc; shared with dimeric partner By similarity
	Metal binding	88	1	Zinc; shared with dimeric partner By similarity
	Binding site	57	1	Substrate By similarity
	Binding site	159	1	Substrate By similarity
	Binding site	204	1	Substrate By similarity
	Binding site	205	1	Ascorbate By similarity
	Binding site	278	1	Ascorbate By similarity
	Binding site	348	1	Substrate By similarity
	Binding site	468	1	Substrate By similarity
Amino acid modifications
	Glycosylation	33	1	N-linked (GlcNAc...) Potential
	Glycosylation	108	1	N-linked (GlcNAc...) Potential
	Glycosylation	175	1	N-linked (GlcNAc...) Potential
	Glycosylation	236	1	N-linked (GlcNAc...) Potential
	Glycosylation	356	1	N-linked (GlcNAc...) Potential
	Glycosylation	379	1	N-linked (GlcNAc...) Potential
	Glycosylation	493	1	N-linked (GlcNAc...) Potential
	Glycosylation	512	1	N-linked (GlcNAc...) Potential
	Disulfide bond	24 ↔ 449		By similarity
	Disulfide bond	32 ↔ 445		By similarity
	Disulfide bond	224 ↔ 232		By similarity
Natural variations
	Alternative sequence	457 – 541	85	Missing in isoform 2.		VSP_038446
	Natural variant	128	1	S → N in strain: cv. Ta-0. Ref.7
	Natural variant	261	1	T → K in strain: cv. Ba-1. Ref.7
	Natural variant	264	1	K → Q in strain: cv. Ba-1. Ref.7
	Natural variant	427	1	G → A in strain: cv. Ag-0, cv. Ba-1, cv. Mh-0, cv. Mr-0 and Tac-0. Ref.7
	Natural variant	459	1	N → G in strain: cv. Su-0. Ref.7
	Natural variant	489	1	V → I in strain: cv. No-0, cv. Rsch-0 and cv. Ta-0. Ref.7
Experimental info
	Sequence conflict	385	1	P → H in AAL06896. Ref.5
	Sequence conflict	426	1	P → A in AAL25596. Ref.5
	Sequence conflict	434	1	A → T in BAH20253. Ref.8
	Sequence conflict	441	1	I → N in BAH20253. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 3736B735DE7A5BD1	FASTA	541	61,133
	10 20 30 40 50 60 MKLLMLAFVF LLALATCKGD EFVCEENEPF TCNQTKLFNS GNFEKGFIFG VASSAYQVEG 70 80 90 100 110 120 GRGRGLNVWD SFTHRFPEKG GADLGNGDTT CDSYTLWQKD IDVMDELNST GYRFSIAWSR 130 140 150 160 170 180 LLPKGKRSRG VNPGAIKYYN GLIDGLVAKN MTPFVTLFHW DLPQTLQDEY NGFLNKTIVD 190 200 210 220 230 240 DFKDYADLCF ELFGDRVKNW ITINQLYTVP TRGYALGTDA PGRCSPKIDV RCPGGNSSTE 250 260 270 280 290 300 PYIVAHNQLL AHAAAVDVYR TKYKDDQKGM IGPVMITRWF LPFDHSQESK DATERAKIFF 310 320 330 340 350 360 HGWFMGPLTE GKYPDIMREY VGDRLPEFSE TEAALVKGSY DFLGLNYYVT QYAQNNQTIV 370 380 390 400 410 420 PSDVHTALMD SRTTLTSKNA TGHAPGPPFN AASYYYPKGI YYVMDYFKTT YGDPLIYVTE 430 440 450 460 470 480 NGFSTPGDED FEKATADYKR IDYLCSHLCF LSKVIKEKNV NVKGYFAWSL GDNYEFCNGF 490 500 510 520 530 540 TVRFGLSYVD FANITGDRDL KASGKWFQKF INVTDEDSTN QDLLRSSVSS KNRDRKSLAD A
	Isoform 2 [UniParc]. Checksum: DE7CE563F352A0BB	FASTA	456	51,481
	10 20 30 40 50 60 MKLLMLAFVF LLALATCKGD EFVCEENEPF TCNQTKLFNS GNFEKGFIFG VASSAYQVEG 70 80 90 100 110 120 GRGRGLNVWD SFTHRFPEKG GADLGNGDTT CDSYTLWQKD IDVMDELNST GYRFSIAWSR 130 140 150 160 170 180 LLPKGKRSRG VNPGAIKYYN GLIDGLVAKN MTPFVTLFHW DLPQTLQDEY NGFLNKTIVD 190 200 210 220 230 240 DFKDYADLCF ELFGDRVKNW ITINQLYTVP TRGYALGTDA PGRCSPKIDV RCPGGNSSTE 250 260 270 280 290 300 PYIVAHNQLL AHAAAVDVYR TKYKDDQKGM IGPVMITRWF LPFDHSQESK DATERAKIFF 310 320 330 340 350 360 HGWFMGPLTE GKYPDIMREY VGDRLPEFSE TEAALVKGSY DFLGLNYYVT QYAQNNQTIV 370 380 390 400 410 420 PSDVHTALMD SRTTLTSKNA TGHAPGPPFN AASYYYPKGI YYVMDYFKTT YGDPLIYVTE 430 440 450 NGFSTPGDED FEKATADYKR IDYLCSHLCF LSKVIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis cDNA sequence encoding myrosinase." Chadchawan S., Bishop J., Thangstad O.P., Bones A.M., Mitchell-Olds T., Bradley D. Plant Physiol. 103:671-671(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: cv. Columbia.
[2]	"The myrosinase gene family in Arabidopsis thaliana: gene organization, expression and evolution." Xue J., Joergensen M., Pihlgren U., Rask L. Plant Mol. Biol. 27:911-922(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia. Tissue: Leaf.
[3]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells." Stracke R., Palme K. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-226.
[7]	"Nucleotide variation at the myrosinase-encoding locus, TGG1, and quantitative myrosinase enzyme activity variation in Arabidopsis thaliana." Stranger B.E., Mitchell-Olds T. Mol. Ecol. 14:295-309(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-497; 43-510; 43-511; 43-512; 43-513; 43-514; 44-511; 44-512; 44-514; 44-522; 45-511 AND 47-512, FUNCTION, VARIANTS ASN-128; LYS-261; GLN-264; ALA-427; GLY-459 AND ILE-489. Strain: cv. Abd-0, cv. Ag-0, cv. Ba-1, cv. Cal-0, cv. Columbia, cv. Cvi-0, cv. Db-1, cv. Ei-2, cv. HOG, cv. Ka-0, cv. Ler-1, cv. Lip-0, cv. Ll-0, cv. Mh-0, cv. Mr-0, cv. Mrk-0, cv. Mt-0, cv. No-0, cv. Per-1, cv. Petergof, cv. Pi-0, cv. Rsch-0, cv. Sei-0, cv. Su-0, cv. Ta-0, cv. Tac-0, cv. Tsu-1 and cv. Wl-0.
[8]	"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs." Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K. DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-541. Strain: cv. Columbia.
[9]	"An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana." Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M., Cooke R. , Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B. Plant J. 4:1051-1061(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 192-250. Strain: cv. C24. Tissue: Flower bud.
[10]	"Cell specific, cross-species expression of myrosinases in Brassica napus, Arabidopsis thaliana and Nicotiana tabacum." Thangstad O.P., Gilde B., Chadchawan S., Seem M., Husebye H., Bradley D., Bones A.M. Plant Mol. Biol. 54:597-611(2004) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[11]	"Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1." Xu Z., Escamilla-Trevino L.L., Zeng L., Lalgondar M., Bevan D.R., Winkel B.S.J., Mohamed A., Cheng C.-L., Shih M.-C., Poulton J.E., Esen A. Plant Mol. Biol. 55:343-367(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[12]	"Arabidopsis myrosinases TGG1 and TGG2 have redundant function in glucosinolate breakdown and insect defense." Barth C., Jander G. Plant J. 46:549-562(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Myrosinases from root and leaves of Arabidopsis thaliana have different catalytic properties." Andersson D., Chakrabarty R., Bejai S., Zhang J., Rask L., Meijer J. Phytochemistry 70:1345-1354(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[14]	"Myrosinases, TGG1 and TGG2, redundantly function in ABA and MeJA signaling in Arabidopsis guard cells." Islam M.M., Tani C., Watanabe-Sugimoto M., Uraji M., Jahan M.S., Masuda C., Nakamura Y., Mori I.C., Murata Y. Plant Cell Physiol. 50:1171-1175(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L11454 mRNA. Translation: AAC18869.1. X79194 Genomic DNA. Translation: CAA55786.1. AF149413 Genomic DNA. Translation: AAD40143.1. CP002688 Genomic DNA. Translation: AED93511.1. CP002688 Genomic DNA. Translation: AED93512.1. AY045681 mRNA. Translation: AAK74039.1. AY054237 mRNA. Translation: AAL06896.1. AY058182 mRNA. Translation: AAL25596.1. AY090382 mRNA. Translation: AAL91284.1. AF083677 mRNA. Translation: AAN60236.1. AJ831440 Genomic DNA. Translation: CAH40799.1. AJ831441 Genomic DNA. Translation: CAH40800.1. AJ831442 Genomic DNA. Translation: CAH40801.1. AJ831443 Genomic DNA. Translation: CAH40802.1. AJ831444 Genomic DNA. Translation: CAH40803.1. AJ831445 Genomic DNA. Translation: CAH40804.1. AJ831446 Genomic DNA. Translation: CAH40805.1. AJ831447 Genomic DNA. Translation: CAH40806.1. AJ831448 Genomic DNA. Translation: CAH40807.1. AJ831449 Genomic DNA. Translation: CAH40808.1. AJ831450 Genomic DNA. Translation: CAH40809.1. AJ831451 Genomic DNA. Translation: CAH40810.1. AJ831452 Genomic DNA. Translation: CAH40811.1. AJ831453 Genomic DNA. Translation: CAH40812.1. AJ831454 Genomic DNA. Translation: CAH40813.1. AJ831455 Genomic DNA. Translation: CAH40814.1. AJ831456 Genomic DNA. Translation: CAH40815.1. AJ831457 Genomic DNA. Translation: CAH40816.1. AJ831458 Genomic DNA. Translation: CAH40817.1. AJ831459 Genomic DNA. Translation: CAH40818.1. AJ831460 Genomic DNA. Translation: CAH40819.1. AJ831461 Genomic DNA. Translation: CAH40820.1. AJ831462 Genomic DNA. Translation: CAH40821.1. AJ831463 Genomic DNA. Translation: CAH40822.1. AJ831464 Genomic DNA. Translation: CAH40823.1. AJ831465 Genomic DNA. Translation: CAH40824.1. AJ831466 Genomic DNA. Translation: CAH40825.1. AJ831467 Genomic DNA. Translation: CAH40826.1. AK317589 mRNA. Translation: BAH20253.1. Z18232 mRNA. Translation: CAA79143.1.
IPI	IPI00522086. IPI00539116.
PIR	S56653.
RefSeq	NP_197972.2. NM_122501.3. NP_851077.1. NM_180746.2.
UniGene	At.23592. At.47944. At.73176.
3D structure databases
ProteinModelPortal	P37702.
SMR	P37702. Positions 21-512.
ModBase	Search...
Protein-protein interaction databases
IntAct	P37702. 1 interaction.
Protein family/group databases
CAZy	GH1. Glycoside Hydrolase Family 1.
2D gel databases
SWISS-2DPAGE	P37702.
Proteomic databases
PRIDE	P37702.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G26000.1; AT5G26000.1; AT5G26000.
GeneID	832669.
KEGG	ath:AT5G26000.
Organism-specific databases
TAIR	At5g26000.
Phylogenomic databases
InParanoid	P37702.
OMA	NWITINQ.
PhylomeDB	P37702.
ProtClustDB	CLSN2689871.
Enzyme and pathway databases
BioCyc	MetaCyc:AT5G26000-MONOMER.
SABIO-RK	P37702.
Gene expression databases
Genevestigator	P37702.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR001360. Glyco_hydro_1. IPR018120. Glyco_hydro_1_AS. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
PANTHER	PTHR10353. PTHR10353. 1 hit.
Pfam	PF00232. Glyco_hydro_1. 1 hit. [Graphical view]
PRINTS	PR00131. GLHYDRLASE1.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00572. GLYCOSYL_HYDROL_F1_1. 1 hit. PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BGL38_ARATH

Accession

Primary (citable) accession number: P37702
Secondary accession number(s): B9DHN6 , Q3E942, Q3V5A7, Q3V5A8, Q3V5A9, Q3V5B1, Q3V5B2, Q3V5B3, Q3V5B4, Q3V5B5, Q3V5B6, Q3V5B7, Q3V5B8, Q3V5B9, Q3V5C0, Q3V5C2, Q3V5C3, Q3V5C4, Q3V5C5, Q3V5C8, Q3V5D1, Q3V5D2, Q8H7H2, Q93Z31, Q940N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program