P52407 (E13B_HEVBR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glucan endo-1,3-beta-glucosidase, basic vacuolar isoform
EC=3.2.1.39

Alternative name(s):
(1->3)-beta-glucan endohydrolase
Short name=(1->3)-beta-glucanase
Beta-1,3-endoglucanase

Cleaved into the following 4 chains:

1. Glucan endo-1,3-beta-glucosidase minor form 3
2. Glucan endo-1,3-beta-glucosidase minor form 2
3. Glucan endo-1,3-beta-glucosidase minor form 1
4. Glucan endo-1,3-beta-glucosidase major form

Gene names

Name:

HGN1

Organism

Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis)

Taxonomic identifier

3981 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Malpighiales › Euphorbiaceae › Crotonoideae › Micrandreae › Hevea

Protein attributes

Sequence length	374 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	Is thought to be an important plant defense-related product against fungal pathogens.
Catalytic activity	Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Subunit structure	Monomer. Ref.4
Subcellular location	Vacuole Potential.
Tissue specificity	Expressed at highest levels in laticifer cells of the petiole. Ref.1
Post-translational modification	Glycosylated in cv. GT.1 and cv. RRIM 600 but not in cv. PR 261. Asn-350 is glycosylated only in cv. GT.1 due to the presence of Ser-352. In cv. PR 261 and cv. RRIM 600, Ser-352 is replaced by Gly so Asn-350 is not glycosylated. Ref.3 In cv. GT.1, four different forms of the enzyme have been detected with differently processed C-termini. In cv. PR 261 and cv. RRIM 600, only 2 forms are detected, a major form which is processed at residue 352 and a minor form which is processed at residue 354.
Polymorphism	The enzyme from cv. GT.1 displays a 3-5 fold lower specific activity than the enzyme from cv. PR 261.
Sequence similarities	Belongs to the glycosyl hydrolase 17 family.
Biophysicochemical properties	pH dependence: Optimum pH is 4.5-5.0. The enzyme from cv. GT.1 displays a second optimum pH at 6.7.

Ontologies

Keywords
Biological process	Plant defense
Cellular component	Vacuole
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein Pyrrolidone carboxylic acid
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro defense response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glucan endo-1,3-beta-D-glucosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 36	36	Potential
	Chain	37 – 356	320	Glucan endo-1,3-beta-glucosidase minor form 3		PRO_0000011843
	Chain	37 – 355	319	Glucan endo-1,3-beta-glucosidase minor form 2		PRO_0000011844
	Chain	37 – 354	318	Glucan endo-1,3-beta-glucosidase minor form 1		PRO_0000011845
	Chain	37 – 352	316	Glucan endo-1,3-beta-glucosidase major form		PRO_0000011846
	Propeptide	357 – 374	18	Removed in mature form Potential		PRO_0000011847
Sites
	Active site	276	1	Nucleophile By similarity
	Active site	333	1	Proton donor By similarity
Amino acid modifications
	Modified residue	37	1	Pyrrolidone carboxylic acid Probable
	Glycosylation	63	1	N-linked (GlcNAc...)
	Glycosylation	350	1	N-linked (GlcNAc...)
	Glycosylation	364	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	342	1	N → D in strain: cv. PR 261 and cv. RRIM 600. Ref.3
	Natural variant	352	1	S → G in strain: cv. PR 261 and cv. RRIM 600. Ref.3
Experimental info
	Sequence conflict	344 – 345	2	WQ → RP Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P52407 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: 7468888769FE3A9D	FASTA	374	41,396
	10 20 30 40 50 60 MAISSSTSGT SSSFPSRTTV MLLLFFFAAS VGITDAQVGV CYGMQGNNLP PVSEVIALYK 70 80 90 100 110 120 KSNITRMRIY DPNRAVLEAL RGSNIELILG VPNSDLQSLT NPSNAKSWVQ KNVRGFWSSV 130 140 150 160 170 180 LFRYIAVGNE ISPVNRGTAW LAQFVLPAMR NIHDAIRSAG LQDQIKVSTA IDLTLVGNSY 190 200 210 220 230 240 PPSAGAFRDD VRSYLDPIIG FLSSIRSPLL ANIYPYFTYA YNPRDISLPY ALFTSPSVVV 250 260 270 280 290 300 WDGQRGYKNL FDATLDALYS ALERASGGSL EVVVSESGWP SAGAFAATFD NGRTYLSNLI 310 320 330 340 350 360 QHVKGGTPKR PNRAIETYLF AMFDENKKQP EVEKHFGLFF PNKWQKYNLN FSAEKNWDIS 370 TEHNATILFL KSDM

References

[1]	"Beta-1,3-glucanase is highly-expressed in laticifers of Hevea brasiliensis." Chye M.-L., Cheung K.-Y. Plant Mol. Biol. 29:397-402(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: cv. RRIM 600. Tissue: Latex.
[2]	"Chitinase and beta-1,3-glucanase in the lutoid-body fraction of Hevea latex." Subroto T., van Koningsveld G.A., Schreuder H.A., Soedjanaatmadja U.M.S., Beintema J.J. Phytochemistry 43:29-37(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 45-64 AND 323-352. Strain: cv. RRIM 600. Tissue: Latex.
[3]	"Enzymic and structural studies on processed proteins from the vacuolar (lutoid-body) fraction of latex of Hevea brasiliensis." Subroto T., de Vries H., Schuringa J.J., Soedjanaatmadja U.M.S., Hofsteenge J., Jekel P.A., Beintema J.J. Plant Physiol. Biochem. 39:1047-1055(2001) Cited for: PROTEIN SEQUENCE OF 323-356, GLYCOSYLATION, PROTEOLYTIC PROCESSING OF C-TERMINUS, VARIANTS ASP-342 AND GLY-352. Strain: cv. GT.1, cv. PR 261 and cv. RRIM 600.
[4]	"Beta-1,3-glucanase isozymes from the latex of Hevea brasiliensis." Churngchow N., Suntaro A., Wititsuwannnakul R. Phytochemistry 39:505-509(1995) Cited for: SUBUNIT. Strain: cv. RRIM 600.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U22147 mRNA. Translation: AAA87456.1.
PIR	S65077.
3D structure databases
ProteinModelPortal	P52407.
SMR	P52407. Positions 38-351.
ModBase	Search...
Protein family/group databases
Allergome	3313. Hev b 2.0101. 386. Hev b 2.
CAZy	GH17. Glycoside Hydrolase Family 17.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR000490. Glyco_hydro_17. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00332. Glyco_hydro_17. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00587. GLYCOSYL_HYDROL_F17. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

E13B_HEVBR

Accession

Primary (citable) accession number: P52407

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	March 1, 2004
Last modified:	May 1, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program