Q5NAT0 (GUN2_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoglucanase 2
EC=3.2.1.4

Alternative name(s):
Endo-1,4-beta glucanase 2
OsCel9A
OsGLU5

Gene names

Name:	GLU5
Ordered Locus Names:	Os01g0220100, LOC_Os01g12070
ORF Names:	OsJ_000889, P0483F08.13, P0489G09.28

Organism

Oryza sativa subsp. japonica (Rice) [Reference proteome]

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza › Oryza sativa

Protein attributes

Sequence length	640 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	Hydrolyzes 1,4-beta-glycosyl linkages of 1,4-beta-glucans and 1,3-1,4-beta-glucans. Possesses broad substrate specificity for hemicelluloses of type II cell walls. Substrate preference is carboxymethyl-cellulose > 1,3-1,4-beta-glucan > lichenan > arabinoxylan > phospho-swollen cellulose > xylan > glucomannan. May participate in lateral root development. Ref.1 Ref.2
Catalytic activity	Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Subcellular location	Secreted By similarity.
Tissue specificity	Expressed in roots and flowers. Ref.8
Developmental stage	Expressed in lateral root primordia during auxin-induced lateral root development. Ref.2
Induction	By auxin in roots (at protein level). Ref.1
Sequence similarities	Belongs to the glycosyl hydrolase 9 (cellulase E) family.
Biophysicochemical properties	pH dependence: Optimum pH is 5.3-5.6 with 1,3-1,4-beta-glucan as substrate (at 35 degrees Celsius). Ref.1

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell wall biogenesis/degradation Cellulose degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cellulase 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 – 34	34	Ref.1
	Chain	35 – 511	477	Endoglucanase 2		PRO_0000249279
	Propeptide	512 – 640	129	Removed in mature form		PRO_0000372490
Sites
	Active site	428	1	By similarity
	Active site	480	1	By similarity
	Active site	489	1	By similarity
Amino acid modifications
	Glycosylation	528	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	616	1	G → S in AK103304. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q5NAT0 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: D68E16BB1B3A35CA	FASTA	640	68,408
	10 20 30 40 50 60 MARGGGAAGV SMAHHLGIAL VVLVFAAMAQ VARGGGGGHD YGMALSKSIL YFEAQRSGVL 70 80 90 100 110 120 PGSQRIAWRA NSGLADGKAN GVDLVGGYYD AGDNVKFGLP MAFTVTMMAW SVIEYGEEMA 130 140 150 160 170 180 AAGELGHAVE AIKWGTDYFA KAHPEPNVLY AEVGDGDSDH NCWQRPEDMT TSRQAYRLDP 190 200 210 220 230 240 QNPGSDLAGE TAAAMAAASL VFRSSNPGYA DQLLQHSKQL FDFADKYRGR YDNSITVARN 250 260 270 280 290 300 YYGSFSGYGD ELLWASAWLY QASDDRRYLD YLANNADALG GTGWSINQFG WDVKYPGVQI 310 320 330 340 350 360 LAAKFLLQGK AGEHAGVLQG YRRKADFFAC SCLGKDAADN VGRTPGGMLY HQRWNNIQFV 370 380 390 400 410 420 TSASFLLAVY SDHLAGGAVR CSGGGGAVAG AAELLAFAKS QVDYILGSNP RGTSYMVGYG 430 440 450 460 470 480 AVYPRQAHHR GSSIASIRAS PSFVSCREGY ASWYGRRGGN PNLLDGAVVG GPDEHDDFAD 490 500 510 520 530 540 ERNNYEQTEA ATYNNAPLMG ILARLAAGHG ARARGRLGQS LQHGIAANHT SLPHGANHQH 550 560 570 580 590 600 ASPVEIEQKA TASWEKDGRT YHRYAVTVSN RSPAGGKTVE ELHIGIGKLY GPVWGLEKAA 610 620 630 640 RYGYVLPSWT PSLPAGESAA FVYVHAAPPA DVWVTGYKLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A rice family 9 glycoside hydrolase isozyme with broad substrate specificity for hemicelluloses in type II cell walls." Yoshida K., Komae K. Plant Cell Physiol. 47:1541-1554(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-64; 48-167; 219-274 AND 295-335, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, MASS SPECTROMETRY. Strain: cv. Sasanishiki. Tissue: Root.
[2]	"Carbohydrate-binding module of a rice endo-beta-1,4-glycanase, OsCel9A, expressed in auxin-induced lateral root primordia, is post-translationally truncated." Yoshida K., Imaizumi N., Kaneko S., Kawagoe Y., Tagiri A., Tanaka H., Nishitani K., Komae K. Plant Cell Physiol. 47:1555-1571(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE. Strain: cv. Sasanishiki. Tissue: Root.
[3]	"The genome sequence and structure of rice chromosome 1." Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M. , Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S., Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H., Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S., Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y., Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T. Nature 420:312-316(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[4]	"The map-based sequence of the rice genome." International rice genome sequencing project (IRGSP) Nature 436:793-800(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[5]	"The rice annotation project database (RAP-DB): 2008 update." The rice annotation project (RAP) Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: cv. Nipponbare.
[6]	"The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H. PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[7]	"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice." The rice full-length cDNA consortium Science 301:376-379(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Nipponbare.
[8]	"OsGLU1, a putative membrane-bound endo-1,4-beta-D-glucanase from rice, affects plant internode elongation." Zhou H.-L., He S.-J., Cao Y.-R., Chen T., Du B.-X., Chu C.-C., Zhang J.-S., Chen S.-Y. Plant Mol. Biol. 60:137-151(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB038510 mRNA. Translation: BAF37260.1. AP002094 Genomic DNA. Translation: BAD81360.1. AP002745 Genomic DNA. Translation: BAD81426.1. AP008207 Genomic DNA. Translation: BAF04337.1. CM000138 Genomic DNA. Translation: EAZ11064.1. AK103304 mRNA. No translation available.
RefSeq	NP_001042423.1. NM_001048958.1.
UniGene	Os.32667.
3D structure databases
HSSP	HSSP built from PDB template 1TF4 based on UniProtKB P26221.
ProteinModelPortal	Q5NAT0.
ModBase	Search...
Protein family/group databases
CAZy	CBM49. Carbohydrate-Binding Module Family 49. GH9. Glycoside Hydrolase Family 9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	LOC_Os01g12070.1; LOC_Os01g12070.1; LOC_Os01g12070.
GeneID	4324643.
KEGG	dosa:Os01t0220100-01. dosa:Os05t0212300-01. osa:4324643.
Organism-specific databases
Gramene	Q5NAT0.
Phylogenomic databases
eggNOG	NOG05134.
HOGENOM	HOG000021033.
ProtClustDB	PLN02171.
Gene expression databases
ArrayExpress	Q5NAT0.
Family and domain databases
Gene3D	1.50.10.10. 1 hit.
InterPro	IPR008928. 6-hairpin_glycosidase-like. IPR012341. 6hp_glycosidase. IPR019028. CBM_49. IPR001701. Glyco_hydro_9. IPR018221. Glyco_hydro_9_AS. [Graphical view]
Pfam	PF09478. CBM49. 1 hit. PF00759. Glyco_hydro_9. 1 hit. [Graphical view]
SMART	SM01063. CBM49. 1 hit. [Graphical view]
SUPFAM	SSF48208. Glyco_trans_6hp. 1 hit.
PROSITE	PS00592. GLYCOSYL_HYDROL_F9_1. False negative. PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GUN2_ORYSJ

Accession

Primary (citable) accession number: Q5NAT0
Secondary accession number(s): A0P889, Q0JPJ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	February 1, 2005
Last modified:	April 3, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program