ID GUN2_ORYSJ Reviewed; 640 AA.
AC Q5NAT0; A0A0P0V072; A0P889; Q0JPJ1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Endoglucanase 2;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 2;
DE AltName: Full=OsCel9A;
DE AltName: Full=OsGLU5;
DE Flags: Precursor;
GN Name=GLU5; OrderedLocusNames=Os01g0220100, LOC_Os01g12070;
GN ORFNames=OsJ_000889, P0483F08.13, P0489G09.28;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-64; 48-167; 219-274 AND
RP 295-335, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Sasanishiki; TISSUE=Root;
RX PubMed=17056618; DOI=10.1093/pcp/pcl020;
RA Yoshida K., Komae K.;
RT "A rice family 9 glycoside hydrolase isozyme with broad substrate
RT specificity for hemicelluloses in type II cell walls.";
RL Plant Cell Physiol. 47:1541-1554(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Sasanishiki; TISSUE=Root;
RX PubMed=17056619; DOI=10.1093/pcp/pcl021;
RA Yoshida K., Imaizumi N., Kaneko S., Kawagoe Y., Tagiri A., Tanaka H.,
RA Nishitani K., Komae K.;
RT "Carbohydrate-binding module of a rice endo-beta-1,4-glycanase, OsCel9A,
RT expressed in auxin-induced lateral root primordia, is post-translationally
RT truncated.";
RL Plant Cell Physiol. 47:1555-1571(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=16463105; DOI=10.1007/s11103-005-2972-x;
RA Zhou H.-L., He S.-J., Cao Y.-R., Chen T., Du B.-X., Chu C.-C., Zhang J.-S.,
RA Chen S.-Y.;
RT "OsGLU1, a putative membrane-bound endo-1,4-beta-D-glucanase from rice,
RT affects plant internode elongation.";
RL Plant Mol. Biol. 60:137-151(2006).
CC -!- FUNCTION: Hydrolyzes 1,4-beta-glycosyl linkages of 1,4-beta-glucans and
CC 1,3-1,4-beta-glucans. Possesses broad substrate specificity for
CC hemicelluloses of type II cell walls. Substrate preference is
CC carboxymethyl-cellulose > 1,3-1,4-beta-glucan > lichenan > arabinoxylan
CC > phospho-swollen cellulose > xylan > glucomannan. May participate in
CC lateral root development. {ECO:0000269|PubMed:17056618,
CC ECO:0000269|PubMed:17056619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.3-5.6 with 1,3-1,4-beta-glucan as substrate (at 35
CC degrees Celsius). {ECO:0000269|PubMed:17056618};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {ECO:0000269|PubMed:16463105}.
CC -!- DEVELOPMENTAL STAGE: Expressed in lateral root primordia during auxin-
CC induced lateral root development. {ECO:0000269|PubMed:17056619}.
CC -!- INDUCTION: By auxin in roots (at protein level).
CC {ECO:0000269|PubMed:17056618}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
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DR EMBL; AB038510; BAF37260.1; -; mRNA.
DR EMBL; AP002094; BAD81360.1; -; Genomic_DNA.
DR EMBL; AP002745; BAD81426.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04337.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS71064.1; -; Genomic_DNA.
DR EMBL; CM000138; EAZ11064.1; -; Genomic_DNA.
DR EMBL; AK103304; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015621149.1; XM_015765663.1.
DR AlphaFoldDB; Q5NAT0; -.
DR SMR; Q5NAT0; -.
DR STRING; 39947.Q5NAT0; -.
DR CAZy; CBM49; Carbohydrate-Binding Module Family 49.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR GlyCosmos; Q5NAT0; 1 site, No reported glycans.
DR PaxDb; 39947-Q5NAT0; -.
DR EnsemblPlants; Os01t0220100-01; Os01t0220100-01; Os01g0220100.
DR GeneID; 4324643; -.
DR Gramene; Os01t0220100-01; Os01t0220100-01; Os01g0220100.
DR KEGG; osa:4324643; -.
DR eggNOG; ENOG502QRF6; Eukaryota.
DR HOGENOM; CLU_008926_1_4_1; -.
DR InParanoid; Q5NAT0; -.
DR OMA; WLYQASD; -.
DR OrthoDB; 1347382at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q5NAT0; OS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR019028; CBM_49.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF190; ENDOGLUCANASE 2; 1.
DR Pfam; PF09478; CBM49; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM01063; CBM49; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Cellulose degradation; Direct protein sequencing; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:17056618"
FT CHAIN 35..511
FT /note="Endoglucanase 2"
FT /id="PRO_0000249279"
FT PROPEP 512..640
FT /note="Removed in mature form"
FT /id="PRO_0000372490"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 428
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 616
FT /note="G -> S (in Ref. 8; AK103304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 68408 MW; D68E16BB1B3A35CA CRC64;
MARGGGAAGV SMAHHLGIAL VVLVFAAMAQ VARGGGGGHD YGMALSKSIL YFEAQRSGVL
PGSQRIAWRA NSGLADGKAN GVDLVGGYYD AGDNVKFGLP MAFTVTMMAW SVIEYGEEMA
AAGELGHAVE AIKWGTDYFA KAHPEPNVLY AEVGDGDSDH NCWQRPEDMT TSRQAYRLDP
QNPGSDLAGE TAAAMAAASL VFRSSNPGYA DQLLQHSKQL FDFADKYRGR YDNSITVARN
YYGSFSGYGD ELLWASAWLY QASDDRRYLD YLANNADALG GTGWSINQFG WDVKYPGVQI
LAAKFLLQGK AGEHAGVLQG YRRKADFFAC SCLGKDAADN VGRTPGGMLY HQRWNNIQFV
TSASFLLAVY SDHLAGGAVR CSGGGGAVAG AAELLAFAKS QVDYILGSNP RGTSYMVGYG
AVYPRQAHHR GSSIASIRAS PSFVSCREGY ASWYGRRGGN PNLLDGAVVG GPDEHDDFAD
ERNNYEQTEA ATYNNAPLMG ILARLAAGHG ARARGRLGQS LQHGIAANHT SLPHGANHQH
ASPVEIEQKA TASWEKDGRT YHRYAVTVSN RSPAGGKTVE ELHIGIGKLY GPVWGLEKAA
RYGYVLPSWT PSLPAGESAA FVYVHAAPPA DVWVTGYKLV
//
