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   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.
DR   Genevisible; Q5NAT0; OS.
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
//