GUN9_ORYSJ
ID GUN9_ORYSJ Reviewed; 619 AA.
AC P0C1U4; A0A0P0VX27; A0P890; Q10LZ4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Endoglucanase 9;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 9;
DE AltName: Full=OsCel9D;
DE AltName: Full=OsGLU1;
GN Name=GLU1; OrderedLocusNames=Os03g0329500, LOC_Os03g21210;
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], AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
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: Involved in cell wall assembly during cell elongation.
CC {ECO:0000269|PubMed:16463105}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16463105,
CC ECO:0000269|PubMed:17056619}.
CC -!- INDUCTION: By gibberellin (GA3) and brassinosteroid.
CC {ECO:0000269|PubMed:16463105}.
CC -!- DISRUPTION PHENOTYPE: Plants are dwarf with reduction in cell
CC elongation and decrease in cellulose content.
CC {ECO:0000269|PubMed:16463105}.
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; AB040817; BAF37261.1; -; mRNA.
DR EMBL; DP000009; ABF95745.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11918.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS84019.1; -; Genomic_DNA.
DR EMBL; AK102748; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015627869.1; XM_015772383.1.
DR AlphaFoldDB; P0C1U4; -.
DR SMR; P0C1U4; -.
DR STRING; 4530.OS03T0329500-01; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; P0C1U4; -.
DR PRIDE; P0C1U4; -.
DR EnsemblPlants; Os03t0329500-01; Os03t0329500-01; Os03g0329500.
DR GeneID; 4332724; -.
DR Gramene; Os03t0329500-01; Os03t0329500-01; Os03g0329500.
DR KEGG; osa:4332724; -.
DR eggNOG; ENOG502QUUK; Eukaryota.
DR HOGENOM; CLU_008926_1_3_1; -.
DR InParanoid; P0C1U4; -.
DR OMA; EFVWGSS; -.
DR OrthoDB; 1195424at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; P0C1U4; OS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Cellulose degradation; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Polysaccharide degradation; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..619
FT /note="Endoglucanase 9"
FT /id="PRO_0000249286"
FT TOPO_DOM 1..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..619
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 167
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 57
FT /note="R -> Q (in Ref. 6; AK102748)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 68369 MW; 7F3CCB374071162A CRC64;
MSMYGRDPWG GPLEICHDSA TDDDRSRNLD LDRGALSRTL DETQQSWLLA GPGDQGRKKK
KYVDLGCLVV SRKLFVWTVG VLLAAAVFAG LVAGIAKAIP RHHRPPPPPD DFTVALRKAL
MFFNAQKSGK LPKNNNVHWR GNSCMKDGLS DPAVGRSLVG GYYDAGDAVK FNFPAAFSMT
LLSWSVIEYS AKYEAVGELG HIRDTIKWGA DYFLKTFNST ADTIDRVVMQ VGSGATSPGS
TQPNDHYCWM RPEDIDYPRP VVECHACSDL AAEMAASLAA ASIVFKDNKA YSQKLVHGAT
TLFKFARQNR GRYSAGGSDA AKFYNSTSYW DEFVWGGSWM YLATGNSSYL QLATHPKLAK
HAGAYWGGPD YGVFSWDNKL TGAQVLLSRL RLFLSPGYPY EEILRTFHNQ TSIIMCSYLP
IFKSFNRTKG GLIQLNHGRP QPLQYVVNAA FLASLYGDYL EAADTPGWYC GPHFYPIETL
RNFARTQIEY ILGKNPLKMS YVVGYGNRYP KRVHHRGASI PKNGVHYGCK GGWKWRETKK
PNPNIIVGAM VAGPDRHDGF KDVRKNYNYT EATLAGNAGL VAALVALSGE GHGVDKNTMF
SAVPPMFPSP PPPPAPWKP
