GUN18_ORYSJ
ID GUN18_ORYSJ Reviewed; 518 AA.
AC Q5Z9P8; A0A0P0X0U4; Q0D9H6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Endoglucanase 18;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 18;
GN OrderedLocusNames=Os06g0715300, LOC_Os06g50140; ORFNames=P0481E08.13;
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 [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 [2]
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 [3]
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 [4]
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).
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; Single-pass type II membrane protein.
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; AP003614; BAD53575.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF20497.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS99495.1; -; Genomic_DNA.
DR EMBL; AK121369; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015642677.1; XM_015787191.1.
DR AlphaFoldDB; Q5Z9P8; -.
DR SMR; Q5Z9P8; -.
DR STRING; 4530.OS06T0715300-01; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; Q5Z9P8; -.
DR PRIDE; Q5Z9P8; -.
DR EnsemblPlants; Os06t0715300-01; Os06t0715300-01; Os06g0715300.
DR GeneID; 4342070; -.
DR Gramene; Os06t0715300-01; Os06t0715300-01; Os06g0715300.
DR KEGG; osa:4342070; -.
DR eggNOG; ENOG502QRF6; Eukaryota.
DR HOGENOM; CLU_008926_1_4_1; -.
DR InParanoid; Q5Z9P8; -.
DR OMA; GHKWLET; -.
DR OrthoDB; 1195424at2759; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5Z9P8; 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; 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.
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..518
FT /note="Endoglucanase 18"
FT /id="PRO_0000249295"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 436
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 491
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 450
FT /note="C -> Y (in Ref. 4; AK121369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 56741 MW; F6DA8EC0D7951B8C CRC64;
MANCVRCCCW LLVLMLMALA ITAAVVFVRY KNGEGVFPFP GVPGAVDHKY ADALAVALQF
FQVQKSGKLV NNTIHWRGDS ALDDGKEAGI DLSKGMYDAG DHMKFGFPMA FTATMLSWSV
LEYGDAMRAA DQRDSAIDAL NWIMDYLVNA HPSDDVLYIQ VGDPKADHKC WERPEKMKEK
RPLTKITPKS PGSDVAAETA AAMAAASLVY KTINKTYSSS LLDHGERLFA FADKHRGSYT
RTFPELSAFY NSTTYQDELL WAASWLYHAT GNHSYLAYAT GKNKDFADLG NPRYFSWDDK
RAGTEVLLSR VSFFASQGSD VAQDDVLGMY KQTADAVMCI LLPDSETAAF RTEGGLLYVA
EWNSLQHPVA SAFLAAVYSD YMQSSGKTEL SCSGQGFSPA DLRKFAKSQA DYLLGSNPMK
ISYLVGYGDR YPEKVHHRGA SIPEDVDTGC DGHKWLETSK PNPNVATGAL VGGPYKNDSF
VDERDNVMQN EATTYNSALV AGLLSALVST SSLARSLS
