ID GUN23_ARATH Reviewed; 493 AA.
AC Q8GY58; Q9SVJ3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 24-JAN-2024, entry version 121.
DE RecName: Full=Endoglucanase 23;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 23;
DE Flags: Precursor;
GN OrderedLocusNames=At4g39000; ORFNames=F19H22.100;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP GENE FAMILY.
RX PubMed=15170254; DOI=10.1007/s00239-003-2571-x;
RA Libertini E., Li Y., McQueen-Mason S.J.;
RT "Phylogenetic analysis of the plant endo-beta-1,4-glucanase gene family.";
RL J. Mol. Evol. 58:506-515(2004).
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: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GY58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GY58-2; Sequence=VSP_020387, VSP_020388;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
CC -!- CAUTION: The conserved 'Asp-461' active site is replaced by a Gly
CC residue. {ECO:0000305}.
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DR EMBL; AL035679; CAB38820.1; -; Genomic_DNA.
DR EMBL; AL161594; CAB80563.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87006.1; -; Genomic_DNA.
DR EMBL; AK117850; BAC42491.1; -; mRNA.
DR EMBL; DQ446906; ABE66120.1; -; mRNA.
DR PIR; T06060; T06060.
DR RefSeq; NP_195611.1; NM_120060.2. [Q8GY58-1]
DR AlphaFoldDB; Q8GY58; -.
DR SMR; Q8GY58; -.
DR STRING; 3702.Q8GY58; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; 3702-AT4G39000-1; -.
DR ProteomicsDB; 247317; -. [Q8GY58-1]
DR EnsemblPlants; AT4G39000.1; AT4G39000.1; AT4G39000. [Q8GY58-1]
DR GeneID; 830055; -.
DR Gramene; AT4G39000.1; AT4G39000.1; AT4G39000. [Q8GY58-1]
DR KEGG; ath:AT4G39000; -.
DR Araport; AT4G39000; -.
DR TAIR; AT4G39000; GH9B17.
DR eggNOG; ENOG502QV58; Eukaryota.
DR HOGENOM; CLU_008926_1_2_1; -.
DR InParanoid; Q8GY58; -.
DR OMA; NCGNLKF; -.
DR OrthoDB; 649923at2759; -.
DR PhylomeDB; Q8GY58; -.
DR BioCyc; ARA:AT4G39000-MONOMER; -.
DR PRO; PR:Q8GY58; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8GY58; baseline and differential.
DR Genevisible; Q8GY58; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF118; ENDOGLUCANASE 23; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Carbohydrate metabolism;
KW Cell wall biogenesis/degradation; Cellulose degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..493
FT /note="Endoglucanase 23"
FT /id="PRO_0000249275"
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 470
FT /evidence="ECO:0000250"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 292..310
FT /note="EVLQNNVTAIAAYKDTAEK -> VWSNFQNQTDVYIYDKCDR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_020387"
FT VAR_SEQ 311..493
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11910074"
FT /id="VSP_020388"
FT CONFLICT 97
FT /note="Missing (in Ref. 3; BAC42491)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="S -> T (in Ref. 3; BAC42491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 493 AA; 54692 MW; B999CEC76F5FDFC3 CRC64;
MKASIYLVTV FILLLLLLPT AIPHDYSDAL RKSILFFEGQ RSGRLPKQQR MAWRRNSALN
DGKNLKTDLV GGYYDAGDNV KFHFPMAFTA TMLAWSSVDF GRYMSQHDFR HNLVAVKWAT
DYLLKTVSQL PNRIFVHVGE VQPDHDCWER PEDMDTPRTA FALDAPYPAS DLAGEIAAAL
AAASIAFKQA NPKYSAILLN KAVQTFQYAD SHRGSYTDNP GIKQAVCPFY CSVNGYKDEL
LWGAAWLRRA TGEDSYLRYL VDNGQAFGES SNYFEFGWDN KVGGVNVLVA KEVLQNNVTA
IAAYKDTAEK MMCSFLPETN GPHMSYTPGG LIYKPGSTQL QNTAALSFLL LTYADYLSTS
SQQLNCGNLK FQPDSLRRIV KRQVDYVLGD NPMKLSYMIG YGERYPGLIH HRGSSIPSVT
VHPAAFGCIA GWNIFSSPNP NPNILIGAVI GGPDVDDRFI GGRTNASETE PTTYINAPFV
GVFAYFKSNP NFS
//
