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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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. DR Genevisible; Q8GY58; AT. 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 //