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GUN23_ARATH
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   03-AUG-2022, entry version 114.
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.AT4G39000.1; -.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   PaxDb; Q8GY58; -.
DR   PRIDE; Q8GY58; -.
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; locus:2120232; AT4G39000.
DR   eggNOG; ENOG502QV58; Eukaryota.
DR   HOGENOM; CLU_008926_1_2_1; -.
DR   InParanoid; Q8GY58; -.
DR   OMA; ETNGPHM; -.
DR   OrthoDB; 1195424at2759; -.
DR   PhylomeDB; Q8GY58; -.
DR   BioCyc; ARA:AT4G39000-MON; -.
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   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   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
 
 
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