GUN22_ARATH
ID GUN22_ARATH Reviewed; 494 AA.
AC Q9SVJ4; F4JUJ7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Endoglucanase 22;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 22;
DE AltName: Full=Glycosyl hydrolase 9B16;
DE Flags: Precursor;
GN Name=GH9B16; OrderedLocusNames=At4g38990; ORFNames=F19H22.90;
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 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
CC -!- CAUTION: The conserved 'Asp-464' active site is replaced by a Gly
CC residue. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE87005.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035679; CAB38819.1; -; Genomic_DNA.
DR EMBL; AL161594; CAB80562.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87005.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; ANM67304.1; -; Genomic_DNA.
DR PIR; T06059; T06059.
DR RefSeq; NP_001329141.1; NM_001342521.1.
DR RefSeq; NP_195610.3; NM_120059.3.
DR AlphaFoldDB; Q9SVJ4; -.
DR SMR; Q9SVJ4; -.
DR STRING; 3702.AT4G38990.1; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PRIDE; Q9SVJ4; -.
DR ProteomicsDB; 230115; -.
DR EnsemblPlants; AT4G38990.2; AT4G38990.2; AT4G38990.
DR GeneID; 830054; -.
DR Gramene; AT4G38990.2; AT4G38990.2; AT4G38990.
DR KEGG; ath:AT4G38990; -.
DR Araport; AT4G38990; -.
DR eggNOG; ENOG502QV58; Eukaryota.
DR InParanoid; Q9SVJ4; -.
DR OMA; HRGSYTN; -.
DR OrthoDB; 1195424at2759; -.
DR PRO; PR:Q9SVJ4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVJ4; 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 Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Cellulose degradation; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..494
FT /note="Endoglucanase 22"
FT /id="PRO_0000249274"
FT ACT_SITE 76
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 473
FT /evidence="ECO:0000250"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 494 AA; 55019 MW; FF242EA53A8070A4 CRC64;
MKPLVCSFIV ILLILLPTTI SHDYSDALTK SILFFEGQRS GYLPREQRMT WRHNSALNDG
KNLNVDLVGG YYDAGDNIKF HFPMAFTTTM LAWSAIDFGS YMSPADLRDN LVALRWGSNY
LLKTVSQLPN RIFVQVGEPT PDHQCWERPE DMDTPRTAYA LEAPKPASDL AGEIAAALAA
ASIAFKRFDP RYSKLLLDNA LRTFEYADSH RGSYTNNPET KLAVCPFYCS VNGYEDELLW
GAAWLRRATG KDSYIKYLVE NRQSFGSDSN YFEFGWDNKV GGVNVLVAKE VFEKNVAAIA
PYKDTAEKLM CSFFLETPGA HMSYSPGGLL YKPGSSQLQN TVALSFLLLT YANYLSKSSQ
QPLQILSTTP LWYLTQRIAN IVGFEKVDYI LGDNPMKMSY MIGYGNRYPR QIHHRGASSP
SITTHPTPVK CSEGWNSFSS PNPDPNVLVG AVIGGPNIDD KFVGGRTNAS ETEPTTYINA
PFVGLLAYFK ANPV
