GUN21_ARATH
ID GUN21_ARATH Reviewed; 620 AA.
AC Q9STW8;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Endoglucanase 21;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 21;
GN Name=KOR3; OrderedLocusNames=At4g24260; ORFNames=T22A6.90;
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 TISSUE SPECIFICITY.
RX PubMed=11488474; DOI=10.1023/a:1010688726755;
RA Moelhoej M., Joergensen B., Ulvskov P., Borkhardt B.;
RT "Two Arabidopsis thaliana genes, KOR2 and KOR3, which encode membrane-
RT anchored endo-1,4-beta-D-glucanases, are differentially expressed in
RT developing leaf trichomes and their support cells.";
RL Plant Mol. Biol. 46:263-275(2001).
RN [4]
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: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in conductive tissues of young roots,
CC cotyledons, rosette leaves, cauline leaves and sepals. Expressed in the
CC leaf trichome support cells. {ECO:0000269|PubMed:11488474}.
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; AL078637; CAB45061.1; -; Genomic_DNA.
DR EMBL; AL161561; CAB79336.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84879.1; -; Genomic_DNA.
DR PIR; T09889; T09889.
DR RefSeq; NP_194157.1; NM_118559.2.
DR AlphaFoldDB; Q9STW8; -.
DR SMR; Q9STW8; -.
DR STRING; 3702.AT4G24260.1; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; Q9STW8; -.
DR PRIDE; Q9STW8; -.
DR ProteomicsDB; 247271; -.
DR EnsemblPlants; AT4G24260.1; AT4G24260.1; AT4G24260.
DR GeneID; 828527; -.
DR Gramene; AT4G24260.1; AT4G24260.1; AT4G24260.
DR KEGG; ath:AT4G24260; -.
DR Araport; AT4G24260; -.
DR TAIR; locus:2135997; AT4G24260.
DR eggNOG; ENOG502QUUK; Eukaryota.
DR HOGENOM; CLU_008926_1_3_1; -.
DR InParanoid; Q9STW8; -.
DR OMA; RYGCKGG; -.
DR OrthoDB; 1195424at2759; -.
DR PhylomeDB; Q9STW8; -.
DR BioCyc; ARA:AT4G24260-MON; -.
DR PRO; PR:Q9STW8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9STW8; baseline and differential.
DR Genevisible; Q9STW8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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 GO; GO:0009624; P:response to nematode; IEP:TAIR.
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; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
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.
DR PROSITE; PS00698; GH9_3; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cell membrane; 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..620
FT /note="Endoglucanase 21"
FT /id="PRO_0000249273"
FT TOPO_DOM 1..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..620
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 514
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 570
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 620 AA; 69585 MW; 7BCF07C806B0BBD0 CRC64;
MYGRDPWGGP LEINAADSMT DDDRSRNLQD LDRATPSRPL DETQQSWLLG PKVLKKKKYV
DLGCILVSRK IFLWTLGTIV VTALLSGFIT LIVKTLPHHH HKEPPPDNYT IALRTALKFF
NAQQSGKLPK NIYNVSWRHD SCLQDGKGDP GQCYKDLVGG YYDAGDSIKF NFPMSYAMTM
LSWSVIEYSA KYQAAGELEH VKELIKWGTD YFLKTFNSSA DNIYVMVEQV GSGVSGRGSE
LHNDHYCWMR PEDIHYKRTV SQCYSSCSDL AAEMAAALAS ASIVFKDNRL YSKNLVHGAK
TLYRFATTSR NRYSQNGKES SKFYNSSMFE DELLWGGAWL YYATGNVTYL ERVTSHHMAE
KAGAFGNSPY YGVFSWDNKL PGAQLLLTRM RLFLSPGYPY EDMLSEFHNQ TGRVMCSYLP
YYKKFNRTNG GLIQLNHGAP QPLQYVANAA FLAALFSDYL EAADTPGWYC GPNFYTTEFL
RNFSRSQIDY ILGKNPRKMS YVVGYGQRYP KQVHHRGASI PKNMKETCTG GFKWKKSKKN
NPNAINGAMV AGPDKHDGFH DIRTNYNYTE PTLAGNAGLV AALVALSGEK AVGGIDKNTM
FSAVPPLVMA TPPPPAPWTP
