GUN12_ARATH
ID GUN12_ARATH Reviewed; 491 AA.
AC O64889;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Endoglucanase 12;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 12;
DE Flags: Precursor;
GN OrderedLocusNames=At2g44540; ORFNames=F4I1.52;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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}.
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DR EMBL; AC003672; AAC27456.1; -; Genomic_DNA.
DR EMBL; AC004521; AAM14965.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10436.1; -; Genomic_DNA.
DR PIR; T02410; T02410.
DR RefSeq; NP_181982.1; NM_130018.2.
DR AlphaFoldDB; O64889; -.
DR SMR; O64889; -.
DR IntAct; O64889; 1.
DR STRING; 3702.AT2G44540.1; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR iPTMnet; O64889; -.
DR PaxDb; O64889; -.
DR PRIDE; O64889; -.
DR ProteomicsDB; 247314; -.
DR EnsemblPlants; AT2G44540.1; AT2G44540.1; AT2G44540.
DR GeneID; 819062; -.
DR Gramene; AT2G44540.1; AT2G44540.1; AT2G44540.
DR KEGG; ath:AT2G44540; -.
DR Araport; AT2G44540; -.
DR TAIR; locus:2042376; AT2G44540.
DR eggNOG; ENOG502QRF6; Eukaryota.
DR HOGENOM; CLU_008926_1_4_1; -.
DR InParanoid; O64889; -.
DR OMA; WYNTHEP; -.
DR OrthoDB; 1195424at2759; -.
DR PhylomeDB; O64889; -.
DR BioCyc; ARA:AT2G44540-MON; -.
DR PRO; PR:O64889; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64889; baseline and differential.
DR Genevisible; O64889; 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 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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..491
FT /note="Endoglucanase 12"
FT /id="PRO_0000249264"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 491 AA; 53421 MW; E8C02220EA89635B CRC64;
MSQSKNGSSQ CLWTSICIVV LVMSMARGAV STNYAEALQK SLLYFEAQRS GKLPPNQKVT
WRGDSALKDG SDAHIDLTGG YYDAGDNMKF GFPLAFTTTM LAWSNIEMGS ELRAHHEQGN
SLRALKWATD YLIKAHPQPN VLYGQVGEGN SDHKCWMRPE DMTTPRTSYR IDAQHPGSDL
AGETAAAMAA ASIAFAPFDK AYANILIGHA KDLFAFAKAH PGLYQNSITN AGGFYASSGY
EDELLWAAAW LHRATNDQIY LNYLTQASGT GGPRSVFAWD DKFVGAQVLM AKLALERKVG
SNGKIAEYKS MAEQFICNCA QKGSNNVKKT PGGLLYFLPW NNLQYTTTAS FVLSAYSKYL
TKAKASIQCP KGALQASDLL QIARSQVDYI LGSNPQKMSY MVGVGTNYPK KPHHRAASIV
SIRKDKTPVT CSGGYDKWYN NPAPNPNVLM GALVGGPNEN DVYGDERSNF QQAEPATVTV
APFVGVLAAV F
