GUN13_ARATH
ID GUN13_ARATH Reviewed; 490 AA.
AC O64890;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Endoglucanase 13;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 13;
DE Flags: Precursor;
GN OrderedLocusNames=At2g44550; ORFNames=F4I1.55;
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; AAC27457.1; -; Genomic_DNA.
DR EMBL; AC004521; AAM14964.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10437.1; -; Genomic_DNA.
DR PIR; T02411; T02411.
DR RefSeq; NP_181983.1; NM_130019.1.
DR AlphaFoldDB; O64890; -.
DR SMR; O64890; -.
DR STRING; 3702.AT2G44550.1; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; O64890; -.
DR PRIDE; O64890; -.
DR ProteomicsDB; 247265; -.
DR EnsemblPlants; AT2G44550.1; AT2G44550.1; AT2G44550.
DR GeneID; 819063; -.
DR Gramene; AT2G44550.1; AT2G44550.1; AT2G44550.
DR KEGG; ath:AT2G44550; -.
DR Araport; AT2G44550; -.
DR TAIR; locus:2042441; AT2G44550.
DR eggNOG; ENOG502QRF6; Eukaryota.
DR HOGENOM; CLU_008926_1_4_1; -.
DR InParanoid; O64890; -.
DR OMA; SHDYVEV; -.
DR OrthoDB; 1195424at2759; -.
DR PhylomeDB; O64890; -.
DR BioCyc; ARA:AT2G44550-MON; -.
DR PRO; PR:O64890; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64890; baseline and differential.
DR Genevisible; O64890; 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 Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Cellulose degradation; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..490
FT /note="Endoglucanase 13"
FT /id="PRO_0000249265"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 490 AA; 53448 MW; 70A6A9155FAFFC08 CRC64;
MSQLKNGSSQ CLWTSICIVL IVMSMAREAV STNYAEALKN SLLYFEAQRS GKLPPNQRVT
WRGDSALRDG SDAHIDLTGG YYDAGDNMKF GFPLAFTTTM LAWSNIEMAS QLRAHHEKGN
ALRALKWATD YLIKAHPQPN VLYGQVGEGN SDHKCWMRPE DMTTPRTSYR IDAQHPGSDL
AGETAAAMAA ASIAFAPSDK AYANILIGHA KDLFAFAKAH RGLYQNSIPN AGGFYASSGY
EDELLWAAAW LHRATNDQIY LDYLTEAETG GPRTVFAWDD KFVGAQVLVA KLALEGKVES
SEQIVEYKSM AEQFICNCAQ KGDNNVKKTP GGLLYFLPWN NLQYTTAATF VLSAYSKYLE
AAKASIDCPD GALQASDLLQ VARSQVDYIL GSNPQKMSYM VGVGTNYPKK PHHRAASIVS
IRQDKTPVTC SGGYDKWYNN PAPNPNVLAG AVVGGPDDND VYGDERSNFQ QAEPATVTTA
PLVGVLALVF
