ID   GUN15_ARATH             Reviewed;         492 AA.
AC   O80497;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Endoglucanase 15;
DE            EC=3.2.1.4;
DE   AltName: Full=Endo-1,4-beta glucanase 15;
DE   Flags: Precursor;
GN   OrderedLocusNames=At2g44570; ORFNames=F16B22.6;
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; AAC27459.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10439.1; -; Genomic_DNA.
DR   PIR; T01584; T01584.
DR   RefSeq; NP_181985.1; NM_130021.3.
DR   AlphaFoldDB; O80497; -.
DR   SMR; O80497; -.
DR   STRING; 3702.O80497; -.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   PaxDb; 3702-AT2G44570-1; -.
DR   ProteomicsDB; 247145; -.
DR   EnsemblPlants; AT2G44570.1; AT2G44570.1; AT2G44570.
DR   GeneID; 819065; -.
DR   Gramene; AT2G44570.1; AT2G44570.1; AT2G44570.
DR   KEGG; ath:AT2G44570; -.
DR   Araport; AT2G44570; -.
DR   TAIR; AT2G44570; GH9B12.
DR   eggNOG; ENOG502QRF6; Eukaryota.
DR   HOGENOM; CLU_008926_1_0_1; -.
DR   InParanoid; O80497; -.
DR   OMA; YVVNATH; -.
DR   OrthoDB; 1347382at2759; -.
DR   PhylomeDB; O80497; -.
DR   BioCyc; ARA:AT2G44570-MONOMER; -.
DR   PRO; PR:O80497; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80497; 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   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF189; ENDOGLUCANASE 15; 1.
DR   Pfam; PF00759; Glyco_hydro_9; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   PROSITE; PS60032; GH9_1; 1.
DR   PROSITE; PS00592; GH9_2; 1.
DR   Genevisible; O80497; AT.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Cellulose degradation; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..492
FT                   /note="Endoglucanase 15"
FT                   /id="PRO_0000249267"
FT   ACT_SITE        86
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT   ACT_SITE        414
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        466
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        475
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
SQ   SEQUENCE   492 AA;  53591 MW;  6FE816C89048D620 CRC64;
     MSCISSQCFI TIKSICIVLL LSITCGAVSA NSNYGEALTK SLLYFEAQRS GKLPLDQRVI
     WRGDSALRDG SDAHVDLTGG YYDAGDNMKF GFPLAFTTTM LAWSSVEMES QLKAHQEHGN
     TLAALRWATD YLIKAHPEPN VLYGQVGDAN LDHACWMRPE DMTTPRPSYR IDPQHPGADL
     AGETAAAMAA ASLAFAPSDS AYAKTLISHA KELFEFAKDY PGVYHNSIPN AGGFYPSSGY
     EDELLWAAAW LHRATGDQTY LDHLTQASNS GGARSVFAWD DKFLGAQVLV AKLVFEGKVK
     NEGKMIEYKS MAEQFICNCA QKGFNNVKKT PGGLLWFLPW DNLQYTATAS FALATYAKYL
     EAAQTSIQCP NGDVLQASDL LNLARAQVDY ILGSNPKKMS YMVGYGTNYP KRPHHRGASI
     VSIKNDPKPV TCNGGFEAWY NNPKPNPNLL VGAIVGGPDE YDAYGDERSD FQHGEPDTVT
     VAPLLGVLAA IA
//