GUN2_ARATH
ID GUN2_ARATH Reviewed; 515 AA.
AC Q9FXI9; Q9LNS3;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Endoglucanase 2;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 2;
DE Flags: Precursor;
GN OrderedLocusNames=At1g19940; ORFNames=F6F9.1, T20H2.27;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007797; AAG12562.1; -; Genomic_DNA.
DR EMBL; AC022472; AAF79918.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29915.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59313.1; -; Genomic_DNA.
DR EMBL; AY048245; AAK82507.1; -; mRNA.
DR EMBL; AY113063; AAM47371.1; -; mRNA.
DR PIR; G86332; G86332.
DR RefSeq; NP_001321680.1; NM_001332419.1.
DR RefSeq; NP_173423.1; NM_101849.2.
DR AlphaFoldDB; Q9FXI9; -.
DR SMR; Q9FXI9; -.
DR STRING; 3702.AT1G19940.1; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; Q9FXI9; -.
DR PRIDE; Q9FXI9; -.
DR ProteomicsDB; 247274; -.
DR EnsemblPlants; AT1G19940.1; AT1G19940.1; AT1G19940.
DR EnsemblPlants; AT1G19940.2; AT1G19940.2; AT1G19940.
DR GeneID; 838583; -.
DR Gramene; AT1G19940.1; AT1G19940.1; AT1G19940.
DR Gramene; AT1G19940.2; AT1G19940.2; AT1G19940.
DR KEGG; ath:AT1G19940; -.
DR Araport; AT1G19940; -.
DR TAIR; locus:2035384; AT1G19940.
DR eggNOG; ENOG502QQZQ; Eukaryota.
DR HOGENOM; CLU_008926_1_4_1; -.
DR InParanoid; Q9FXI9; -.
DR OMA; YLINCHP; -.
DR OrthoDB; 1195424at2759; -.
DR PhylomeDB; Q9FXI9; -.
DR BioCyc; ARA:AT1G19940-MON; -.
DR PRO; PR:Q9FXI9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXI9; baseline and differential.
DR Genevisible; Q9FXI9; 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..31
FT /evidence="ECO:0000255"
FT CHAIN 32..515
FT /note="Endoglucanase 2"
FT /id="PRO_0000249255"
FT ACT_SITE 100
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 433
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 515 AA; 56708 MW; F21BEC7479B5E209 CRC64;
MVAKPRSRCC CCSVFIGVII LIAIIIAVIF TIRHRSNHSD DDGSNVKNYA NALKIAMQFF
DIQKSGKLEN NEISWRGDSG LKDGSEASID LSKGLYDAGD HMKFGFPMAF TATVLSWSIL
EYGDQMASLN LLDHAKDSLK WTTDFLINAH PSPNVLYIQV GDPVTDHKCW DRPETMTRKR
TLTKIDTKTP GTEVAAETAA AMAAASLVFK ESDTKYSSTL LKHAKQLFDF ADNNRGSYSV
NIPEVQSYYN STGYGDELLW AASWLYHATE DQTYLDFVSE NGEEFGNFGS PSWFSWDNKL
PGTHILLSRL TFFKKGLSGS KGLQGFKETA EAVMCGLIPS SPTATSSRTD GGLIWVSEWN
ALQHPVSSAF LATLYSDYML TSGVKELSCS DQSFKPSDLR KFARSQADYM LGKNPEKMSY
LVGYGEKYPE FVHHRGASIP ADATTGCKDG FKWLNSDEPN PNVAYGALVG GPFLNDTFID
ARNNSMQNEP STYNSALVVG LLSSLVTTSS SVESF
