GUN10_ARATH
ID GUN10_ARATH Reviewed; 525 AA.
AC Q8LCP6; Q9LR07;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Endoglucanase 10;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 10;
DE Flags: Precursor;
GN OrderedLocusNames=At1g75680; ORFNames=F10A5.13;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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; AC006434; AAF87112.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35745.1; -; Genomic_DNA.
DR EMBL; AY039938; AAK64042.1; -; mRNA.
DR EMBL; AY150451; AAN12892.1; -; mRNA.
DR EMBL; AY086475; AAM63477.1; -; mRNA.
DR PIR; E96786; E96786.
DR RefSeq; NP_177697.1; NM_106219.3.
DR AlphaFoldDB; Q8LCP6; -.
DR SMR; Q8LCP6; -.
DR STRING; 3702.AT1G75680.1; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR SwissPalm; Q8LCP6; -.
DR PaxDb; Q8LCP6; -.
DR PRIDE; Q8LCP6; -.
DR ProteomicsDB; 230116; -.
DR EnsemblPlants; AT1G75680.1; AT1G75680.1; AT1G75680.
DR GeneID; 843902; -.
DR Gramene; AT1G75680.1; AT1G75680.1; AT1G75680.
DR KEGG; ath:AT1G75680; -.
DR Araport; AT1G75680; -.
DR TAIR; locus:2005599; AT1G75680.
DR eggNOG; ENOG502QRF6; Eukaryota.
DR HOGENOM; CLU_008926_1_4_1; -.
DR InParanoid; Q8LCP6; -.
DR OMA; SKNNEAH; -.
DR OrthoDB; 1195424at2759; -.
DR PhylomeDB; Q8LCP6; -.
DR BioCyc; ARA:AT1G75680-MON; -.
DR PRO; PR:Q8LCP6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LCP6; baseline and differential.
DR Genevisible; Q8LCP6; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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..525
FT /note="Endoglucanase 10"
FT /id="PRO_0000249262"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 45
FT /note="G -> C (in Ref. 4; AAM63477)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="N -> D (in Ref. 4; AAM63477)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 57868 MW; FBC3704F4BB8BB71 CRC64;
MEEKSKSRGW CGWFIAIIVL ASVILAVVYT VKLRTKKSGD DDGGGPVPGP PGAIDKKYAD
ALKLALQFFD IQKSGKLENN KIPWRGDSGL KDGSEDNLDL SKGLYDAGDH IKFGFPMAFT
ATVLSWSILE YGDQMNAVNQ LDPAKDSLRW ITDYLIKAHP SDNVLYIQVG DPKVDHPCWE
RPEDMKEKRP LTKIDVDTPG TEVAAETAAA MASASLVFKD SDPTYSATLL KHAKQLFNFA
DTKRGSYSVN IPEVQKFYNS TGYGDELLWA ASWLYHATED KTYLDYVSNH GKEFASFGNP
TWFSWDNKLA GTQVLLSRLL FFKKDLSGSK GLGNYRNTAK AVMCGLLPKS PTSTASRTNG
GLIWVSEWNS MQQSVSSAFL ASLFSDYMLT SRIHKISCDG KIFKATELRD FAKSQADYML
GKNPLGTSFV VGYGDKYPQF VHHRGASIPA DATTGCLDGF KWFNSTKPNP NIAYGALVGG
PFFNETFTDS RENPMQNEPT TYNNALLVGL LSSLVTTSST LQSLK
