GUN9_ARATH
ID GUN9_ARATH Reviewed; 484 AA.
AC Q9C9H5; P80855; Q38817; Q8LDE8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Endoglucanase 9;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase 3;
DE Short=AtCEL3;
DE AltName: Full=Endo-1,4-beta glucanase 9;
DE Flags: Precursor;
GN Name=CEL3; OrderedLocusNames=At1g71380; ORFNames=F26A9.24;
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] {ECO:0000312|EMBL:AAG51817.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000312|EMBL:AAG51817.1};
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] {ECO:0000312|EMBL:AAM63253.1}
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] {ECO:0000312|EMBL:AAM63253.1}
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-484.
RC STRAIN=cv. Columbia;
RA Lu G., Ferl R.J.;
RT "An Arabidopsis cDNA encoding beta-glucanase.";
RL Plant Mol. Biol. 29:883-883(1995).
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 22-40, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9188482; DOI=10.1074/jbc.272.25.15841;
RA Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P.,
RA Slabas A.R.;
RT "Differential extraction and protein sequencing reveals major differences
RT in patterns of primary cell wall proteins from plants.";
RL J. Biol. Chem. 272:15841-15848(1997).
RN [6]
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).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15604746; DOI=10.1007/s11103-004-3380-3;
RA del Campillo E., Abdel-Aziz A., Crawford D., Patterson S.E.;
RT "Root cap specific expression of an endo-beta-1,4-D-glucanase (cellulase):
RT a new marker to study root development in Arabidopsis.";
RL Plant Mol. Biol. 56:309-323(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, cell wall {ECO:0000269|PubMed:9188482}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in root cap cells.
CC {ECO:0000269|PubMed:15604746}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA90944.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC016163; AAG51817.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35195.1; -; Genomic_DNA.
DR EMBL; AY086043; AAM63253.1; -; mRNA.
DR EMBL; U17888; AAA90944.1; ALT_FRAME; mRNA.
DR PIR; S61430; S61430.
DR RefSeq; NP_177294.1; NM_105807.2.
DR AlphaFoldDB; Q9C9H5; -.
DR SMR; Q9C9H5; -.
DR BioGRID; 28699; 8.
DR IntAct; Q9C9H5; 16.
DR STRING; 3702.AT1G71380.1; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; Q9C9H5; -.
DR PRIDE; Q9C9H5; -.
DR ProteomicsDB; 247320; -.
DR EnsemblPlants; AT1G71380.1; AT1G71380.1; AT1G71380.
DR GeneID; 843479; -.
DR Gramene; AT1G71380.1; AT1G71380.1; AT1G71380.
DR KEGG; ath:AT1G71380; -.
DR Araport; AT1G71380; -.
DR TAIR; locus:2825314; AT1G71380.
DR eggNOG; ENOG502QRXS; Eukaryota.
DR HOGENOM; CLU_008926_1_2_1; -.
DR InParanoid; Q9C9H5; -.
DR OMA; GGFQPFF; -.
DR OrthoDB; 1195424at2759; -.
DR PhylomeDB; Q9C9H5; -.
DR BioCyc; ARA:AT1G71380-MON; -.
DR BRENDA; 3.2.1.4; 399.
DR PRO; PR:Q9C9H5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9H5; baseline and differential.
DR Genevisible; Q9C9H5; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; 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; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
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.
DR PROSITE; PS00698; GH9_3; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall; Cell wall biogenesis/degradation;
KW Cellulose degradation; Direct protein sequencing; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:9188482"
FT CHAIN 22..484
FT /note="Endoglucanase 9"
FT /id="PRO_0000043221"
FT ACT_SITE 77
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT CONFLICT 135
FT /note="G -> A (in Ref. 4; AAA90944)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="E -> K (in Ref. 4; AAA90944)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="D -> N (in Ref. 3; AAM63253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 53274 MW; 227D3945FCD2AF39 CRC64;
MTSLFFFVLL FSSLLISNGD ANPNYKEALS KSLLFFQGQR SGPLPRGQQI SWRASSGLSD
GSAAHVDLTG GYYDAGDNVK FNLPMAFTTT MLSWSALEYG KRMGPELENA RVNIRWATDY
LLKCARATPG KLYVGVGDPN VDHKCWERPE DMDTPRTVYS VSASNPGSDV AAETAAALAA
ASMVFRKVDS KYSRLLLATA KDVMQFAIQY QGAYSDSLSS SVCPFYCSYS GYKDELMWGA
SWLLRATNNP YYANFIKSLG GGDQPDIFSW DNKYAGAYVL LSRRALLNKD SNFEQYKQAA
ENFICKILPD SPSSSTQYTQ GGLMYKLPQS NLQYVTSITF LLTTYAKYMK ATKHTFNCGS
SVIVPNALIS LSKRQVDYIL GDNPIKMSYM VGFSSNFPKR IHHRASSLPS HALRSQSLGC
NGGFQSFYTQ NPNPNILTGA IVGGPNQNDG YPDQRDDYSH AEPATYINAA FVGPLAYFAA
GRST
