GUN3_ARATH
ID GUN3_ARATH Reviewed; 484 AA.
AC Q2V4L8; O23134;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Endoglucanase 3;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase 5;
DE Short=AtCEL5;
DE AltName: Full=Endo-1,4-beta glucanase 3;
DE Flags: Precursor;
GN Name=CEL5; OrderedLocusNames=At1g22880; ORFNames=F19G10.16;
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 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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
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 -!- FUNCTION: May be involved in the sloughing (cell-cell separation) of
CC the root cap cells from root tip. {ECO:0000269|PubMed:15604746}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2V4L8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2V4L8-2; Sequence=VSP_020386;
CC -!- TISSUE SPECIFICITY: Specifically expressed in root cap cells.
CC {ECO:0000269|PubMed:15604746}.
CC -!- INDUCTION: Down-regulated by auxin (IAA) and abscisic acid (ABA).
CC {ECO:0000269|PubMed:15604746}.
CC -!- MISCELLANEOUS: The sloughing of root-cap cells from the root tip is a
CC process of cell-cell separation that entails cell wall break down. It
CC is important in plant development because it assists the growing root
CC in penetrating the soil.
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; AF000657; AAB72171.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30299.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30300.1; -; Genomic_DNA.
DR PIR; G86362; G86362.
DR RefSeq; NP_001031082.1; NM_001036005.2. [Q2V4L8-2]
DR RefSeq; NP_173701.1; NM_102134.3. [Q2V4L8-1]
DR AlphaFoldDB; Q2V4L8; -.
DR SMR; Q2V4L8; -.
DR STRING; 3702.AT1G22880.1; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; Q2V4L8; -.
DR PRIDE; Q2V4L8; -.
DR ProteomicsDB; 247241; -. [Q2V4L8-1]
DR EnsemblPlants; AT1G22880.1; AT1G22880.1; AT1G22880. [Q2V4L8-1]
DR EnsemblPlants; AT1G22880.2; AT1G22880.2; AT1G22880. [Q2V4L8-2]
DR GeneID; 838893; -.
DR Gramene; AT1G22880.1; AT1G22880.1; AT1G22880. [Q2V4L8-1]
DR Gramene; AT1G22880.2; AT1G22880.2; AT1G22880. [Q2V4L8-2]
DR KEGG; ath:AT1G22880; -.
DR Araport; AT1G22880; -.
DR TAIR; locus:2017704; AT1G22880.
DR eggNOG; ENOG502QRXS; Eukaryota.
DR HOGENOM; CLU_008926_1_2_1; -.
DR InParanoid; Q2V4L8; -.
DR OMA; MKSSKHT; -.
DR OrthoDB; 1195424at2759; -.
DR PhylomeDB; Q2V4L8; -.
DR BioCyc; ARA:AT1G22880-MON; -.
DR PRO; PR:Q2V4L8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q2V4L8; baseline and differential.
DR Genevisible; Q2V4L8; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; 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 2: Evidence at transcript level;
KW Alternative splicing; Carbohydrate metabolism;
KW Cell wall biogenesis/degradation; Cellulose degradation; Glycoprotein;
KW Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..484
FT /note="Endoglucanase 3"
FT /id="PRO_0000249256"
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 CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_020386"
SQ SEQUENCE 484 AA; 53662 MW; FFB4FF2A83AE813B CRC64;
MASPFFFVFL LSALSLENTY ASPNYREALS KSLLFFQGQR SGRLPSDQQL SWRSSSGLSD
GSSAHVDLTG GYYDAGDNVK FNFPMAFTTT MLSWSSLEYG KKMGPELQNS RVAIRWATDY
LLKCARATPG KLYVGVGDPN GDHKCWERPE DMDTPRTVYS VSPSNPGSDV AAETAAALAA
SSMVFRKVDP KYSRLLLATA KKVMQFAIQY RGAYSNSLSS SVCPFYCSYS GYKDELLWGA
AWLHRATNDP YYTNFIKSLG GGDQPDIFSW DNKYAGAYVL LSRRAVLNKD NNFELYKQAA
ENFMCKILPN SPSSSTKYTK GGLMYKLPQS NLQYVTSITF LLTTYAKYMK STKQTFNCGN
SLIVPNALIN LSKRQVDYVL GVNPMKMSYM VGFSSNFPKR IHHRGSSLPS RAVRSNSLGC
NGGFQSFRTQ NPNPNILTGA IVGGPNQNDE YPDQRDDYTR SEPATYINAA FVGPLAYFAA
SRSP
