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   24-JAN-2024, entry version 115.
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.Q2V4L8; -.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   GlyCosmos; Q2V4L8; 1 site, No reported glycans.
DR   PaxDb; 3702-AT1G22880-1; -.
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; AT1G22880; CEL5.
DR   eggNOG; ENOG502QRXS; Eukaryota.
DR   HOGENOM; CLU_008926_1_2_1; -.
DR   InParanoid; Q2V4L8; -.
DR   OMA; WSANYLL; -.
DR   OrthoDB; 1347382at2759; -.
DR   PhylomeDB; Q2V4L8; -.
DR   BioCyc; ARA:AT1G22880-MONOMER; -.
DR   PRO; PR:Q2V4L8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q2V4L8; baseline and differential.
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   PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR   PANTHER; PTHR22298:SF111; ENDOGLUCANASE 3; 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   PROSITE; PS00698; GH9_3; 1.
DR   Genevisible; Q2V4L8; AT.
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
//