ID   GUN1_ARATH              Reviewed;         501 AA.
AC   Q9SRX3; O64949;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 135.
DE   RecName: Full=Endoglucanase 1;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase 2;
DE            Short=AtCEL2;
DE   AltName: Full=Endo-1,4-beta glucanase 1;
DE   Flags: Precursor;
GN   Name=CEL2; OrderedLocusNames=At1g02800; ORFNames=F22D16.21;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=10074717; DOI=10.1046/j.1365-313x.1999.00359.x;
RA   Yung M.-H., Schaffer R., Putterill J.;
RT   "Identification of genes expressed during early Arabidopsis carpel
RT   development by mRNA differential display: characterisation of ATCEL2, a
RT   novel endo-1,4-beta-D-glucanase gene.";
RL   Plant J. 17:203-208(1999).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) 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:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing septum and ovule
CC       primordia during the early stages of flower development.
CC       {ECO:0000269|PubMed:10074717}.
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; AF034573; AAC16418.1; -; mRNA.
DR   EMBL; AC009525; AAF02887.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27471.1; -; Genomic_DNA.
DR   EMBL; AK228979; BAF00867.1; -; mRNA.
DR   PIR; A86158; A86158.
DR   PIR; T52135; T52135.
DR   RefSeq; NP_171779.1; NM_100159.3.
DR   AlphaFoldDB; Q9SRX3; -.
DR   SMR; Q9SRX3; -.
DR   STRING; 3702.Q9SRX3; -.
DR   CAZy; GH9; Glycoside Hydrolase Family 9.
DR   MetOSite; Q9SRX3; -.
DR   PaxDb; 3702-AT1G02800-1; -.
DR   ProteomicsDB; 247240; -.
DR   EnsemblPlants; AT1G02800.1; AT1G02800.1; AT1G02800.
DR   GeneID; 839385; -.
DR   Gramene; AT1G02800.1; AT1G02800.1; AT1G02800.
DR   KEGG; ath:AT1G02800; -.
DR   Araport; AT1G02800; -.
DR   TAIR; AT1G02800; CEL2.
DR   eggNOG; ENOG502QPI6; Eukaryota.
DR   HOGENOM; CLU_008926_1_2_1; -.
DR   InParanoid; Q9SRX3; -.
DR   OMA; KMGESNM; -.
DR   OrthoDB; 1347382at2759; -.
DR   PhylomeDB; Q9SRX3; -.
DR   BioCyc; ARA:AT1G02800-MONOMER; -.
DR   PRO; PR:Q9SRX3; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SRX3; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; TAS:TAIR.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007389; P:pattern specification process; TAS:TAIR.
DR   GO; GO:0009624; P:response to nematode; IEP:TAIR.
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:SF124; ENDOGLUCANASE 1; 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; Q9SRX3; AT.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW   Cellulose degradation; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..501
FT                   /note="Endoglucanase 1"
FT                   /id="PRO_0000249254"
FT   ACT_SITE        96
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT   ACT_SITE        473
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT   ACT_SITE        482
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT   CONFLICT        330
FT                   /note="L -> I (in Ref. 1; AAC16418)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   501 AA;  55419 MW;  913F592A058505B7 CRC64;
     MALYLSSSRL ITFLSFILLL SNGFSSSSSR PSIHHRHHLD NHNYKDALSK SILFFEGQRS
     GKLPPNQRMT WRSNSGLSDG SALNVDLVGG YYDAGDNMKF GFPMAFTTTM LSWSLIEFGG
     LMKSELPNAK DAIRWATDFL LKATSHPDTI YVQVGDPNMD HACWERPEDM DTPRSVFKVD
     KNNPGSDIAG EIAAALAAAS IVFRKCDPSY SNHLLQRAIT VFTFADKYRG PYSAGLAPEV
     CPFYCSYSGY QDELLWGAAW LQKATNNPTY LNYIKANGQI LGADEFDNMF SWDNKHVGAR
     ILLSKEFLIQ KVKSLEEYKE HADSFICSVL PGASSSQYTP GGLLFKMGES NMQYVTSTSF
     LLLTYAKYLT SARTVAYCGG SVVTPARLRS IAKKQVDYLL GGNPLKMSYM VGYGLKYPRR
     IHHRGSSLPS VAVHPTRIQC HDGFSLFTSQ SPNPNDLVGA VVGGPDQNDQ FPDERSDYGR
     SEPATYINAP LVGALAYLAR S
//