GUN25_ARATH
ID GUN25_ARATH Reviewed; 621 AA.
AC Q38890; Q56W54; Q56WU0; Q8H0S4; Q8LD74; Q94C24;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Endoglucanase 25;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase homolog OR16pep;
DE AltName: Full=Endo-1,4-beta glucanase 25;
DE AltName: Full=Protein KORRIGAN;
DE AltName: Full=Protein RADIALLY SWOLLEN 2;
GN Name=KOR; Synonyms=DEC, KOR1, RSW2; OrderedLocusNames=At5g49720;
GN ORFNames=K2I5.8;
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].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=10520455; DOI=10.3109/10425179809008460;
RA Loebler M.;
RT "An Arabidopsis thaliana cDNA homologous to cellulase.";
RL DNA Seq. 8:253-256(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=9755157; DOI=10.1093/emboj/17.19.5563;
RA Nicol F., His I., Jauneau A., Vernhettes S., Canut H., Hoefte H.;
RT "A plasma membrane-bound putative endo-1,4-beta-D-glucanase is required for
RT normal wall assembly and cell elongation in Arabidopsis.";
RL EMBO J. 17:5563-5576(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF 48-LYS-LYS-49 AND TYR-59.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10899980; DOI=10.2307/3871261;
RA Zuo J., Niu Q.-W., Nishizawa N., Wu Y., Kost B., Chua N.-H.;
RT "KORRIGAN, an Arabidopsis endo-1,4-beta-glucanase, localizes to the cell
RT plate by polarized targeting and is essential for cytokinesis.";
RL Plant Cell 12:1137-1152(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-621.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, AND MUTAGENESIS OF SER-183; GLY-344 AND GLY-429.
RX PubMed=11351091; DOI=10.1104/pp.126.1.278;
RA Lane D.R., Wiedemeier A., Peng L., Hoefte H., Vernhettes S., Desprez T.,
RA Hocart C.H., Birch R.J., Baskin T.I., Burn J.E., Arioli T., Betzner A.S.,
RA Williamson R.E.;
RT "Temperature-sensitive alleles of RSW2 link the KORRIGAN endo-1,4-beta-
RT glucanase to cellulose synthesis and cytokinesis in Arabidopsis.";
RL Plant Physiol. 126:278-288(2001).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [13]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF PRO-250 AND PRO-553.
RX PubMed=14871312; DOI=10.1111/j.1365-313x.2003.02000.x;
RA Szyjanowicz P.M., McKinnon I., Taylor N.G., Gardiner J., Jarvis M.C.,
RA Turner S.R.;
RT "The irregular xylem 2 mutant is an allele of korrigan that affects the
RT secondary cell wall of Arabidopsis thaliana.";
RL Plant J. 37:730-740(2004).
RN [14]
RP FUNCTION.
RX PubMed=16284310; DOI=10.1105/tpc.105.036228;
RA Robert S., Bichet A., Grandjean O., Kierzkowski D., Satiat-Jeunemaitre B.,
RA Pelletier S., Hauser M.-T., Hoefte H., Vernhettes S.;
RT "An Arabidopsis endo-1,4-beta-D-glucanase involved in cellulose synthesis
RT undergoes regulated intracellular cycling.";
RL Plant Cell 17:3378-3389(2005).
RN [15]
RP GLYCOSYLATION.
RX PubMed=18408158; DOI=10.1073/pnas.0800237105;
RA Kang J.S., Frank J., Kang C.H., Kajiura H., Vikram M., Ueda A., Kim S.,
RA Bahk J.D., Triplett B., Fujiyama K., Lee S.Y., von Schaewen A., Koiwa H.;
RT "Salt tolerance of Arabidopsis thaliana requires maturation of N-
RT glycosylated proteins in the Golgi apparatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5933-5938(2008).
CC -!- FUNCTION: Required for cellulose microfibrils formation. Involved in
CC cell wall assembly during cell elongation and cell plate maturation in
CC cytokinesis. Required for secondary cell wall formation in the
CC developing xylem. May cycle through different intracellular
CC compartments, including plasma membrane. {ECO:0000269|PubMed:10899980,
CC ECO:0000269|PubMed:11351091, ECO:0000269|PubMed:14871312,
CC ECO:0000269|PubMed:16284310, ECO:0000269|PubMed:9755157}.
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: Cell membrane {ECO:0000269|PubMed:9755157};
CC Single-pass type II membrane protein {ECO:0000269|PubMed:9755157}.
CC Note=Cell plate.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and stems, at
CC intermediate levels in leaves and flowers, and at lower levels in
CC siliques. Expressed in xylem (at protein level).
CC {ECO:0000269|PubMed:10899980, ECO:0000269|PubMed:14871312,
CC ECO:0000269|PubMed:9755157}.
CC -!- DEVELOPMENTAL STAGE: Expressed during hypocotyl elongation in the dark.
CC {ECO:0000269|PubMed:9755157}.
CC -!- PTM: Glycosylated. N-glycosylation of KOR in the endoplasmic reticulum
CC followed by N-glycan modifications in the Golgi are essential for
CC catalytic activity. {ECO:0000269|PubMed:18408158}.
CC -!- DISRUPTION PHENOTYPE: Plants are extremely dwarf and show severe
CC abnormal morphology with incomplete cell walls, aberrant cell plates
CC and multinucleated cells. {ECO:0000269|PubMed:9755157}.
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; U37702; AAB60304.1; -; mRNA.
DR EMBL; AF073875; AAC83240.1; -; Genomic_DNA.
DR EMBL; AF074092; AAC33467.1; -; Genomic_DNA.
DR EMBL; AF074375; AAC35344.1; -; mRNA.
DR EMBL; AB025613; BAA98160.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95850.1; -; Genomic_DNA.
DR EMBL; AY037218; AAK59818.1; -; mRNA.
DR EMBL; BT002221; AAN72232.1; -; mRNA.
DR EMBL; AY086165; AAM63370.1; -; mRNA.
DR EMBL; AK221941; BAD94393.1; -; mRNA.
DR EMBL; AK222193; BAD95336.1; -; mRNA.
DR PIR; S71215; S71215.
DR RefSeq; NP_199783.1; NM_124350.3.
DR AlphaFoldDB; Q38890; -.
DR SMR; Q38890; -.
DR BioGRID; 20281; 8.
DR STRING; 3702.AT5G49720.1; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR iPTMnet; Q38890; -.
DR SwissPalm; Q38890; -.
DR PaxDb; Q38890; -.
DR PRIDE; Q38890; -.
DR ProteomicsDB; 247246; -.
DR EnsemblPlants; AT5G49720.1; AT5G49720.1; AT5G49720.
DR GeneID; 835035; -.
DR Gramene; AT5G49720.1; AT5G49720.1; AT5G49720.
DR KEGG; ath:AT5G49720; -.
DR Araport; AT5G49720; -.
DR TAIR; locus:2157022; AT5G49720.
DR eggNOG; ENOG502QUUK; Eukaryota.
DR HOGENOM; CLU_008926_1_3_1; -.
DR InParanoid; Q38890; -.
DR OMA; KNPPKMS; -.
DR OrthoDB; 1195424at2759; -.
DR PhylomeDB; Q38890; -.
DR BioCyc; MetaCyc:MON-2367; -.
DR PRO; PR:Q38890; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38890; baseline and differential.
DR Genevisible; Q38890; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0005769; C:early endosome; IDA:TAIR.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0008810; F:cellulase activity; ISS:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:TAIR.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; IMP:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IMP: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 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 membrane; Cell wall biogenesis/degradation;
KW Cellulose degradation; Glycoprotein; Glycosidase; Hydrolase; Membrane;
KW Polysaccharide degradation; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..621
FT /note="Endoglucanase 25"
FT /id="PRO_0000249277"
FT TOPO_DOM 1..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..621
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..49
FT /note="Polarized targeting signal 1 (PTS1)"
FT REGION 59..62
FT /note="Polarized targeting signal 2 (PTS2)"
FT ACT_SITE 165
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 561
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 570
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 48..49
FT /note="LL->AA: Abolishes polarized targeting to cell
FT plate."
FT /evidence="ECO:0000269|PubMed:10899980"
FT MUTAGEN 59
FT /note="Y->A: Abolishes polarized targeting to cell plate."
FT /evidence="ECO:0000269|PubMed:10899980"
FT MUTAGEN 183
FT /note="S->N: In rsw2-3; decrease in cellulose production."
FT /evidence="ECO:0000269|PubMed:11351091"
FT MUTAGEN 250
FT /note="P->L: In irx2-1; decrease in cellulose production."
FT /evidence="ECO:0000269|PubMed:14871312"
FT MUTAGEN 344
FT /note="G->R: In rsw2-4; decrease in cellulose production."
FT /evidence="ECO:0000269|PubMed:11351091"
FT MUTAGEN 429
FT /note="G->R: In rsw2-1 and rsw2-2; decrease in cellulose
FT production."
FT /evidence="ECO:0000269|PubMed:11351091"
FT MUTAGEN 553
FT /note="P->L: In irx2-2; decrease in cellulose production."
FT /evidence="ECO:0000269|PubMed:14871312"
FT CONFLICT 7
FT /note="W -> S (in Ref. 7; AAM63370)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="Y -> D (in Ref. 6; AAK59818)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="W -> R (in Ref. 7; AAM63370)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="Y -> C (in Ref. 6; AAK59818/AAN72232)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="V -> A (in Ref. 8; BAD94393)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 621 AA; 69191 MW; 798D8B8CC5DEBF42 CRC64;
MYGRDPWGGP LEINTADSAT DDDRSRNLND LDRAALSRPL DETQQSWLLG PTEQKKKKYV
DLGCIIVSRK IFVWTVGTLV AAALLAGFIT LIVKTVPRHH PKTPPPDNYT IALHKALKFF
NAQKSGKLPK HNNVSWRGNS GLQDGKGETG SFYKDLVGGY YDAGDAIKFN FPMAYAMTML
SWSVIEYSAK YEAAGELTHV KELIKWGTDY FLKTFNSTAD SIDDLVSQVG SGNTDDGNTD
PNDHYCWMRP EDMDYKRPVT TCNGGCSDLA AEMAAALASA SIVFKDNKEY SKKLVHGAKV
VYQFGRTRRG RYSAGTAESS KFYNSSMYWD EFIWGGAWMY YATGNVTYLN LITQPTMAKH
AGAFWGGPYY GVFSWDNKLA GAQLLLSRLR LFLSPGYPYE EILRTFHNQT SIVMCSYLPI
FNKFNRTNGG LIELNHGAPQ PLQYSVNAAF LATLYSDYLD AADTPGWYCG PNFYSTSVLR
DFARSQIDYI LGKNPRKMSY VVGFGTKYPR HVHHRGASIP KNKVKYNCKG GWKWRDSKKP
NPNTIEGAMV AGPDKRDGYR DVRMNYNYTE PTLAGNAGLV AALVALSGEE EATGKIDKNT
IFSAVPPLFP TPPPPPAPWK P
