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Endoglucanase 25 (EC 3.2.1.4) (Cellulase homolog OR16pep) (Endo-1,4-beta glucanase 25) (Protein KORRIGAN) (Protein RADIALLY SWOLLEN 2)

 GUN25_ARATH             Reviewed;         621 AA.
Q38890; Q56W54; Q56WU0; Q8H0S4; Q8LD74; Q94C24;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-JUL-2017, entry version 131.
RecName: Full=Endoglucanase 25;
EC=3.2.1.4;
AltName: Full=Cellulase homolog OR16pep;
AltName: Full=Endo-1,4-beta glucanase 25;
AltName: Full=Protein KORRIGAN;
AltName: Full=Protein RADIALLY SWOLLEN 2;
Name=KOR; Synonyms=DEC, KOR1, RSW2; OrderedLocusNames=At5g49720;
ORFNames=K2I5.8;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=10520455; DOI=10.3109/10425179809008460;
Loebler M.;
"An Arabidopsis thaliana cDNA homologous to cellulase.";
DNA Seq. 8:253-256(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=9755157; DOI=10.1093/emboj/17.19.5563;
Nicol F., His I., Jauneau A., Vernhettes S., Canut H., Hoefte H.;
"A plasma membrane-bound putative endo-1,4-beta-D-glucanase is
required for normal wall assembly and cell elongation in
Arabidopsis.";
EMBO J. 17:5563-5576(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF 48-LYS-LYS-49 AND TYR-59.
STRAIN=cv. Landsberg erecta;
PubMed=10899980; DOI=10.1105/tpc.12.7.1137;
Zuo J., Niu Q.-W., Nishizawa N., Wu Y., Kost B., Chua N.-H.;
"KORRIGAN, an Arabidopsis endo-1,4-beta-glucanase, localizes to the
cell plate by polarized targeting and is essential for cytokinesis.";
Plant Cell 12:1137-1152(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-621.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION, AND MUTAGENESIS OF SER-183; GLY-344 AND GLY-429.
PubMed=11351091; DOI=10.1104/pp.126.1.278;
Lane D.R., Wiedemeier A., Peng L., Hoefte H., Vernhettes S.,
Desprez T., Hocart C.H., Birch R.J., Baskin T.I., Burn J.E.,
Arioli T., Betzner A.S., Williamson R.E.;
"Temperature-sensitive alleles of RSW2 link the KORRIGAN endo-1,4-
beta-glucanase to cellulose synthesis and cytokinesis in
Arabidopsis.";
Plant Physiol. 126:278-288(2001).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. La-0;
PubMed=14506206; DOI=10.1074/mcp.T300006-MCP200;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Large-scale analysis of in vivo phosphorylated membrane proteins by
immobilized metal ion affinity chromatography and mass spectrometry.";
Mol. Cell. Proteomics 2:1234-1243(2003).
[11]
GENE FAMILY.
PubMed=15170254; DOI=10.1007/s00239-003-2571-x;
Libertini E., Li Y., McQueen-Mason S.J.;
"Phylogenetic analysis of the plant endo-beta-1,4-glucanase gene
family.";
J. Mol. Evol. 58:506-515(2004).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15308754; DOI=10.1105/tpc.104.023150;
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
"Phosphoproteomics of the Arabidopsis plasma membrane and a new
phosphorylation site database.";
Plant Cell 16:2394-2405(2004).
[13]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF PRO-250 AND PRO-553.
PubMed=14871312; DOI=10.1111/j.1365-313X.2003.02000.x;
Szyjanowicz P.M., McKinnon I., Taylor N.G., Gardiner J., Jarvis M.C.,
Turner S.R.;
"The irregular xylem 2 mutant is an allele of korrigan that affects
the secondary cell wall of Arabidopsis thaliana.";
Plant J. 37:730-740(2004).
[14]
FUNCTION.
PubMed=16284310; DOI=10.1105/tpc.105.036228;
Robert S., Bichet A., Grandjean O., Kierzkowski D.,
Satiat-Jeunemaitre B., Pelletier S., Hauser M.-T., Hoefte H.,
Vernhettes S.;
"An Arabidopsis endo-1,4-beta-D-glucanase involved in cellulose
synthesis undergoes regulated intracellular cycling.";
Plant Cell 17:3378-3389(2005).
[15]
GLYCOSYLATION.
PubMed=18408158; DOI=10.1073/pnas.0800237105;
Kang J.S., Frank J., Kang C.H., Kajiura H., Vikram M., Ueda A.,
Kim S., Bahk J.D., Triplett B., Fujiyama K., Lee S.Y.,
von Schaewen A., Koiwa H.;
"Salt tolerance of Arabidopsis thaliana requires maturation of N-
glycosylated proteins in the Golgi apparatus.";
Proc. Natl. Acad. Sci. U.S.A. 105:5933-5938(2008).
-!- FUNCTION: Required for cellulose microfibrils formation. Involved
in cell wall assembly during cell elongation and cell plate
maturation in cytokinesis. Required for secondary cell wall
formation in the developing xylem. May cycle through different
intracellular compartments, including plasma membrane.
{ECO:0000269|PubMed:10899980, ECO:0000269|PubMed:11351091,
ECO:0000269|PubMed:14871312, ECO:0000269|PubMed:16284310,
ECO:0000269|PubMed:9755157}.
-!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic
linkages in cellulose, lichenin and cereal beta-D-glucans.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9755157};
Single-pass type II membrane protein {ECO:0000269|PubMed:9755157}.
Note=Cell plate.
-!- TISSUE SPECIFICITY: Highly expressed in roots and stems, at
intermediate levels in leaves and flowers, and at lower levels in
siliques. Expressed in xylem (at protein level).
{ECO:0000269|PubMed:10899980, ECO:0000269|PubMed:14871312,
ECO:0000269|PubMed:9755157}.
-!- DEVELOPMENTAL STAGE: Expressed during hypocotyl elongation in the
dark. {ECO:0000269|PubMed:9755157}.
-!- PTM: Glycosylated. N-glycosylation of KOR in the endoplasmic
reticulum followed by N-glycan modifications in the Golgi are
essential for catalytic activity. {ECO:0000269|PubMed:18408158}.
-!- DISRUPTION PHENOTYPE: Plants are extremely dwarf and show severe
abnormal morphology with incomplete cell walls, aberrant cell
plates and multinucleated cells. {ECO:0000269|PubMed:9755157}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E)
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U37702; AAB60304.1; -; mRNA.
EMBL; AF073875; AAC83240.1; -; Genomic_DNA.
EMBL; AF074092; AAC33467.1; -; Genomic_DNA.
EMBL; AF074375; AAC35344.1; -; mRNA.
EMBL; AB025613; BAA98160.1; -; Genomic_DNA.
EMBL; CP002688; AED95850.1; -; Genomic_DNA.
EMBL; AY037218; AAK59818.1; -; mRNA.
EMBL; BT002221; AAN72232.1; -; mRNA.
EMBL; AY086165; AAM63370.1; -; mRNA.
EMBL; AK221941; BAD94393.1; -; mRNA.
EMBL; AK222193; BAD95336.1; -; mRNA.
PIR; S71215; S71215.
RefSeq; NP_199783.1; NM_124350.3.
UniGene; At.21098; -.
UniGene; At.23416; -.
ProteinModelPortal; Q38890; -.
SMR; Q38890; -.
BioGrid; 20281; 8.
STRING; 3702.AT5G49720.1; -.
CAZy; GH9; Glycoside Hydrolase Family 9.
iPTMnet; Q38890; -.
SwissPalm; Q38890; -.
PaxDb; Q38890; -.
EnsemblPlants; AT5G49720.1; AT5G49720.1; AT5G49720.
GeneID; 835035; -.
Gramene; AT5G49720.1; AT5G49720.1; AT5G49720.
KEGG; ath:AT5G49720; -.
Araport; AT5G49720; -.
TAIR; locus:2157022; AT5G49720.
eggNOG; ENOG410IE9Y; Eukaryota.
eggNOG; ENOG410XP0H; LUCA.
HOGENOM; HOG000021033; -.
InParanoid; Q38890; -.
OMA; GPLEINT; -.
OrthoDB; EOG093604V7; -.
PhylomeDB; Q38890; -.
BioCyc; MetaCyc:MONOMER-2367; -.
PRO; PR:Q38890; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q38890; baseline and differential.
Genevisible; Q38890; AT.
GO; GO:0009504; C:cell plate; IDA:TAIR.
GO; GO:0005769; C:early endosome; IDA:TAIR.
GO; GO:0005768; C:endosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
GO; GO:0008810; F:cellulase activity; ISS:TAIR.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
GO; GO:0043622; P:cortical microtubule organization; IMP:TAIR.
GO; GO:0042538; P:hyperosmotic salinity response; IMP:TAIR.
GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
GO; GO:0048367; P:shoot system development; IMP:TAIR.
GO; GO:0009826; P:unidimensional cell growth; IMP:TAIR.
InterPro; IPR008928; 6-hairpin_glycosidase-like.
InterPro; IPR001701; Glyco_hydro_9.
InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
InterPro; IPR018221; Glyco_hydro_9_His_AS.
Pfam; PF00759; Glyco_hydro_9; 1.
SUPFAM; SSF48208; SSF48208; 1.
PROSITE; PS00592; GLYCOSYL_HYDROL_F9_1; 1.
PROSITE; PS00698; GLYCOSYL_HYDROL_F9_2; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Cell membrane;
Cell wall biogenesis/degradation; Cellulose degradation;
Complete proteome; Glycoprotein; Glycosidase; Hydrolase; Membrane;
Polysaccharide degradation; Reference proteome; Signal-anchor;
Transmembrane; Transmembrane helix.
CHAIN 1 621 Endoglucanase 25.
/FTId=PRO_0000249277.
TOPO_DOM 1 70 Cytoplasmic. {ECO:0000255}.
TRANSMEM 71 91 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 92 621 Extracellular. {ECO:0000255}.
REGION 48 49 Polarized targeting signal 1 (PTS1).
REGION 59 62 Polarized targeting signal 2 (PTS2).
ACT_SITE 513 513 {ECO:0000250}.
ACT_SITE 561 561 {ECO:0000250}.
ACT_SITE 570 570 {ECO:0000250}.
CARBOHYD 108 108 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 216 216 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 425 425 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 567 567 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 48 49 LL->AA: Abolishes polarized targeting to
cell plate.
{ECO:0000269|PubMed:10899980}.
MUTAGEN 59 59 Y->A: Abolishes polarized targeting to
cell plate.
{ECO:0000269|PubMed:10899980}.
MUTAGEN 183 183 S->N: In rsw2-3; decrease in cellulose
production.
{ECO:0000269|PubMed:11351091}.
MUTAGEN 250 250 P->L: In irx2-1; decrease in cellulose
production.
{ECO:0000269|PubMed:14871312}.
MUTAGEN 344 344 G->R: In rsw2-4; decrease in cellulose
production.
{ECO:0000269|PubMed:11351091}.
MUTAGEN 429 429 G->R: In rsw2-1 and rsw2-2; decrease in
cellulose production.
{ECO:0000269|PubMed:11351091}.
MUTAGEN 553 553 P->L: In irx2-2; decrease in cellulose
production.
{ECO:0000269|PubMed:14871312}.
CONFLICT 7 7 W -> S (in Ref. 7; AAM63370).
{ECO:0000305}.
CONFLICT 59 59 Y -> D (in Ref. 6; AAK59818).
{ECO:0000305}.
CONFLICT 338 338 W -> R (in Ref. 7; AAM63370).
{ECO:0000305}.
CONFLICT 397 397 Y -> C (in Ref. 6; AAK59818/AAN72232).
{ECO:0000305}.
CONFLICT 605 605 V -> A (in Ref. 8; BAD94393).
{ECO:0000305}.
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


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