GUN7_ARATH
ID GUN7_ARATH Reviewed; 623 AA.
AC O04478;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Endoglucanase 7;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 7;
GN Name=KOR2; OrderedLocusNames=At1g65610; ORFNames=F5I14.14;
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 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 [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11488474; DOI=10.1023/a:1010688726755;
RA Moelhoej M., Joergensen B., Ulvskov P., Borkhardt B.;
RT "Two Arabidopsis thaliana genes, KOR2 and KOR3, which encode membrane-
RT anchored endo-1,4-beta-D-glucanases, are differentially expressed in
RT developing leaf trichomes and their support cells.";
RL Plant Mol. Biol. 46:263-275(2001).
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: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in basal region of leaf blade and
CC proximal parts of leaf and floral organ. {ECO:0000269|PubMed:11488474}.
CC -!- DEVELOPMENTAL STAGE: Early expressed in the development of root hairs
CC within the root differentiation zone. Expressed late in the development
CC of leaf trichomes when the stalks and branches are expanded.
CC {ECO:0000269|PubMed:11488474}.
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; AC001229; AAB60922.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34400.1; -; Genomic_DNA.
DR EMBL; AK229402; BAF01264.1; -; mRNA.
DR PIR; B96681; B96681.
DR RefSeq; NP_176738.1; NM_105234.3.
DR AlphaFoldDB; O04478; -.
DR SMR; O04478; -.
DR STRING; 3702.AT1G65610.1; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; O04478; -.
DR PRIDE; O04478; -.
DR ProteomicsDB; 247151; -.
DR EnsemblPlants; AT1G65610.1; AT1G65610.1; AT1G65610.
DR GeneID; 842872; -.
DR Gramene; AT1G65610.1; AT1G65610.1; AT1G65610.
DR KEGG; ath:AT1G65610; -.
DR Araport; AT1G65610; -.
DR TAIR; locus:2034158; AT1G65610.
DR eggNOG; ENOG502QSIM; Eukaryota.
DR HOGENOM; CLU_008926_1_3_1; -.
DR InParanoid; O04478; -.
DR OMA; TMCSYLH; -.
DR OrthoDB; 1195424at2759; -.
DR PhylomeDB; O04478; -.
DR BioCyc; ARA:AT1G65610-MON; -.
DR PRO; PR:O04478; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04478; baseline and differential.
DR Genevisible; O04478; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Carbohydrate metabolism; 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..623
FT /note="Endoglucanase 7"
FT /id="PRO_0000249260"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..623
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 565
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 623 AA; 69836 MW; 8186D6B5497D1FD4 CRC64;
MHPGNVWGGS LDAVDSDRIA AEEEERLRNT TEWDRGAIHS QRSELDETQQ GWLLAPQDNW
RKKKKKYVNL GCVSVSRTVF LWTVGSIAVL FLVVALPIII VKSLPRHKSA PPPPDNYTLA
LHKALQFFDA QKSGKLPKKN KVSWRGDSGT KDGLPDVVGG LVGGYYDGGS NVKFHFPMAF
SMTMLSWSLI EYSHKYKAID EYDHMRDVLK WGTDYLLLTF NNSATRLDHI YTQVGGGLRD
SESPDDIYCW QKPEDMSYDR PVLSSTSAAD LGAEVSAALA AASIVFTDKP DYAKKLKKGA
ETLYPFFRSK SRRKRYSDGQ PTAQAFYNST SMFDEFMWAG AWLYYATGNK TYIQFATTPS
VPQTAKAFAN RPELMVPSWN NKLPGAMLLM TRYRLFLNPG FPYENMLNRY HNATGITMCA
YLKQYNVFNR TSGGLMQLNL GKPRPLEYVA HASFLASLFA DYLNSTGVPG WYCGPTFVEN
HVLKDFAQSQ IDYILGDNPL KMSYVVGFGK KFPRRVHHRG ATIPNDKKRR SCREGLKYRD
TKNPNPNNIT GAMVGGPNKF DEFHDLRNNY NASEPTLSGN AGLVAALVSL TSSGGQQIDK
NTMFNSVPPL YSPTPPPPKA WKP
