GUN5_ARATH
ID GUN5_ARATH Reviewed; 627 AA.
AC Q9M995;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Endoglucanase 5;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 5;
DE Flags: Precursor;
GN OrderedLocusNames=At1g48930; ORFNames=F27J15.28, F27K7.5;
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;
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 [4]
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 -!- INTERACTION:
CC Q9M995; Q9SZU7: KAI2; NbExp=3; IntAct=EBI-25530015, EBI-25519488;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; AC016041; AAF69707.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32368.1; -; Genomic_DNA.
DR EMBL; BT002935; AAO22749.1; -; mRNA.
DR EMBL; BT005638; AAO64058.1; -; mRNA.
DR PIR; B96527; B96527.
DR RefSeq; NP_175323.1; NM_103786.3.
DR AlphaFoldDB; Q9M995; -.
DR SMR; Q9M995; -.
DR BioGRID; 26540; 1.
DR IntAct; Q9M995; 1.
DR STRING; 3702.AT1G48930.1; -.
DR CAZy; CBM49; Carbohydrate-Binding Module Family 49.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; Q9M995; -.
DR PRIDE; Q9M995; -.
DR ProteomicsDB; 247318; -.
DR EnsemblPlants; AT1G48930.1; AT1G48930.1; AT1G48930.
DR GeneID; 841315; -.
DR Gramene; AT1G48930.1; AT1G48930.1; AT1G48930.
DR KEGG; ath:AT1G48930; -.
DR Araport; AT1G48930; -.
DR TAIR; locus:2028441; AT1G48930.
DR eggNOG; ENOG502QRF6; Eukaryota.
DR HOGENOM; CLU_008926_1_4_1; -.
DR InParanoid; Q9M995; -.
DR OMA; TNAKDMY; -.
DR OrthoDB; 1195424at2759; -.
DR PhylomeDB; Q9M995; -.
DR BioCyc; ARA:AT1G48930-MON; -.
DR PRO; PR:Q9M995; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M995; baseline and differential.
DR Genevisible; Q9M995; AT.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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; IPR019028; CBM_49.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR Pfam; PF09478; CBM49; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM01063; CBM49; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation;
KW Cellulose degradation; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..627
FT /note="Endoglucanase 5"
FT /id="PRO_0000249258"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 477
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 627 AA; 69080 MW; 271C44CB63F06644 CRC64;
MRKFGGSLFG VSLLLSVLLA AATAAAEYYN YGSALDKTFL FFEAQRSGKL PAAQRVKWRG
PSGLKDGLAQ GVSLEGGYYD AGDHVKFGLP MAFAVTMLSW AAVDNRKELS SSNQMQQTLW
SIRWGTDYFI KAHPQPNVLW GQVGDGESDH YCWERPEDMT TSRTAYKLDP YHPGSDLAGE
TAAALAAASL AFKPFNSSYS ALLLSHAKEL FSFADKYRGL YTNSIPNAKA FYMSSGYSDE
LLWAAAWLHR ATGDQYYLKY AMDNSGYMGG TGWGVKEFSW DNKYAGVQIL LSKILLEGKG
GIYTSTLKQY QTKADYFACA CLKKNGGYNI QTTPGGLMYV REWNNLQYAS AAAYLLAVYS
DYLSAANAKL NCPDGLVQPQ GLLDFARSQA DYILGKNRQG MSYVVGYGPK YPIRVHHRGS
SIPSIFAQRS SVSCVQGFDS WYRRSQGDPN VIYGALVGGP DENDNYSDDR SNYEQSEPTL
SGTAPLVGLF AKLYGGSLGS YGGGSYKPYE TTKPAASSYK ATPTTYSPKQ SGAQIEFLHS
ITSNWIAGNT RYYRHKVIIK NNSQKPISDL KLKIEDLSGP IWGLNPTGQK YTYQLPQWQK
TLRAGQAYDF VYVQGGPQAK VSVLSYN
