GUN19_ARATH
ID GUN19_ARATH Reviewed; 626 AA.
AC Q8L7I0; O82513;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Endoglucanase 19;
DE EC=3.2.1.4;
DE AltName: Full=Endo-1,4-beta glucanase 19;
DE Flags: Precursor;
GN OrderedLocusNames=At4g11050; ORFNames=F2P3.1, T22B4.30;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC35539.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB43040.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81206.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF080120; AAC35539.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL049876; CAB43040.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161518; CAB81206.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82966.1; -; Genomic_DNA.
DR EMBL; AY133685; AAM91619.1; -; mRNA.
DR PIR; T01929; T01929.
DR RefSeq; NP_001328091.1; NM_001340701.1.
DR RefSeq; NP_192843.2; NM_117175.3.
DR AlphaFoldDB; Q8L7I0; -.
DR SMR; Q8L7I0; -.
DR STRING; 3702.AT4G11050.1; -.
DR CAZy; CBM49; Carbohydrate-Binding Module Family 49.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR PaxDb; Q8L7I0; -.
DR PRIDE; Q8L7I0; -.
DR EnsemblPlants; AT4G11050.1; AT4G11050.1; AT4G11050.
DR GeneID; 826706; -.
DR Gramene; AT4G11050.1; AT4G11050.1; AT4G11050.
DR KEGG; ath:AT4G11050; -.
DR Araport; AT4G11050; -.
DR TAIR; locus:2136073; AT4G11050.
DR eggNOG; ENOG502QRF6; Eukaryota.
DR HOGENOM; CLU_008926_1_4_1; -.
DR InParanoid; Q8L7I0; -.
DR OrthoDB; 1195424at2759; -.
DR PhylomeDB; Q8L7I0; -.
DR BioCyc; ARA:AT4G11050-MON; -.
DR PRO; PR:Q8L7I0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L7I0; baseline and differential.
DR Genevisible; Q8L7I0; 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; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
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.
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;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..626
FT /note="Endoglucanase 19"
FT /id="PRO_0000249271"
FT REGION 515..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..529
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 626 AA; 69345 MW; 6F7457C97EEF655F CRC64;
MGSRTTISIL VVLLLGLVQL AISGHDYKQA LSKSILFFEA QRSGHLPPNQ RVSWRSHSGL
YDGKSSGVDL VGGYYDAGDN VKFGLPMAFT VTTMCWSIIE YGGQLESNGE LGHAIDAVKW
GTDYFIKAHP EPNVLYGEVG DGKSDHYCWQ RPEEMTTDRR AYKIDRNNPG SDLAGETAAA
MAAASIVFRR SDPSYSAELL RHAHQLFEFA DKYRGKYDSS ITVAQKYYRS VSGYNDELLW
AAAWLYQATN DKYYLDYLGK NGDSMGGTGW SMTEFGWDVK YAGVQTLVAK VLMQGKGGEH
TAVFERYQQK AEQFMCSLLG KSTKNIKKTP GGLIFRQSWN NMQFVTSASF LATVYSDYLS
YSKRDLLCSQ GNISPSQLLE FSKSQVDYIL GDNPRATSYM VGYGENYPRQ VHHRGSSIVS
FNVDQKFVTC RGGYATWFSR KGSDPNVLTG ALVGGPDAYD NFADQRDNYE QTEPATYNNA
PLLGVLARLI SGSTGFDQLL PGVSPTPSPV IIKPAPVPQR KPTKPPAASS PSPITISQKM
TNSWKNEGKV YYRYSTILTN RSTKTLKILK ISITKLYGPI WGVTKTGNSF SFPSWMQSLP
SGKSMEFVYI HSASPADVLV SNYSLE
