位置:首页 > 蛋白库 > E137_ARATH
E137_ARATH
ID   E137_ARATH              Reviewed;         504 AA.
AC   Q9M069; O65675; P80829;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase 7;
DE            EC=3.2.1.39;
DE   AltName: Full=(1->3)-beta-glucan endohydrolase 7;
DE            Short=(1->3)-beta-glucanase 7;
DE   AltName: Full=Beta-1,3-endoglucanase 7;
DE            Short=Beta-1,3-glucanase 7;
DE   Flags: Precursor;
GN   OrderedLocusNames=At4g34480; ORFNames=T4L20.60;
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] {ECO:0000305, ECO:0000312|EMBL:CAB80165.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000269|PubMed:10617198};
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] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 23-38, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=9188482; DOI=10.1074/jbc.272.25.15841;
RA   Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P.,
RA   Slabas A.R.;
RT   "Differential extraction and protein sequencing reveals major differences
RT   in patterns of primary cell wall proteins from plants.";
RL   J. Biol. Chem. 272:15841-15848(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9188482}. Secreted,
CC       cell wall {ECO:0000269|PubMed:9188482}.
CC   -!- PTM: Contains two additional disulfide bonds. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA18827.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80165.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL023094; CAA18827.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161585; CAB80165.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86384.1; -; Genomic_DNA.
DR   PIR; D85406; D85406.
DR   PIR; T05268; T05268.
DR   RefSeq; NP_001328502.1; NM_001342285.1.
DR   RefSeq; NP_195174.6; NM_119613.8.
DR   AlphaFoldDB; Q9M069; -.
DR   SMR; Q9M069; -.
DR   STRING; 3702.AT4G34480.1; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   PaxDb; Q9M069; -.
DR   PRIDE; Q9M069; -.
DR   ProteomicsDB; 222008; -.
DR   EnsemblPlants; AT4G34480.1; AT4G34480.1; AT4G34480.
DR   GeneID; 829599; -.
DR   Gramene; AT4G34480.1; AT4G34480.1; AT4G34480.
DR   KEGG; ath:AT4G34480; -.
DR   Araport; AT4G34480; -.
DR   TAIR; locus:2139519; AT4G34480.
DR   eggNOG; ENOG502QQY7; Eukaryota.
DR   HOGENOM; CLU_024953_1_0_1; -.
DR   InParanoid; Q9M069; -.
DR   OMA; WPTRGDA; -.
DR   OrthoDB; 966331at2759; -.
DR   PhylomeDB; Q9M069; -.
DR   BioCyc; ARA:AT4G34480-MON; -.
DR   PRO; PR:Q9M069; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9M069; baseline and differential.
DR   Genevisible; Q9M069; AT.
DR   GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR044965; Glyco_hydro_17_plant.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR012946; X8.
DR   PANTHER; PTHR32227; PTHR32227; 1.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   Pfam; PF07983; X8; 1.
DR   SMART; SM00768; X8; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW   Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:9188482"
FT   CHAIN           23..504
FT                   /note="Glucan endo-1,3-beta-glucosidase 7"
FT                   /id="PRO_0000042684"
FT   ACT_SITE        119
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        264
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   DISULFID        365..427
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   504 AA;  53121 MW;  77FF26A6AF36C167 CRC64;
     MALSISIYFL LIFLSHFPSS HAEPFIGVNY GQVADNLPPP SETVKLLQST SIQKVRLYGA
     DPAIIKALAG TGVGIVIGAA NGDVPSLASD PNAATQWINS NVLPFYPASK IMLITVGNEI
     LMSNDPNLVN QLLPAMQNVQ KALEAVSLGG KIKVSTVNSM TVLGSSDPPS SGSFAAGYQT
     GLKGILQFLS DTGSPFAINP YPFFAYQSDP RPETLAFCLF EPNAGRVDSK TGIKYTNMFD
     AQVDAVHSAL KSMGFEKVEI VVAETGWASR GDANEVGASV DNAKAYNGNL IAHLRSMVGT
     PLMPGKPVDT YIFALYDENL KPGPSSERAF GLFKTDLSMV YDVGLAKSSS SSQTPSGKVT
     SSGWCVPKKG ATNEELQASL DWACGHGIDC GAIQPGGACF EPNNVVSHAA YAMNMYFQKS
     PKQPTDCDFS KTATVTSQNP SYNNCVYPGG GGGGGGGGGG SKAVMNKYVS SDKVEKKNGA
     TEPKVSSSLS FLLIFLSLIF HVYM
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024