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Xyloglucan endotransglucosylase/hydrolase protein 14 (At-XTH14) (XTH-14) (EC 2.4.1.207)

 XTH14_ARATH             Reviewed;         287 AA.
Q9ZSU4;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-APR-2018, entry version 131.
RecName: Full=Xyloglucan endotransglucosylase/hydrolase protein 14 {ECO:0000303|PubMed:12514239};
Short=At-XTH14 {ECO:0000303|PubMed:12514239};
Short=XTH-14 {ECO:0000303|PubMed:12514239};
EC=2.4.1.207 {ECO:0000269|PubMed:10406121};
Flags: Precursor;
Name=XTH14 {ECO:0000303|PubMed:12514239};
Synonyms=XTR9 {ECO:0000303|PubMed:10406121};
OrderedLocusNames=At4g25820 {ECO:0000312|Araport:AT4G25820};
ORFNames=F14M19.100 {ECO:0000312|EMBL:CAB39603.1};
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], FUNCTION, ENZYME ACTIVITY, AND
GLYCOSYLATION.
PubMed=10406121; DOI=10.1046/j.1365-313X.1999.00459.x;
Campbell P., Braam J.;
"In vitro activities of four xyloglucan endotransglycosylases from
Arabidopsis.";
Plant J. 18:371-382(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
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).
[5]
TISSUE SPECIFICITY.
PubMed=11673616; DOI=10.1093/pcp/pce154;
Yokoyama R., Nishitani K.;
"A comprehensive expression analysis of all members of a gene family
encoding cell-wall enzymes allowed us to predict cis-regulatory
regions involved in cell-wall construction in specific organs of
Arabidopsis.";
Plant Cell Physiol. 42:1025-1033(2001).
[6]
NOMENCLATURE.
PubMed=12514239; DOI=10.1093/pcp/pcf171;
Rose J.K.C., Braam J., Fry S.C., Nishitani K.;
"The XTH family of enzymes involved in xyloglucan
endotransglucosylation and endohydrolysis: current perspectives and a
new unifying nomenclature.";
Plant Cell Physiol. 43:1421-1435(2002).
[7]
INDUCTION BY ALUMINUM.
PubMed=21285327; DOI=10.1104/pp.111.172221;
Yang J.L., Zhu X.F., Peng Y.X., Zheng C., Li G.X., Liu Y., Shi Y.Z.,
Zheng S.J.;
"Cell wall hemicellulose contributes significantly to aluminum
adsorption and root growth in Arabidopsis.";
Plant Physiol. 155:1885-1892(2011).
-!- FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or
endotransglycosylation (XET). Cleaves and religates xyloglucan
polymers, an essential constituent of the primary cell wall, and
thereby participates in cell wall construction of growing tissues.
Has some preference for non-fucosylated xyloglucan polymer. No
apparent XEH activity in vitro. {ECO:0000269|PubMed:10406121}.
-!- CATALYTIC ACTIVITY: Breaks a beta-(1->4) bond in the backbone of a
xyloglucan and transfers the xyloglucanyl segment on to O-4 of the
non-reducing terminal glucose residue of an acceptor, which can be
a xyloglucan or an oligosaccharide of xyloglucan.
{ECO:0000269|PubMed:10406121}.
-!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}. Secreted,
extracellular space, apoplast {ECO:0000305}.
-!- TISSUE SPECIFICITY: Root specific. {ECO:0000269|PubMed:11673616}.
-!- INDUCTION: Down-regulated by aluminum.
{ECO:0000269|PubMed:21285327}.
-!- PTM: Contains at least one intrachain disulfide bond essential for
its enzymatic activity. {ECO:0000250}.
-!- PTM: N-glycosylated; not essential for its enzymatic activity.
{ECO:0000269|PubMed:10406121}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group
2 subfamily. {ECO:0000305}.
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EMBL; AF093672; AAD12249.1; -; mRNA.
EMBL; AL049480; CAB39603.1; -; Genomic_DNA.
EMBL; AL161564; CAB79437.1; -; Genomic_DNA.
EMBL; CP002687; AEE85118.1; -; Genomic_DNA.
EMBL; AY093183; AAM13182.1; -; mRNA.
EMBL; BT003385; AAO30048.1; -; mRNA.
PIR; T04236; T04236.
RefSeq; NP_194312.1; NM_118714.4.
UniGene; At.2902; -.
ProteinModelPortal; Q9ZSU4; -.
SMR; Q9ZSU4; -.
STRING; 3702.AT4G25820.1; -.
CAZy; GH16; Glycoside Hydrolase Family 16.
iPTMnet; Q9ZSU4; -.
PaxDb; Q9ZSU4; -.
EnsemblPlants; AT4G25820.1; AT4G25820.1; AT4G25820.
GeneID; 828687; -.
Gramene; AT4G25820.1; AT4G25820.1; AT4G25820.
KEGG; ath:AT4G25820; -.
Araport; AT4G25820; -.
TAIR; locus:2117492; AT4G25820.
eggNOG; ENOG410IFD4; Eukaryota.
eggNOG; COG2273; LUCA.
HOGENOM; HOG000236368; -.
InParanoid; Q9ZSU4; -.
KO; K08235; -.
OMA; ANIFENG; -.
OrthoDB; EOG093614S5; -.
PhylomeDB; Q9ZSU4; -.
BioCyc; ARA:AT4G25820-MONOMER; -.
BRENDA; 2.4.1.207; 399.
PRO; PR:Q9ZSU4; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9ZSU4; baseline and differential.
Genevisible; Q9ZSU4; AT.
GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
GO; GO:0016762; F:xyloglucan:xyloglucosyl transferase activity; IEA:UniProtKB-EC.
GO; GO:0042546; P:cell wall biogenesis; IEA:InterPro.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0010411; P:xyloglucan metabolic process; IEA:InterPro.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR000757; GH16.
InterPro; IPR008263; GH16_AS.
InterPro; IPR010713; XET_C.
InterPro; IPR016455; XTH.
Pfam; PF00722; Glyco_hydro_16; 1.
Pfam; PF06955; XET_C; 1.
PIRSF; PIRSF005604; XET; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS01034; GH16_1; 1.
PROSITE; PS51762; GH16_2; 1.
1: Evidence at protein level;
Apoplast; Cell wall; Cell wall biogenesis/degradation;
Complete proteome; Disulfide bond; Glycoprotein; Glycosidase;
Hydrolase; Reference proteome; Secreted; Signal; Transferase.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 287 Xyloglucan endotransglucosylase/hydrolase
protein 14.
/FTId=PRO_0000011814.
DOMAIN 28 218 GH16. {ECO:0000255|PROSITE-
ProRule:PRU01098}.
ACT_SITE 104 104 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10064}.
ACT_SITE 108 108 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU10064}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:10406121}.
SEQUENCE 287 AA; 32740 MW; 42D596152C85848D CRC64;
MACFATKQPL LLSLLLAIGF FVVAASAGNF YESFDITWGN GRANIFENGQ LLTCTLDKVS
GSGFQSKKEY LFGKIDMKLK LVAGNSAGTV TAYYLSSKGT AWDEIDFEFL GNRTGHPYTI
HTNVFTGGKG DREMQFRLWF DPTADFHTYT VHWNPVNIIF LVDGIPIRVF KNNEKNGVAY
PKNQPMRIYS SLWEADDWAT EGGRVKIDWS NAPFKASYRN FNDQSSCSRT SSSKWVTCEP
NSNSWMWTTL NPAQYGKMMW VQRDFMIYNY CTDFKRFPQG LPKECKL


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