Q9SV61 (XTH1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative xyloglucan endotransglucosylase/hydrolase protein 1
Short name=At-XTH1
Short name=XTH-1
EC=2.4.1.207

Gene names

Name:	XTH1
Ordered Locus Names:	At4g13080
ORF Names:	F25G13.170

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	May catalyze 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 By similarity.
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.
Subcellular location	Secreted › cell wall Probable. Secreted › extracellular space › apoplast Probable.
Post-translational modification	Contains at least one intrachain disulfide bond essential for its enzymatic activity By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 16 family. XTH group 1 subfamily.
Sequence caution	The sequence CAB45507.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAB78350.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Apoplast Cell wall Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular glucan metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	apoplast Inferred from electronic annotation. Source: UniProtKB-SubCell cell wall Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro xyloglucan:xyloglucosyl transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 292	271	Putative xyloglucan endotransglucosylase/hydrolase protein 1		PRO_0000011801
Sites
	Active site	110	1	Nucleophile By similarity
	Active site	114	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	177	1	N-linked (GlcNAc...) Potential
	Glycosylation	212	1	N-linked (GlcNAc...) Potential
	Glycosylation	226	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9SV61 [UniParc]. Last modified May 31, 2011. Version 2. Checksum: B4459C51EECBB139	FASTA	292	33,247
	10 20 30 40 50 60 MEYLSIFGFV SVLYLIIRVD ARAYEVNGID QSKVGFDDNY VVTWGQNNVL KLNQGKEVQL 70 80 90 100 110 120 SLDHSSGSGF ESKNHYESGF FQIRIKVPPK DTSGVVTAFY LTSKGNTHDE VDFEFLGNKE 130 140 150 160 170 180 GKLAVQTNVF TNGKGNREQK LALWFDPSKD FHTYAILWNP YQIVLYVDNI PVRVFKNTTS 190 200 210 220 230 240 QGMNYPSKPM QVVVSLWNGE NWATDGGKSK INWSLAPFKA NFQGFNNSGC FTNAEKNACG 250 260 270 280 290 SSAYWWNTGS YSKLSDSEQK AYTNVRQKYM NYDYCSDKVR FHVPPSECKW NN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." 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. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"The XTH family of enzymes involved in xyloglucan endotransglucosylation and endohydrolysis: current perspectives and a new unifying nomenclature." Rose J.K.C., Braam J., Fry S.C., Nishitani K. Plant Cell Physiol. 43:1421-1435(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE.
+	Additional computationally mapped references.

Web resources

XTH-World

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL079349 Genomic DNA. Translation: CAB45507.1. Different initiation. AL161535 Genomic DNA. Translation: CAB78350.1. Different initiation. CP002687 Genomic DNA. Translation: AEE83228.1.
IPI	IPI00523926.
PIR	T10210.
RefSeq	NP_193044.2. NM_117377.2.
UniGene	At.54296.
3D structure databases
ProteinModelPortal	Q9SV61.
SMR	Q9SV61. Positions 34-289.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT4G13080.1-P.
Protein family/group databases
CAZy	GH16. Glycoside Hydrolase Family 16.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G13080.1; AT4G13080.1; AT4G13080.
GeneID	826922.
KEGG	ath:AT4G13080.
Organism-specific databases
TAIR	At4g13080.
Phylogenomic databases
eggNOG	COG2273.
HOGENOM	HOG000236368.
InParanoid	Q9SV61.
KO	K08235.
OMA	GSGFFHM.
Gene expression databases
Genevestigator	Q9SV61.
GermOnline	AT4G13080. Arabidopsis thaliana.
Family and domain databases
Gene3D	2.60.120.200. 1 hit.
InterPro	IPR008264. Beta_glucanase. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR000757. Glyco_hydro_16. IPR016455. XET. IPR010713. XET_C. [Graphical view]
Pfam	PF00722. Glyco_hydro_16. 1 hit. PF06955. XET_C. 1 hit. [Graphical view]
PIRSF	PIRSF005604. XET. 1 hit.
PRINTS	PR00737. GLHYDRLASE16.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS01034. GLYCOSYL_HYDROL_F16. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XTH1_ARATH

Accession

Primary (citable) accession number: Q9SV61

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	May 31, 2011
Last modified:	May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program