Xyloglucan endotransglucosylase/hydrolase protein 22 precursor

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Q38857 (XTH22_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Xyloglucan endotransglucosylase/hydrolase protein 22
Short name=At-XTH22
Short name=XTH-22
EC=2.4.1.207

Alternative name(s):
Touch protein 4

Gene names

Name:	XTH22
Synonyms:	TCH4
Ordered Locus Names:	At5g57560
ORF Names:	MUA2.13

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	284 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Its induction in case of mechanical stress, suggests that it may contribute in the adaptive changes in morphogenesis by being recruited to alter tissues tensil strength, or flexibility, enabling adaptation to mechanically stressful environments. Ref.1
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. Ref.10
Subcellular location	Secreted › cell wall Probable. Secreted › extracellular space › apoplast Probable.
Tissue specificity	Highly expressed. Predominantly expressed in green siliques. Expressed in young expanding leaves, trichomes, lateral root primordia, vascular tissue, abscission zones and elongating hypocols. Following wind stimulation, it decreases in the leaves of wind-stimulated plants, while it strongly increases in sites around cells of the pith parenchyma, between the vascular elements, and within the epidermis. Ref.1 Ref.8 Ref.11
Induction	In response to mechanical perturbations such as wind or touch. Induced by auxin and brassinolide. Ref.1 Ref.2 Ref.7 Ref.11
Post-translational modification	Contains at least one intrachain disulfide bond essential for its enzymatic activity. N-glycosylated; essential for its enzymatic activity. Ref.9 Ref.10
Sequence similarities	Belongs to the glycosyl hydrolase 16 family. XTH group 2 subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 6.0-6.5. Temperature dependence: Optimum temperature from 12 to 18 degrees Celsius. Cold tolerant.

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 plant-type cell wall organization Traceable author statement Ref.8. Source: TAIR response to auxin stimulus Inferred from expression pattern Ref.1. Source: TAIR response to brassinosteroid stimulus Inferred from expression pattern Ref.1. Source: TAIR response to cold Inferred from expression pattern PubMed 16214899 PubMed 8756505. Source: TAIR response to heat Inferred from expression pattern PubMed 2302732. Source: TAIR response to mechanical stimulus Inferred from expression pattern Ref.8. Source: TAIR
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 22430844. Source: TAIR apoplast Inferred from electronic annotation. Source: UniProtKB-SubCell cell wall Inferred from direct assay Ref.8. Source: TAIR
Molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro xyloglucan:xyloglucosyl transferase activity Inferred from direct assay Ref.10. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Potential

Chain

22 – 284

263

Xyloglucan endotransglucosylase/hydrolase protein 22

PRO_0000011822

Sites

Active site

Nucleophile By similarity

Active site

101

Proton donor By similarity

Amino acid modifications

Glycosylation

105

N-linked (GlcNAc...) Potential

Glycosylation

230

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

E → D: Induces mislocalization. Ref.9

Mutagenesis

E → Q: Loss of function. Ref.9

Sequences

Sequence

Length

Mass (Da)

Tools

Q38857 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E5FCAA8C673530F7
Show »

FASTA

284

32,093

        10         20         30         40         50         60 
MAITYLLPLF LSLIITSSVS ANFQRDVEIT WGDGRGQIKN NGELLTLSLD KSSGSGFQSK 

        70         80         90        100        110        120 
NEYLFGKVSM QMKLVPGNSA GTVTTLYLKS PGTTWDEIDF EFLGNSSGEP YTLHTNVYTQ 

       130        140        150        160        170        180 
GKGDKEQQFK LWFDPTANFH TYTILWNPQR IIFTVDGTPI REFKNMESLG TLFPKNKPMR 

       190        200        210        220        230        240 
MYSSLWNADD WATRGGLVKT DWSKAPFTAS YRGFQQEACV WSNGKSSCPN ASKQGTTTGS 

       250        260        270        280 
WLSQELDSTA QQRMRWVQRN YMIYNYCTDA KRFPQGLPKE CLAA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis TCH4, regulated by hormones and the environment, encodes a xyloglucan endotransglycosylase." Xu W., Purugganan M.M., Polisensky D.H., Antosiewicz D.M., Fry S.C., Braam J. Plant Cell 7:1555-1567(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION. Strain: cv. Columbia.
[2]	"The Arabidopsis XET-related gene family: environmental and hormonal regulation of expression." Xu W., Campbell P., Vargheese A.K., Braam J. Plant J. 9:879-889(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. Strain: cv. Columbia.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones." Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S. DNA Res. 5:131-145(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves and guard cells." Stracke R., Palme K. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-121.
[7]	"The Arabidopsis TCH4 xyloglucan endotransglycosylase. Substrate specificity, pH optimum, and cold tolerance." Purugganan M.M., Braam J., Fry S.C. Plant Physiol. 115:181-190(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[8]	"Cellular localization of Arabidopsis xyloglucan endotransglycosylase-related proteins during development and after wind stimulation." Antosiewicz D.M., Purugganan M.M., Polisensky D.H., Braam J. Plant Physiol. 115:1319-1328(1997) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Co- and/or post-translational modifications are critical for TCH4 XET activity." Campbell P., Braam J. Plant J. 15:553-561(1998) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION, DISULFIDE BOND, MUTAGENESIS OF GLU-97.
[10]	"In vitro activities of four xyloglucan endotransglycosylases from Arabidopsis." Campbell P., Braam J. Plant J. 18:371-382(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME ACTIVITY, GLYCOSYLATION.
[11]	"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." Yokoyama R., Nishitani K. Plant Cell Physiol. 42:1025-1033(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[12]	"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	U27609 Genomic DNA. Translation: AAA92363.1. AF051338 mRNA. Translation: AAC05572.1. AB011482 Genomic DNA. Translation: BAB08791.1. CP002688 Genomic DNA. Translation: AED96915.1. AF367262 mRNA. Translation: AAK56251.1. AF446881 mRNA. Translation: AAL38614.1. AY052712 mRNA. Translation: AAK96616.1. AY055102 mRNA. Translation: AAL05902.1. AF083792 mRNA. Translation: AAN60350.1.
IPI	IPI00544337.
PIR	T52097.
RefSeq	NP_200564.1. NM_125137.3.
UniGene	At.24429.
3D structure databases
ProteinModelPortal	Q38857.
SMR	Q38857. Positions 19-281.
ModBase	Search...
Protein-protein interaction databases
STRING	3702.AT5G57560.1-P.
Protein family/group databases
CAZy	GH16. Glycoside Hydrolase Family 16.
Proteomic databases
PaxDb	Q38857.
PRIDE	Q38857.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G57560.1; AT5G57560.1; AT5G57560.
GeneID	835860.
KEGG	ath:AT5G57560.
Organism-specific databases
GeneFarm	2641. 265.
TAIR	At5g57560.
Phylogenomic databases
eggNOG	COG2273.
HOGENOM	HOG000236368.
InParanoid	Q38857.
KO	K14504.
OMA	CPNASKQ.
PhylomeDB	Q38857.
ProtClustDB	CLSN2685867.
Gene expression databases
Genevestigator	Q38857.
GermOnline	AT5G57560. Arabidopsis thaliana.
Family and domain databases
Gene3D	2.60.120.200. 1 hit.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR000757. Glyco_hydro_16. IPR008263. Glycoside_hydrolase_16_AS. 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.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS01034. GLYCOSYL_HYDROL_F16. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XTH22_ARATH

Accession

Primary (citable) accession number: Q38857
Secondary accession number(s): Q8H783

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2003
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents