Xylanase inhibitor protein 1 precursor - Triticum aestivum (Wheat)

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Q8L5C6 (XIP1_WHEAT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 51. 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·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Xylanase inhibitor protein 1
Short name=XIP-1
Short name=XIP-I

Alternative name(s):
Class III chitinase homolog

Gene names

Name:

XIPI

Organism

Triticum aestivum (Wheat)

Taxonomic identifier

4565 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Triticum

Protein attributes

Sequence length	304 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	Fungal xylanase inhibitor. Possesses competitive inhibiting activity against fungal endo-1,4-beta-D-xylanases belonging to glycoside hydrolase family 10 (GH10) and family 11 (GH11). Possesses also inhibitory activity towards barley alpha-amylases. Binding to xylanases or amylases is necessary for inhibition activity. May function in plant defense against secreted fungal pathogen xylanases. Is similar to class III chitinases, but does not exhibit chitinase activity. Ref.1 Ref.2 Ref.3 Ref.4
Subunit structure	Binds to fungal GH10 and GH11 xylanases. Forms also a ternary complex with barley alpha-amylase 1 (AMY1) and insoluble starch. Ref.3 Ref.4
Subcellular location	Secreted Potential.
Developmental stage	Expressed in immature embryos 3 weeks after pollination, in roots and shoots of 3 day and 5 day old seedlings, and in roots of 10 day old seedlings. Ref.5
Induction	By wounding, methyl jasmonate, and by E.graminis infection in leaves. Ref.5
Sequence similarities	Belongs to the glycosyl hydrolase 18 family. Xylanase inhibitor subfamily.

Ontologies

Keywords
Biological process	Plant defense
Cellular component	Secreted
Domain	Signal
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro defense response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

Ref.1 Ref.2

Chain

31 – 304

274

Xylanase inhibitor protein 1

PRO_0000011990

Regions

Region

178 – 184

Interaction with fungal GH11 xylanase

Region

262 – 275

Interaction with fungal GH10 xylanase

Amino acid modifications

Glycosylation

119

N-linked (GlcNAc...)

Glycosylation

295

N-linked (GlcNAc...)

Disulfide bond

55 ↔ 96

Disulfide bond

194 ↔ 225

Experimental info

Sequence conflict

F → L in CAD19479. Ref.1

Sequence conflict

214

V → A in CAD19479. Ref.1

Secondary structure

304

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q8L5C6 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: FA0FEF12FE853E30
Show »

FASTA

304

33,275

        10         20         30         40         50         60 
MAPLAARRPA CLLALLSVAA ALFLTPTALA AGGKTGQVTV FWGRNKAEGS LREACDSGMY 

        70         80         90        100        110        120 
TMVTMSFLDV FGANGKYHLD LSGHDLSSVG ADIKHCQSKG VPVSLSIGGY GTGYSLPSNR 

       130        140        150        160        170        180 
SALDLFDHLW NSYFGGSKPS VPRPFGDAWL DGVDLFLEHG TPADRYDVLA LELAKHNIRG 

       190        200        210        220        230        240 
GPGKPLHLTA TVRCGYPPAA HVGRALATGI FERVHVRTYE SDKWCNQNLG WEGSWDKWTA 

       250        260        270        280        290        300 
AYPATRFYVG LTADDKSHQW VHPKNVYYGV APVAQKKDNY GGIMLWDRYF DKQTNYSSLI 


KYYA

« Hide

References

[1]	"Functional identification of the cDNA coding for a wheat endo-1,4-beta-D-xylanase inhibitor." Elliott G.O., Hughes R.K., Juge N., Kroon P.A., Williamson G. FEBS Lett. 519:66-70(2002) [PubMed: 12023019] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-80; 180-193; 247-264 AND 265-276, FUNCTION. Strain: cv. Chinese Spring. Tissue: Pericarp and Testa.
[2]	"A novel class of protein from wheat which inhibits xylanases." McLauchlan W.R., Garcia-Conesa M.T., Williamson G., Roza M., Ravestein P., Maat J. Biochem. J. 338:441-446(1999) [PubMed: 10024521] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-45, FUNCTION.
[3]	"Interactions defining the specificity between fungal xylanases and the xylanase-inhibiting protein XIP-I from wheat." Flatman R., McLauchlan W.R., Juge N., Furniss C., Berrin J.-G., Hughes R.K., Manzanares P., Ladbury J.E., O'Brien R., Williamson G. Biochem. J. 365:773-781(2002) [PubMed: 11955286] [Abstract] Cited for: FUNCTION, INTERACTION WITH FUNGAL XYLANASES.
[4]	"Cross-inhibitory activity of cereal protein inhibitors against alpha-amylases and xylanases." Sancho A.I., Faulds C.B., Svensson B., Bartolome B., Williamson G., Juge N. Biochim. Biophys. Acta 1650:136-144(2003) [PubMed: 12922177] [Abstract] Cited for: FUNCTION, INTERACTION WITH AMY1.
[5]	"A wheat xylanase inhibitor gene, Xip-I, but not Taxi-I, is significantly induced by biotic and abiotic signals that trigger plant defense." Igawa T., Tokai T., Kudo T., Yamaguchi I., Kimura M. Biosci. Biotechnol. Biochem. 69:1058-1063(2005) [PubMed: 15914935] [Abstract] Cited for: DEVELOPMENTAL STAGE, INDUCTION.
[6]	"Structural analysis of xylanase inhibitor protein I (XIP-I), a proteinaceous xylanase inhibitor from wheat (Triticum aestivum, var. Soisson)." Payan F., Flatman R., Porciero S., Williamson G., Juge N., Roussel A. Biochem. J. 372:399-405(2003) [PubMed: 12617724] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[7]	"The dual nature of the wheat xylanase protein inhibitor XIP-I: structural basis for the inhibition of family 10 and family 11 xylanases." Payan F., Leone P., Porciero S., Furniss C., Tahir T., Williamson G., Durand A., Manzanares P., Gilbert H.J., Juge N., Roussel A. J. Biol. Chem. 279:36029-36037(2004) [PubMed: 15181003] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FUNGAL XYLANASES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ422119 mRNA. Translation: CAD19479.1.

UniGene

Ta.38246.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OM0	X-ray	1.80	A	31-304	[»]
1TA3	X-ray	1.70	A	31-304	[»]
1TE1	X-ray	2.50	A	31-304	[»]

ProteinModelPortal

Q8L5C6.

SMR

Q8L5C6. Positions 31-304.

ModBase

Search...

Protein family/group databases

Allergome

9596. Tri a XI.

CAZy

GH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

Gramene

Q8L5C6.

Family and domain databases

InterPro

IPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS01095. CHITINASE_18. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

XIP1_WHEAT

Accession

Primary (citable) accession number: Q8L5C6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	August 16, 2005
Last modified:	October 19, 2011
This is version 51 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Organism-specific databases

Family and domain databases

Entry information

Relevant documents