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Protein

Xylanase inhibitor protein 1

Gene

XIPI

Organism
Triticum aestivum (Wheat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Plant defense

Protein family/group databases

CAZyiGH18. Glycoside Hydrolase Family 18.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylanase inhibitor protein 1
Short name:
XIP-1
Short name:
XIP-I
Alternative name(s):
Class III chitinase homolog
Gene namesi
Name:XIPI
OrganismiTriticum aestivum (Wheat)
Taxonomic identifieri4565 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeTriticinaeTriticum
Proteomesi
  • UP000019116 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei9596. Tri a XI.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 30302 PublicationsAdd
BLAST
Chaini31 – 304274Xylanase inhibitor protein 1PRO_0000011990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 96
Glycosylationi119 – 1191N-linked (GlcNAc...)
Disulfide bondi194 ↔ 225
Glycosylationi295 – 2951N-linked (GlcNAc...)

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Developmental stagei

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.1 Publication

Inductioni

By wounding, methyl jasmonate, and by E.graminis infection in leaves.1 Publication

Gene expression databases

ExpressionAtlasiQ8L5C6. baseline and differential.
GenevisibleiQ8L5C6. TA.

Interactioni

Subunit structurei

Binds to fungal GH10 and GH11 xylanases. Forms also a ternary complex with barley alpha-amylase 1 (AMY1) and insoluble starch.1 Publication

Structurei

Secondary structure

1
304
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 447Combined sources
Helixi46 – 483Combined sources
Helixi51 – 566Combined sources
Beta strandi61 – 7515Combined sources
Helixi86 – 883Combined sources
Helixi89 – 9810Combined sources
Beta strandi103 – 11210Combined sources
Helixi119 – 13315Combined sources
Turni144 – 1474Combined sources
Beta strandi151 – 1599Combined sources
Helixi166 – 1749Combined sources
Beta strandi179 – 1835Combined sources
Beta strandi187 – 1926Combined sources
Beta strandi194 – 1974Combined sources
Helixi200 – 2067Combined sources
Beta strandi213 – 2175Combined sources
Turni227 – 2293Combined sources
Helixi231 – 24111Combined sources
Beta strandi245 – 2528Combined sources
Helixi263 – 2686Combined sources
Helixi270 – 2745Combined sources
Beta strandi280 – 2867Combined sources
Helixi288 – 2947Combined sources
Helixi296 – 3005Combined sources
Turni301 – 3033Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OM0X-ray1.80A31-304[»]
1TA3X-ray1.70A31-304[»]
1TE1X-ray2.50A31-304[»]
ProteinModelPortaliQ8L5C6.
SMRiQ8L5C6. Positions 31-304.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8L5C6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni178 – 1847Interaction with fungal GH11 xylanase
Regioni262 – 27514Interaction with fungal GH10 xylanaseAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

OMAiYDDADCE.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8L5C6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPLAARRPA CLLALLSVAA ALFLTPTALA AGGKTGQVTV FWGRNKAEGS
60 70 80 90 100
LREACDSGMY TMVTMSFLDV FGANGKYHLD LSGHDLSSVG ADIKHCQSKG
110 120 130 140 150
VPVSLSIGGY GTGYSLPSNR SALDLFDHLW NSYFGGSKPS VPRPFGDAWL
160 170 180 190 200
DGVDLFLEHG TPADRYDVLA LELAKHNIRG GPGKPLHLTA TVRCGYPPAA
210 220 230 240 250
HVGRALATGI FERVHVRTYE SDKWCNQNLG WEGSWDKWTA AYPATRFYVG
260 270 280 290 300
LTADDKSHQW VHPKNVYYGV APVAQKKDNY GGIMLWDRYF DKQTNYSSLI

KYYA
Length:304
Mass (Da):33,275
Last modified:August 16, 2005 - v2
Checksum:iFA0FEF12FE853E30
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671F → L in CAD19479 (PubMed:12023019).Curated
Sequence conflicti214 – 2141V → A in CAD19479 (PubMed:12023019).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ422119 mRNA. Translation: CAD19479.1.
UniGeneiTa.38246.

Genome annotation databases

EnsemblPlantsiTraes_4DS_F33F58A71.1; Traes_4DS_F33F58A71.1; Traes_4DS_F33F58A71.
GrameneiTraes_4DS_F33F58A71.1; Traes_4DS_F33F58A71.1; Traes_4DS_F33F58A71.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ422119 mRNA. Translation: CAD19479.1.
UniGeneiTa.38246.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OM0X-ray1.80A31-304[»]
1TA3X-ray1.70A31-304[»]
1TE1X-ray2.50A31-304[»]
ProteinModelPortaliQ8L5C6.
SMRiQ8L5C6. Positions 31-304.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei9596. Tri a XI.
CAZyiGH18. Glycoside Hydrolase Family 18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiTraes_4DS_F33F58A71.1; Traes_4DS_F33F58A71.1; Traes_4DS_F33F58A71.
GrameneiTraes_4DS_F33F58A71.1; Traes_4DS_F33F58A71.1; Traes_4DS_F33F58A71.

Phylogenomic databases

OMAiYDDADCE.

Miscellaneous databases

EvolutionaryTraceiQ8L5C6.

Gene expression databases

ExpressionAtlasiQ8L5C6. baseline and differential.
GenevisibleiQ8L5C6. TA.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001223. Glyco_hydro18_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FUNGAL XYLANASES.

Entry informationi

Entry nameiXIP1_WHEAT
AccessioniPrimary (citable) accession number: Q8L5C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: February 17, 2016
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.