XIP1_WHEAT
ID XIP1_WHEAT Reviewed; 304 AA.
AC Q8L5C6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Xylanase inhibitor protein 1 {ECO:0000303|PubMed:12023019};
DE Short=XIP-1 {ECO:0000303|PubMed:12023019};
DE Short=XIP-I {ECO:0000303|PubMed:12023019};
DE AltName: Full=Class III chitinase homolog {ECO:0000305};
DE Flags: Precursor;
GN Name=XIPI {ECO:0000303|PubMed:12023019};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-80; 180-193; 247-264 AND
RP 265-276, AND FUNCTION.
RC STRAIN=cv. Chinese Spring; TISSUE=Pericarp, and Testa;
RX PubMed=12023019; DOI=10.1016/s0014-5793(02)02710-2;
RA Elliott G.O., Hughes R.K., Juge N., Kroon P.A., Williamson G.;
RT "Functional identification of the cDNA coding for a wheat endo-1,4-beta-D-
RT xylanase inhibitor.";
RL FEBS Lett. 519:66-70(2002).
RN [2]
RP PROTEIN SEQUENCE OF 31-45, AND FUNCTION.
RX PubMed=10024521; DOI=10.1042/bj3380441;
RA McLauchlan W.R., Garcia-Conesa M.T., Williamson G., Roza M., Ravestein P.,
RA Maat J.;
RT "A novel class of protein from wheat which inhibits xylanases.";
RL Biochem. J. 338:441-446(1999).
RN [3]
RP FUNCTION, AND INTERACTION WITH FUNGAL XYLANASES.
RX PubMed=11955286; DOI=10.1042/bj20020168;
RA Flatman R., McLauchlan W.R., Juge N., Furniss C., Berrin J.-G.,
RA Hughes R.K., Manzanares P., Ladbury J.E., O'Brien R., Williamson G.;
RT "Interactions defining the specificity between fungal xylanases and the
RT xylanase-inhibiting protein XIP-I from wheat.";
RL Biochem. J. 365:773-781(2002).
RN [4]
RP FUNCTION, AND INTERACTION WITH AMY1.
RX PubMed=12922177; DOI=10.1016/s1570-9639(03)00209-7;
RA Sancho A.I., Faulds C.B., Svensson B., Bartolome B., Williamson G.,
RA Juge N.;
RT "Cross-inhibitory activity of cereal protein inhibitors against alpha-
RT amylases and xylanases.";
RL Biochim. Biophys. Acta 1650:136-144(2003).
RN [5]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=15914935; DOI=10.1271/bbb.69.1058;
RA Igawa T., Tokai T., Kudo T., Yamaguchi I., Kimura M.;
RT "A wheat xylanase inhibitor gene, Xip-I, but not Taxi-I, is significantly
RT induced by biotic and abiotic signals that trigger plant defense.";
RL Biosci. Biotechnol. Biochem. 69:1058-1063(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 31-304.
RX PubMed=12617724; DOI=10.1042/bj20021802;
RA Payan F., Flatman R., Porciero S., Williamson G., Juge N., Roussel A.;
RT "Structural analysis of xylanase inhibitor protein I (XIP-I), a
RT proteinaceous xylanase inhibitor from wheat (Triticum aestivum, var.
RT Soisson).";
RL Biochem. J. 372:399-405(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 31-304 IN COMPLEX WITH FUNGAL
RP XYLANASES, GLYCOSYLATION AT ASN-119 AND ASN-295, AND DISULFIDE BONDS.
RX PubMed=15181003; DOI=10.1074/jbc.m404225200;
RA Payan F., Leone P., Porciero S., Furniss C., Tahir T., Williamson G.,
RA Durand A., Manzanares P., Gilbert H.J., Juge N., Roussel A.;
RT "The dual nature of the wheat xylanase protein inhibitor XIP-I: structural
RT basis for the inhibition of family 10 and family 11 xylanases.";
RL J. Biol. Chem. 279:36029-36037(2004).
CC -!- FUNCTION: Fungal xylanase inhibitor. Possesses competitive inhibiting
CC activity against fungal endo-1,4-beta-D-xylanases belonging to
CC glycoside hydrolase family 10 (GH10) and family 11 (GH11). Possesses
CC also inhibitory activity towards barley alpha-amylases. Binding to
CC xylanases or amylases is necessary for inhibition activity. May
CC function in plant defense against secreted fungal pathogen xylanases.
CC Is similar to class III chitinases, but does not exhibit chitinase
CC activity. {ECO:0000269|PubMed:10024521, ECO:0000269|PubMed:11955286,
CC ECO:0000269|PubMed:12023019, ECO:0000269|PubMed:12922177}.
CC -!- SUBUNIT: Binds to fungal GH10 and GH11 xylanases. Forms also a ternary
CC complex with barley alpha-amylase 1 (AMY1) and insoluble starch.
CC {ECO:0000269|PubMed:15181003}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in immature embryos 3 weeks after
CC pollination, in roots and shoots of 3 day and 5 day old seedlings, and
CC in roots of 10 day old seedlings. {ECO:0000269|PubMed:15914935}.
CC -!- INDUCTION: By wounding, methyl jasmonate, and by E.graminis infection
CC in leaves. {ECO:0000269|PubMed:15914935}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Xylanase
CC inhibitor subfamily. {ECO:0000305}.
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DR EMBL; AJ422119; CAD19479.1; -; mRNA.
DR PDB; 1OM0; X-ray; 1.80 A; A=31-304.
DR PDB; 1TA3; X-ray; 1.70 A; A=31-304.
DR PDB; 1TE1; X-ray; 2.50 A; A=31-304.
DR PDBsum; 1OM0; -.
DR PDBsum; 1TA3; -.
DR PDBsum; 1TE1; -.
DR AlphaFoldDB; Q8L5C6; -.
DR SMR; Q8L5C6; -.
DR STRING; 4565.Traes_4DS_F33F58A71.1; -.
DR Allergome; 9596; Tri a XI.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR iPTMnet; Q8L5C6; -.
DR PRIDE; Q8L5C6; -.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_007818_0_0_1; -.
DR EvolutionaryTrace; Q8L5C6; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; Q8L5C6; baseline and differential.
DR Genevisible; Q8L5C6; TA.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosidase; Hydrolase; Plant defense; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:10024521,
FT ECO:0000269|PubMed:12023019"
FT CHAIN 31..304
FT /note="Xylanase inhibitor protein 1"
FT /id="PRO_0000011990"
FT DOMAIN 36..304
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 178..184
FT /note="Interaction with fungal GH11 xylanase"
FT /evidence="ECO:0000269|PubMed:15181003"
FT REGION 262..275
FT /note="Interaction with fungal GH10 xylanase"
FT /evidence="ECO:0000269|PubMed:15181003"
FT ACT_SITE 158
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:15181003, ECO:0007744|PDB:1TE1"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:15181003, ECO:0007744|PDB:1TE1"
FT DISULFID 55..96
FT /evidence="ECO:0000269|PubMed:15181003,
FT ECO:0007744|PDB:1TE1"
FT DISULFID 194..225
FT /evidence="ECO:0000269|PubMed:15181003,
FT ECO:0007744|PDB:1TE1"
FT CONFLICT 67
FT /note="F -> L (in Ref. 1; CAD19479)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="V -> A (in Ref. 1; CAD19479)"
FT /evidence="ECO:0000305"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 61..75
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:1TA3"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1TA3"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:1OM0"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:1TA3"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:1TA3"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:1TA3"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:1TA3"
SQ SEQUENCE 304 AA; 33275 MW; FA0FEF12FE853E30 CRC64;
MAPLAARRPA CLLALLSVAA ALFLTPTALA AGGKTGQVTV FWGRNKAEGS LREACDSGMY
TMVTMSFLDV FGANGKYHLD LSGHDLSSVG ADIKHCQSKG VPVSLSIGGY GTGYSLPSNR
SALDLFDHLW NSYFGGSKPS VPRPFGDAWL DGVDLFLEHG TPADRYDVLA LELAKHNIRG
GPGKPLHLTA TVRCGYPPAA HVGRALATGI FERVHVRTYE SDKWCNQNLG WEGSWDKWTA
AYPATRFYVG LTADDKSHQW VHPKNVYYGV APVAQKKDNY GGIMLWDRYF DKQTNYSSLI
KYYA
