ID Q8H0K8_WHEAT Unreviewed; 402 AA.
AC Q8H0K8;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 121.
DE SubName: Full=Xylanase inhibitor {ECO:0000313|EMBL:BAD72880.1, ECO:0000313|EMBL:CAD27730.1, ECO:0000313|EnsemblPlants:TraesCS3B02G514800.1.cds1};
DE Flags: Precursor;
GN Name=xiI {ECO:0000313|EMBL:CAD27730.1};
GN Synonyms=taxi-I {ECO:0000313|EMBL:BAD72880.1};
GN ORFNames=TRAES_3BF012400030CFD_c1 {ECO:0000313|EMBL:CDM85049.1};
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 {ECO:0000313|EMBL:CAD27730.1};
RN [1] {ECO:0000313|EMBL:CAD27730.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12681519; DOI=10.1016/S0014-5793(03)00276-X;
RA Fierens K., Brijs K., Courtin C.M., Gebruers K., Goesaert H.,
RA Raedschelders G., Robben J., Van Campenhout S., Volckaert G., Delcour J.A.;
RT "Molecular identification of wheat endoxylanase inhibitor TAXI-I1, member
RT of a new class of plant proteins.";
RL FEBS Lett. 540:259-263(2003).
RN [2] {ECO:0007829|PDB:1T6E, ECO:0007829|PDB:1T6G}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 22-402, AND DISULFIDE BONDS.
RX PubMed=15166216; DOI=10.1074/jbc.M404212200;
RA Sansen S., De Ranter C.J., Gebruers K., Brijs K., Courtin C.M.,
RA Delcour J.A., Rabijns A.;
RT "Structural basis for inhibition of Aspergillus niger xylanase by triticum
RT aestivum xylanase inhibitor-I.";
RL J. Biol. Chem. 279:36022-36028(2004).
RN [3] {ECO:0000313|EMBL:BAD72880.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15564518; DOI=10.1093/pcp/pch195;
RA Igawa T., Ochiai-Fukuda T., Takahashi-Ando N., Ohsato S., Shibata T.,
RA Yamaguchi I., Kimura M.;
RT "New TAXI-type xylanase inhibitor genes are inducible by pathogens and
RT wounding in hexaploid wheat.";
RL Plant Cell Physiol. 45:1347-1360(2004).
RN [4] {ECO:0007829|PDB:2B42}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 22-402, AND DISULFIDE BONDS.
RX PubMed=19769747; DOI=10.1111/j.1742-4658.2009.07105.x;
RA Pollet A., Sansen S., Raedschelders G., Gebruers K., Rabijns A.,
RA Delcour J.A., Courtin C.M.;
RT "Identification of structural determinants for inhibition strength and
RT specificity of wheat xylanase inhibitors TAXI-IA and TAXI-IIA.";
RL FEBS J. 276:3916-3927(2009).
RN [5] {ECO:0000313|EMBL:CDM85049.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25035497; DOI=10.1126/science.1249721;
RA Choulet F., Alberti A., Theil S., Glover N., Barbe V., Daron J.,
RA Pingault L., Sourdille P., Couloux A., Paux E., Leroy P., Mangenot S.,
RA Guilhot N., Le Gouis J., Balfourier F., Alaux M., Jamilloux V., Poulain J.,
RA Durand C., Bellec A., Gaspin C., Safar J., Dolezel J., Rogers J.,
RA Vandepoele K., Aury J.M., Mayer K., Berges H., Quesneville H., Wincker P.,
RA Feuillet C.;
RT "Structural and functional partitioning of bread wheat chromosome 3B.";
RL Science 345:1249721-1249721(2014).
RN [6] {ECO:0000313|EnsemblPlants:TraesCS3B02G514800.1.cds1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS3B02G514800.1.cds1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [7] {ECO:0000313|EnsemblPlants:TraesCS3B02G514800.1.cds1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; AB114626; BAD72880.1; -; mRNA.
DR EMBL; AJ438880; CAD27730.1; -; Genomic_DNA.
DR EMBL; HG670306; CDM85049.1; -; Genomic_DNA.
DR PDB; 1T6E; X-ray; 1.70 A; X=22-402.
DR PDB; 1T6G; X-ray; 1.80 A; A/B=22-402.
DR PDB; 2B42; X-ray; 2.50 A; A=22-402.
DR PDBsum; 1T6E; -.
DR PDBsum; 1T6G; -.
DR PDBsum; 2B42; -.
DR SMR; Q8H0K8; -.
DR IntAct; Q8H0K8; 1.
DR MINT; Q8H0K8; -.
DR STRING; 4565.Q8H0K8; -.
DR MEROPS; A01.974; -.
DR EnsemblPlants; TraesCS3B02G514800.1; TraesCS3B02G514800.1.cds1; TraesCS3B02G514800.
DR Gramene; TraesCAD_scaffold_007879_01G000200.1; TraesCAD_scaffold_007879_01G000200.1; TraesCAD_scaffold_007879_01G000200.
DR Gramene; TraesCLE_scaffold_032072_01G000300.1; TraesCLE_scaffold_032072_01G000300.1; TraesCLE_scaffold_032072_01G000300.
DR Gramene; TraesCS3B02G514800.1; TraesCS3B02G514800.1.cds1; TraesCS3B02G514800.
DR Gramene; TraesCS3B03G1276900.1; TraesCS3B03G1276900.1.CDS1; TraesCS3B03G1276900.
DR Gramene; TraesPAR_scaffold_021097_01G000200.1; TraesPAR_scaffold_021097_01G000200.1; TraesPAR_scaffold_021097_01G000200.
DR Gramene; TraesROB_scaffold_059328_01G000200.1; TraesROB_scaffold_059328_01G000200.1; TraesROB_scaffold_059328_01G000200.
DR Gramene; TraesWEE_scaffold_018558_01G000300.1; TraesWEE_scaffold_018558_01G000300.1; TraesWEE_scaffold_018558_01G000300.
DR HOGENOM; CLU_032185_1_0_1; -.
DR OMA; KQGTACV; -.
DR OrthoDB; 1213461at2759; -.
DR Proteomes; UP000019116; Chromosome 3B.
DR ExpressionAtlas; Q8H0K8; baseline and differential.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd05489; xylanase_inhibitor_I_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR InterPro; IPR033868; Xylanase_inhibitor_I-like.
DR PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR PANTHER; PTHR47965:SF35; XYLANASE INHIBITOR; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:1T6E, ECO:0007829|PDB:1T6G};
KW Carbohydrate metabolism {ECO:0000313|EMBL:CAD27730.1};
KW Glycosidase {ECO:0000313|EMBL:CAD27730.1};
KW Hydrolase {ECO:0000313|EMBL:CAD27730.1};
KW Polysaccharide degradation {ECO:0000313|EMBL:CAD27730.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000313|EMBL:CAD27730.1}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..402
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010509549"
FT DOMAIN 33..391
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DISULFID 60..145
FT /evidence="ECO:0007829|PDB:1T6E, ECO:0007829|PDB:1T6G"
FT DISULFID 71..92
FT /evidence="ECO:0007829|PDB:1T6E"
FT DISULFID 76..101
FT /evidence="ECO:0007829|PDB:1T6E, ECO:0007829|PDB:1T6G"
FT DISULFID 87..113
FT /evidence="ECO:0007829|PDB:1T6E, ECO:0007829|PDB:1T6G"
FT DISULFID 188..399
FT /evidence="ECO:0007829|PDB:1T6E, ECO:0007829|PDB:1T6G"
FT DISULFID 303..348
FT /evidence="ECO:0007829|PDB:1T6E, ECO:0007829|PDB:1T6G"
SQ SEQUENCE 402 AA; 40934 MW; 0DB5894716737BFB CRC64;
MPPVLLLVLA ASLVALPSCQ SLPVLAPVTK DPATSLYTIP FHDGASLVLD VAGPLVWSTC
DGGQPPAEIP CSSPTCLLAN AYPAPGCPAP SCGSDKHDKP CTAYPYNPVS GACAAGSLSH
TRFVANTTDG SKPVSKVNVG VLAACAPSKL LASLPRGSTG VAGLANSGLA LPAQVASAQK
VANRFLLCLP TGGPGVAIFG GGPVPWPQFT QSMPYTPLVT KGGSPAHYIS ARSIVVGDTR
VPVPEGALAT GGVMLSTRLP YVLLRPDVYR PLMDAFTKAL AAQHANGAPV ARAVEAVAPF
GVCYDTKTLG NNLGGYAVPN VQLGLDGGSD WTMTGKNSMV DVKQGTACVA FVEMKGVAAG
DGRAPAVILG GAQMEDFVLD FDMEKKRLGF SRLPHFTGCG GL
//