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Database: UniProt
Entry: Q8H0K8
LinkDB: Q8H0K8
Original site: Q8H0K8 
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
//
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