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WIN2_SOLTU
ID   WIN2_SOLTU              Reviewed;         211 AA.
AC   P09762;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Wound-induced protein WIN2;
DE   Flags: Precursor;
GN   Name=WIN2;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Maris Piper;
RX   PubMed=2710099; DOI=10.1007/bf00339718;
RA   Stanford A., Bevan M., Northcote D.;
RT   "Differential expression within a family of novel wound-induced genes in
RT   potato.";
RL   Mol. Gen. Genet. 215:200-208(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44;
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
CC   -!- INDUCTION: By wounding.
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DR   EMBL; X13497; CAA31852.1; -; Genomic_DNA.
DR   PIR; S04927; S04927.
DR   RefSeq; NP_001275628.1; NM_001288699.1.
DR   AlphaFoldDB; P09762; -.
DR   SMR; P09762; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   EnsemblPlants; PGSC0003DMT400050018; PGSC0003DMT400050018; PGSC0003DMG400019435.
DR   EnsemblPlants; RHC01H1G3444.2.1; RHC01H1G3444.2.1; RHC01H1G3444.2.
DR   GeneID; 102581743; -.
DR   Gramene; PGSC0003DMT400050018; PGSC0003DMT400050018; PGSC0003DMG400019435.
DR   Gramene; RHC01H1G3444.2.1; RHC01H1G3444.2.1; RHC01H1G3444.2.
DR   KEGG; sot:102581743; -.
DR   HOGENOM; CLU_1328439_0_0_1; -.
DR   InParanoid; P09762; -.
DR   OrthoDB; 1332779at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P09762; baseline.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:InterPro.
DR   GO; GO:0050832; P:defense response to fungus; IEA:InterPro.
DR   Gene3D; 2.40.40.10; -; 1.
DR   Gene3D; 3.30.60.10; -; 1.
DR   InterPro; IPR018226; Barwin_CS.
DR   InterPro; IPR001153; Barwin_dom.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR044301; PR4.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR46351; PTHR46351; 1.
DR   Pfam; PF00967; Barwin; 1.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   PRINTS; PR00602; BARWIN.
DR   PRINTS; PR00451; CHITINBINDNG.
DR   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
DR   SUPFAM; SSF57016; SSF57016; 1.
DR   PROSITE; PS00771; BARWIN_1; 1.
DR   PROSITE; PS00772; BARWIN_2; 1.
DR   PROSITE; PS51174; BARWIN_3; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
PE   2: Evidence at transcript level;
KW   Chitin-binding; Disulfide bond; Reference proteome; Signal.
FT   SIGNAL          1..25
FT   CHAIN           26..211
FT                   /note="Wound-induced protein WIN2"
FT                   /id="PRO_0000005286"
FT   DOMAIN          26..68
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DOMAIN          77..198
FT                   /note="Barwin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00527"
FT   DISULFID        28..43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        37..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        42..56
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        62..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
SQ   SEQUENCE   211 AA;  22498 MW;  F7831ACC7BCAB9F8 CRC64;
     MVKLSCGPIL LALVLCISLT SVANAQQCGR QRGGALCGNN LCCSQFGWCG STPEYCSPSQ
     GCQSQCTGSG PDPGQGGSAQ NVRATYHIYN PQNVGWDLNA VSAYCSTWDA NKPYAWRSKY
     GWTAFCGPVG PRGRDSCGKC LRVTNTRTGA QTTVRIVDQC SNGGLDLDIN VFQQIDTDGV
     GNQQGHLIVN YQFVNCGDNV NVPLLSVVDK E
 
 
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