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PUIB_WHEAT
ID   PUIB_WHEAT              Reviewed;         148 AA.
AC   Q10464; Q546N5; Q5BHS0; Q6ISY2; Q6J5P4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Puroindoline-B;
DE   Flags: Precursor;
GN   Name=PINB;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Capitole; TISSUE=Seed;
RX   PubMed=7516201; DOI=10.1007/bf00024197;
RA   Gautier M.-F., Aleman M.-F., Guirao A., Marion D., Joudrier P.;
RT   "Triticum aestivum puroindolines, two basic cystine-rich seed proteins:
RT   cDNA sequence analysis and developmental gene expression.";
RL   Plant Mol. Biol. 25:43-57(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Penawawa; TISSUE=Seed;
RX   AGRICOLA=IND23303453;
RA   Lillemo M., Simeone M.C., Morris C.F.;
RT   "Analysis of puroindoline a and b sequences from Triticum aestivum cv.
RT   'Penawawa' and related dipoloid taxa.";
RL   Euphytica 126:321-331(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-75.
RC   STRAIN=cv. Cheyenne, and cv. Chinese Spring; TISSUE=Seed;
RX   AGRICOLA=IND43829610; DOI=10.1016/j.jcs.2006.02.002;
RA   Simeone M.C., Gedye K.R., Mason-Gamer R., Gill B.S., Morris C.F.;
RT   "Conserved regulatory elements identified from a comparative puroindoline
RT   gene sequence survey of Triticum and Aegilops diploid taxa.";
RL   J. Cereal Sci. 44:21-33(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Jing 771, and cv. Tachun 3; TISSUE=Leaf;
RA   Chang C., Li W., Li B., Liu G.;
RT   "A new variation of puroindoline b in common wheat.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-75.
RC   STRAIN=cv. Renan;
RG   Genoscope;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Takeuchi T., Sato M., Suzuki T., Yoshimura Y., Nakamichi K., Kobayashi S.,
RA   Nishimura T., Ikenaga M., Sato N.;
RT   "Sequence analysis of Pina-D1b allele in hard wheat.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PROTEIN SEQUENCE OF 30-148.
RA   Blochet J.E., Kaboulou A., Compoint J.P., Marion D.;
RT   "Amphiphilic proteins from wheat flour: specific extraction, structure and
RT   lipid-binding properties.";
RL   (In) Bushuk W., Tkachuk R. (eds.);
RL   Gluten proteins, pp.314-325, American Association of Cereal Chemists, St.
RL   Paul (1991).
RN   [8]
RP   FUNCTION.
RX   PubMed=12668449; DOI=10.1016/s0006-3495(03)75046-2;
RA   Charnet P., Molle G., Marion D., Rousset M., Lullien-Pellerin V.;
RT   "Puroindolines form ion channels in biological membranes.";
RL   Biophys. J. 84:2416-2426(2003).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16240178; DOI=10.1007/s11103-005-8270-9;
RA   Capparelli R., Amoroso M.G., Palumbo D., Iannaccone M., Faleri C.,
RA   Cresti M.;
RT   "Two plant puroindolines colocalize in wheat seed and in vitro
RT   synergistically fight against pathogens.";
RL   Plant Mol. Biol. 58:857-867(2005).
RN   [10]
RP   FUNCTION, MASS SPECTROMETRY, POLYMORPHISM, AND VARIANTS ARG-73; SER-75 AND
RP   PRO-89.
RX   PubMed=17076702; DOI=10.1111/j.1742-4658.2006.05528.x;
RA   Day L., Bhandari D.G., Greenwell P., Leonard S.A., Schofield J.D.;
RT   "Characterization of wheat puroindoline proteins.";
RL   FEBS J. 273:5358-5373(2006).
CC   -!- FUNCTION: Acts as a membranotoxin, probably through its antibacterial
CC       and antifungal activities, contributing to the defense mechanism of the
CC       plant against predators. Forms monovalent cation-selective ion channels
CC       in membranes. Has antibacterial activity against the Gram-positive
CC       bacteria S.aureus and C.michiganensis, and the Gram-negative bacteria
CC       E.coli, P.syringae pv phaseoli, A.tumefaciens and E.carotovora subsp
CC       carotovora. Acts synergistically with PINA against bacteria.
CC       Contributes to grain texture and hardness.
CC       {ECO:0000269|PubMed:12668449, ECO:0000269|PubMed:16240178,
CC       ECO:0000269|PubMed:17076702}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16240178}. Secreted,
CC       extracellular space {ECO:0000269|PubMed:16240178}.
CC   -!- TISSUE SPECIFICITY: Endosperm and aleurone layer of developing kernels.
CC       In the aleurone layer, mainly localized to starch granules and the
CC       surface of the plasma membrane, forming a uniform layer, also abundant
CC       in the intercellular space. In the endosperm, mainly localized to
CC       starch granules and the plasma membrane, but less abundant in the
CC       intercellular space. Not found in roots or coleoptiles.
CC       {ECO:0000269|PubMed:16240178, ECO:0000269|PubMed:7516201,
CC       ECO:0000269|Ref.2}.
CC   -!- DEVELOPMENTAL STAGE: Starts to accumulate in seeds between 8 and 12
CC       days after flowering. Levels increase markedly between 15 and 18 days
CC       after flowering, reaching a peak between 26 and 33 days after
CC       flowering. Levels then decline rapidly at none is detected at 40 days
CC       after flowering. Not detected in germinated seeds.
CC       {ECO:0000269|PubMed:7516201}.
CC   -!- PTM: Five disulfide bonds are present.
CC   -!- MASS SPECTROMETRY: Mass=13076; Method=Electrospray; Note=In cv.
CC       Riband.; Evidence={ECO:0000269|PubMed:17076702};
CC   -!- MASS SPECTROMETRY: Mass=13076; Method=MALDI; Note=In cv. Consort.;
CC       Evidence={ECO:0000269|PubMed:17076702};
CC   -!- MASS SPECTROMETRY: Mass=13103; Method=Electrospray; Note=In cv.
CC       Hereward.; Evidence={ECO:0000269|PubMed:17076702};
CC   -!- MASS SPECTROMETRY: Mass=13106; Method=MALDI; Note=In cv. Hereward.;
CC       Evidence={ECO:0000269|PubMed:17076702};
CC   -!- MASS SPECTROMETRY: Mass=13045; Method=Electrospray; Note=In cv.
CC       Soissons.; Evidence={ECO:0000269|PubMed:17076702};
CC   -!- POLYMORPHISM: Variation in, or absence of, PINB is associated with
CC       variation in grain texture.
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DR   EMBL; X69912; CAA49537.1; -; mRNA.
DR   EMBL; AJ302100; CAC33791.1; -; Genomic_DNA.
DR   EMBL; DQ363913; ABD72479.1; -; Genomic_DNA.
DR   EMBL; DQ363914; ABD72480.1; -; Genomic_DNA.
DR   EMBL; AB177390; BAD21119.1; -; Genomic_DNA.
DR   EMBL; AB180737; BAD22738.1; -; Genomic_DNA.
DR   EMBL; AY598029; AAT40245.1; -; Genomic_DNA.
DR   EMBL; AY640304; AAT40244.1; -; Genomic_DNA.
DR   EMBL; CR626934; CAH10199.1; -; Genomic_DNA.
DR   EMBL; CT009735; CAJ15420.1; -; Genomic_DNA.
DR   EMBL; AB262660; BAE96109.1; -; Genomic_DNA.
DR   PIR; S46514; S46514.
DR   AlphaFoldDB; Q10464; -.
DR   PRIDE; Q10464; -.
DR   HOGENOM; CLU_1621987_0_0_1; -.
DR   OMA; CEQMSET; -.
DR   Proteomes; UP000019116; Unplaced.
DR   ExpressionAtlas; Q10464; baseline.
DR   Genevisible; Q10464; TA.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   CDD; cd00261; AAI_SS; 1.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR044723; AAI_SS_dom.
DR   InterPro; IPR006106; Allergen/soft/tryp_amyl_inhib.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   InterPro; IPR001954; Glia_glutenin.
DR   PANTHER; PTHR33454; PTHR33454; 1.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PRINTS; PR00808; AMLASEINHBTR.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Membrane; Plant defense; Reference proteome; Secreted; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..29
FT                   /evidence="ECO:0000269|Ref.7"
FT                   /id="PRO_0000032288"
FT   CHAIN           30..148
FT                   /note="Puroindoline-B"
FT                   /id="PRO_0000032289"
FT   VARIANT         73
FT                   /note="W -> R (found in hard wheats, including cv.
FT                   Soissons)"
FT                   /evidence="ECO:0000269|PubMed:17076702"
FT   VARIANT         75
FT                   /note="G -> S (found in hard wheats, including cv. Buster
FT                   and cv. Shamrock)"
FT                   /evidence="ECO:0000269|PubMed:17076702, ECO:0000269|Ref.3,
FT                   ECO:0000269|Ref.5"
FT   VARIANT         89
FT                   /note="L -> P (found in cv. Chablis, but no mature PINB
FT                   protein is found in this cultivar)"
FT                   /evidence="ECO:0000269|PubMed:17076702"
FT   CONFLICT        8..9
FT                   /note="AL -> TI (in Ref. 4; BAD21119/AAT40245)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="S -> I (in Ref. 4; BAD22738/AAT40244)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   148 AA;  16792 MW;  327904B4EBEC2C16 CRC64;
     MKTLFLLALL ALVASTTFAQ YSEVGGWYNE VGGGGGSQQC PQERPKLSSC KDYVMERCFT
     MKDFPVTWPT KWWKGGCEHE VREKCCKQLS QIAPQCRCDS IRRVIQGRLG GFLGIWRGEV
     FKQLQRAQSL PSKCNMGADC KFPSGYYW
 
 
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