PUIA_WHEAT
ID PUIA_WHEAT Reviewed; 148 AA.
AC P33432; Q5BHS1; Q6J542; Q6L5P2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Puroindoline-A;
DE Flags: Precursor;
GN Name=PINA;
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].
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. U29; TISSUE=Leaf;
RA Chang C., Li W., Li B., Liu G.;
RT "Some new allele variations of puroindolines gene in common wheat.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Renan;
RG Genoscope;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 29-146, DISULFIDE BONDS, AND VARIANTS ASP-29 DEL;
RP 144-ILE--TYR-146 DEL AND TYR-146 DEL.
RC STRAIN=cv. Camp Remy; TISSUE=Endosperm;
RX PubMed=8365477; DOI=10.1016/0014-5793(93)80249-t;
RA Blochet J.-E., Chevalier C., Forest E., Pebay-Peyroula E., Gautier M.-F.,
RA Joudrier P., Pezolet M., Marion D.;
RT "Complete amino acid sequence of puroindoline, a new basic and cystine-rich
RT protein with a unique tryptophan-rich domain, isolated from wheat endosperm
RT by Triton X-114 phase partitioning.";
RL FEBS Lett. 329:336-340(1993).
RN [7]
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 [8]
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 [9]
RP FUNCTION, MASS SPECTROMETRY, AND POLYMORPHISM.
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 PINB 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=12741; Method=Electrospray; Note=In cv.
CC Riband.; Evidence={ECO:0000269|PubMed:17076702};
CC -!- MASS SPECTROMETRY: Mass=12743; Method=Electrospray; Note=In cv.
CC Hereward.; Evidence={ECO:0000269|PubMed:17076702};
CC -!- MASS SPECTROMETRY: Mass=12744; Method=Electrospray; Note=In cv.
CC Soissons.; Evidence={ECO:0000269|PubMed:17076702};
CC -!- POLYMORPHISM: Variation in, or absence of, PINA is associated with
CC variation in grain texture.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT40243.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD21121.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X69913; CAA49538.1; -; mRNA.
DR EMBL; X69914; CAA49539.1; -; mRNA.
DR EMBL; AJ302091; CAC33790.1; -; Genomic_DNA.
DR EMBL; DQ363911; ABD72477.1; -; Genomic_DNA.
DR EMBL; DQ363912; ABD72478.1; -; Genomic_DNA.
DR EMBL; AB177392; BAD21121.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AB181238; BAD22739.1; -; Genomic_DNA.
DR EMBL; AY599893; AAT40243.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CR626934; CAH10197.1; -; Genomic_DNA.
DR EMBL; CT009735; CAJ15418.1; -; Genomic_DNA.
DR PIR; S46515; S46515.
DR AlphaFoldDB; P33432; -.
DR TCDB; 1.C.66.1.1; the puroindoline (puroindoline) family.
DR PRIDE; P33432; -.
DR EnsemblPlants; TraesCAD_scaffold_013709_01G000600.1; TraesCAD_scaffold_013709_01G000600.1; TraesCAD_scaffold_013709_01G000600.
DR EnsemblPlants; TraesCLE_scaffold_000763_01G000800.1; TraesCLE_scaffold_000763_01G000800.1; TraesCLE_scaffold_000763_01G000800.
DR EnsemblPlants; TraesCS5D02G004100.1; TraesCS5D02G004100.1.cds1; TraesCS5D02G004100.
DR EnsemblPlants; TraesPAR_scaffold_003170_01G000700.1; TraesPAR_scaffold_003170_01G000700.1; TraesPAR_scaffold_003170_01G000700.
DR EnsemblPlants; TraesROB_scaffold_024256_01G000400.1; TraesROB_scaffold_024256_01G000400.1; TraesROB_scaffold_024256_01G000400.
DR Gramene; TraesCAD_scaffold_013709_01G000600.1; TraesCAD_scaffold_013709_01G000600.1; TraesCAD_scaffold_013709_01G000600.
DR Gramene; TraesCLE_scaffold_000763_01G000800.1; TraesCLE_scaffold_000763_01G000800.1; TraesCLE_scaffold_000763_01G000800.
DR Gramene; TraesCS5D02G004100.1; TraesCS5D02G004100.1.cds1; TraesCS5D02G004100.
DR Gramene; TraesPAR_scaffold_003170_01G000700.1; TraesPAR_scaffold_003170_01G000700.1; TraesPAR_scaffold_003170_01G000700.
DR Gramene; TraesROB_scaffold_024256_01G000400.1; TraesROB_scaffold_024256_01G000400.1; TraesROB_scaffold_024256_01G000400.
DR HOGENOM; CLU_1621987_0_0_1; -.
DR OMA; GCEELLH; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P33432; baseline and differential.
DR Genevisible; P33432; 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: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; 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 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..28
FT /evidence="ECO:0000269|PubMed:8365477"
FT /id="PRO_0000032285"
FT CHAIN 29..146
FT /note="Puroindoline-A"
FT /id="PRO_0000032286"
FT PROPEP 147..148
FT /note="Removed in mature form"
FT /id="PRO_0000032287"
FT VARIANT 29
FT /note="Missing (in a few molecules)"
FT /evidence="ECO:0000269|PubMed:8365477"
FT VARIANT 144..146
FT /note="Missing (in about 50% of the molecules)"
FT /evidence="ECO:0000269|PubMed:8365477"
FT VARIANT 146
FT /note="Missing (in almost all molecules)"
FT /evidence="ECO:0000269|PubMed:8365477"
FT CONFLICT 13
FT /note="V -> E (in Ref. 4; BAD21121/AAT40243)"
FT /evidence="ECO:0000305"
FT CONFLICT 139..140
FT /note="NI -> KL (in Ref. 4; BAD22739)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 148 AA; 16387 MW; BA9E0DB7EF5E9D2C CRC64;
MKALFLIGLL ALVASTAFAQ YSEVVGSYDV AGGGGAQQCP VETKLNSCRN YLLDRCSTMK
DFPVTWRWWK WWKGGCQELL GECCSRLGQM PPQCRCNIIQ GSIQGDLGGI FGFQRDRASK
VIQEAKNLPP RCNQGPPCNI PGTIGYYW
