GDA9_WHEAT
ID GDA9_WHEAT Reviewed; 307 AA.
AC P18573;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Alpha/beta-gliadin MM1;
DE AltName: Full=Prolamin;
DE Flags: Precursor;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Chinese Spring; TISSUE=Endosperm;
RX PubMed=2102865; DOI=10.1007/bf00016521;
RA Garcia-Maroto F., Manana C., Garcia-Olmedo F., Carbonero P.;
RT "Nucleotide sequence of a cDNA encoding an alpha/beta-type gliadin from
RT hexaploid wheat (Triticum aestivum).";
RL Plant Mol. Biol. 14:867-868(1990).
RN [2]
RP ALLERGEN, AND REGION.
RX PubMed=12351792; DOI=10.1126/science.1074129;
RA Shan L., Molberg O., Parrot I., Hausch F., Filiz F., Gray G.M.,
RA Sollid L.M., Khosla C.;
RT "Structural basis for gluten intolerance in celiac sprue.";
RL Science 297:2275-2279(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 243-260 IN COMPLEX WITH
RP HLA-DQA1/HLA-DQB1 HETERODIMER.
RX PubMed=17629515; DOI=10.1016/j.immuni.2007.05.015;
RA Henderson K.N., Tye-Din J.A., Reid H.H., Chen Z., Borg N.A., Beissbarth T.,
RA Tatham A., Mannering S.I., Purcell A.W., Dudek N.L., van Heel D.A.,
RA McCluskey J., Rossjohn J., Anderson R.P.;
RT "A structural and immunological basis for the role of human leukocyte
RT antigen DQ8 in celiac disease.";
RL Immunity 27:23-34(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 243-260 IN COMPLEX WITH
RP HLA-DQA1/HLA-DQB1 HETERODIMER.
RX PubMed=23063329; DOI=10.1016/j.immuni.2012.07.013;
RA Broughton S.E., Petersen J., Theodossis A., Scally S.W., Loh K.L.,
RA Thompson A., van Bergen J., Kooy-Winkelaar Y., Henderson K.N., Beddoe T.,
RA Tye-Din J.A., Mannering S.I., Purcell A.W., McCluskey J., Anderson R.P.,
RA Koning F., Reid H.H., Rossjohn J.;
RT "Biased T cell receptor usage directed against human leukocyte antigen DQ8-
RT restricted gliadin peptides is associated with celiac disease.";
RL Immunity 37:611-621(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 246-260 IN COMPLEX WITH
RP HLA-DQA1/HLA-DQB1 HETERODIMER.
RX PubMed=25948817; DOI=10.4049/jimmunol.1500161;
RA Petersen J., van Bergen J., Loh K.L., Kooy-Winkelaar Y., Beringer D.X.,
RA Thompson A., Bakker S.F., Mulder C.J., Ladell K., McLaren J.E., Price D.A.,
RA Rossjohn J., Reid H.H., Koning F.;
RT "Determinants of gliadin-specific T cell selection in celiac disease.";
RL J. Immunol. 194:6112-6122(2015).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 246-260 IN COMPLEX WITH
RP HLA-DQA1/HLA-DQB1 HETERODIMER.
RX PubMed=27568928; DOI=10.1016/j.str.2016.07.010;
RA Petersen J., Kooy-Winkelaar Y., Loh K.L., Tran M., van Bergen J.,
RA Koning F., Rossjohn J., Reid H.H.;
RT "Diverse T cell receptor gene usage in HLA-DQ8-associated celiac disease
RT converges into a consensus binding solution.";
RL Structure 24:1643-1657(2016).
CC -!- FUNCTION: Gliadin is the major seed storage protein in wheat.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in endosperm.
CC {ECO:0000269|PubMed:2102865}.
CC -!- PTM: Substrate of transglutaminase. {ECO:0000305|PubMed:12351792}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Is the cause of the
CC celiac disease, also known as celiac sprue or gluten-sensitive
CC enteropathy. {ECO:0000269|PubMed:12351792}.
CC -!- MISCELLANEOUS: An internal 33-mer peptide seems to be the primary
CC initiator of the inflammatory response to gluten in Celiac Sprue
CC patients. {ECO:0000269|PubMed:12351792}.
CC -!- MISCELLANEOUS: The alpha/beta-gliadins can be divided into 5 homology
CC classes. Sequence divergence between the classes is due to single base
CC substitutions and to duplications or deletions within or near direct
CC repeats. There are more than a 100 copies of the gene for alpha/beta-
CC gliadin per haploid genome. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the gliadin/glutenin family. {ECO:0000305}.
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DR EMBL; X17361; CAA35238.1; -; mRNA.
DR PIR; S10015; S10015.
DR PDB; 2NNA; X-ray; 2.10 A; C=243-260.
DR PDB; 4GG6; X-ray; 3.20 A; I/J=243-260.
DR PDB; 4OZF; X-ray; 2.70 A; J=96-105.
DR PDB; 4OZG; X-ray; 3.00 A; I/J=96-105.
DR PDB; 4OZH; X-ray; 2.80 A; I/J=96-105.
DR PDB; 4OZI; X-ray; 3.20 A; I/J=79-89.
DR PDB; 4Z7U; X-ray; 2.70 A; I/J=246-264.
DR PDB; 4Z7V; X-ray; 2.65 A; I/J=246-264.
DR PDB; 4Z7W; X-ray; 2.89 A; I/J=246-264.
DR PDB; 5KS9; X-ray; 2.55 A; I/J=246-260.
DR PDBsum; 2NNA; -.
DR PDBsum; 4GG6; -.
DR PDBsum; 4OZF; -.
DR PDBsum; 4OZG; -.
DR PDBsum; 4OZH; -.
DR PDBsum; 4OZI; -.
DR PDBsum; 4Z7U; -.
DR PDBsum; 4Z7V; -.
DR PDBsum; 4Z7W; -.
DR PDBsum; 5KS9; -.
DR AlphaFoldDB; P18573; -.
DR SMR; P18573; -.
DR IntAct; P18573; 2.
DR PRIDE; P18573; -.
DR ABCD; P18573; 8 sequenced antibodies.
DR EvolutionaryTrace; P18573; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P18573; baseline and differential.
DR GO; GO:0045735; F:nutrient reservoir activity; 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 PRINTS; PR00208; GLIADGLUTEN.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Reference proteome; Repeat; Seed storage protein;
KW Signal; Storage protein.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..307
FT /note="Alpha/beta-gliadin MM1"
FT /id="PRO_0000032275"
FT REGION 29..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..108
FT /note="Sufficient to initiate the primary inflammatory
FT response to gluten in Celiac Sprue patients"
FT /evidence="ECO:0000269|PubMed:12351792"
FT REGION 242..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..114
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 307 AA; 35397 MW; 06C1858BD96F1E08 CRC64;
MKTFLILALL AIVATTARIA VRVPVPQLQP QNPSQQQPQE QVPLVQQQQF PGQQQPFPPQ
QPYPQPQPFP SQQPYLQLQP FPQPQLPYPQ PQLPYPQPQL PYPQPQPFRP QQPYPQSQPQ
YSQPQQPISQ QQQQQQQQQQ QKQQQQQQQQ ILQQILQQQL IPCRDVVLQQ HSIAYGSSQV
LQQSTYQLVQ QLCCQQLWQI PEQSRCQAIH NVVHAIILHQ QQQQQQQQQQ QPLSQVSFQQ
PQQQYPSGQG SFQPSQQNPQ AQGSVQPQQL PQFEEIRNLA LETLPAMCNV YIPPYCTIAP
VGIFGTN
