ID   GLTB_WHEAT              Reviewed;         307 AA.
AC   P10386;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Glutenin, low molecular weight subunit 1D1;
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 [GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring;
RX   PubMed=2733691; DOI=10.1007/bf00332234;
RA   Colot V., Bartels D., Thompson R., Flavell R.;
RT   "Molecular characterization of an active wheat LMW glutenin gene and its
RT   relation to other wheat and barley prolamin genes.";
RL   Mol. Gen. Genet. 216:81-90(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=8440244; DOI=10.1002/j.1460-2075.1993.tb05686.x;
RA   Hammond-Kosack M.C., Holdsworth M.J., Bevan M.W.;
RT   "In vivo footprinting of a low molecular weight glutenin gene (LMWG-1D1) in
RT   wheat endosperm.";
RL   EMBO J. 12:545-554(1993).
CC   -!- FUNCTION: Glutenins are high-molecular weight seed storage proteins of
CC       wheat endosperm. Thought to be responsible for the visco-elastic
CC       property of wheat dough.
CC   -!- SUBUNIT: Disulfide-bridge linked aggregates.
CC   -!- TISSUE SPECIFICITY: Expressed in endosperm, but not in husk and leaf
CC       tissues. {ECO:0000269|PubMed:8440244}.
CC   -!- MISCELLANEOUS: Glutenins are coded by several genes on each of the
CC       group 1 chromosomes of wheat.
CC   -!- SIMILARITY: Belongs to the gliadin/glutenin family. {ECO:0000305}.
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DR   EMBL; X13306; CAA31685.1; -; Genomic_DNA.
DR   PIR; S04325; S04325.
DR   AlphaFoldDB; P10386; -.
DR   SMR; P10386; -.
DR   Allergome; 2674; Tri a 36.
DR   PRIDE; P10386; -.
DR   OMA; ARVHQTE; -.
DR   Proteomes; UP000019116; Unplaced.
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; PF13016; Gliadin; 1.
DR   PRINTS; PR00208; GLIADGLUTEN.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Reference proteome; Repeat; Seed storage protein; Signal;
KW   Storage protein.
FT   SIGNAL          1..23
FT   CHAIN           24..307
FT                   /note="Glutenin, low molecular weight subunit 1D1"
FT                   /id="PRO_0000032212"
FT   REGION          31..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   307 AA;  34928 MW;  FE476503CAC5A93A CRC64;
     MKTFLVFALL AVAATSAIAQ METRCIPGLE RPWQQQPLPP QQTFPQQPLF SQQQQQQLFP
     QQPSFSQQQP PFWQQQPPFS QQQPILPQQP PFSQQQQLVL PQQPPFSQQQ QPVLPPQQSP
     FPQQQQQHQQ LVQQQIPVVQ PSILQQLNPC KVFLQQQCSP VAMPQRLARS QMLQQSSCHV
     MQQQCCQQLP QIPQQSRYEA IRAIIYSIIL QEQQQVQGSI QSQQQQPQQL GQCVSQPQQQ
     SQQQLGQQPQ QQQLAQGTFL QPHQIAQLEV MTSIALRILP TMCSVNVPLY RTTTSVPFGV
     GTGVGAY