ID   HOG3_HORVU              Reviewed;         289 AA.
AC   P80198;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Gamma-hordein-3;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-11, AND NUCLEOTIDE SEQUENCE OF 4-289.
RC   STRAIN=cv. HOR2CA; TISSUE=Endosperm;
RX   PubMed=7506098; DOI=10.1046/j.1365-313x.1993.04050841.x;
RA   Rechinger K.B., Simpson D.J., Svendsen I., Cameron-Mills V.;
RT   "A role for gamma 3 hordein in the transport and targeting of prolamin
RT   polypeptides to the vacuole of developing barley endosperm.";
RL   Plant J. 4:841-853(1993).
CC   -!- FUNCTION: Has a role in the transport and targeting of prolamins to the
CC       vacuole of developing barley endosperm.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Vacuole. Note=Cytoplasmic (as
CC       globules) and vacuolar (as protein bodies).
CC   -!- TISSUE SPECIFICITY: Developing endosperm.
CC   -!- DOMAIN: Sulfur-rich hordein which possesses an N-terminal half composed
CC       of proline-glutamine blocks organized in repeating units and a C-
CC       terminal half where the repeats are dispersed and less conserved.
CC   -!- SIMILARITY: Belongs to the gliadin/glutenin family. {ECO:0000305}.
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DR   EMBL; X72628; CAA51204.1; -; mRNA.
DR   PIR; T05718; T05718.
DR   AlphaFoldDB; P80198; -.
DR   Allergome; 3331; Hor v 20.0101.
DR   Allergome; 421; Hor v 20.
DR   ExpressionAtlas; P80198; baseline.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Seed storage protein;
KW   Storage protein; Vacuole.
FT   CHAIN           1..289
FT                   /note="Gamma-hordein-3"
FT                   /id="PRO_0000102600"
FT   REGION          1..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..57
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   289 AA;  33189 MW;  322CB6D7D6F55658 CRC64;
     ITTTTMQFNP SGLELERPQQ LFPQWQPLPQ QPPFLQQEPE QPYPQQQPLP QQQPFPQQPQ
     LPHQHQFPQQ LPQQQFPQQM PLQPQQQFPQ QMPLQPQQQP QFPQQKPFGQ YQQPLTQQPY
     PQQQPLAQQQ PSIEEQHQLN LCKEFLLQQC TLDEKVPLLQ SVISFLRPHI SQQNSCQLKR
     QQCCQQLANI NEQSRCPAIQ TIVHAIVMQQ QVQQQVGHGF VQSQLQQLGQ GMPIQLQQQP
     GQAFVLPQQQ AQFKVVGSLV IQTLPMLCNV HVPPYCSPFG SMATGSGGQ