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HOG1_HORVU
ID   HOG1_HORVU              Reviewed;         305 AA.
AC   P17990;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Gamma-hordein-1;
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Carina;
RX   AGRICOLA=IND92000023; DOI=10.1007/BF00039026;
RA   Cameron-Mills V., Brandt A.;
RT   "A gamma-hordein gene.";
RL   Plant Mol. Biol. 11:449-461(1988).
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; X13508; CAA31861.1; -; Genomic_DNA.
DR   EMBL; M36378; AAA32955.1; -; Genomic_DNA.
DR   PIR; S08312; S08312.
DR   AlphaFoldDB; P17990; -.
DR   PRIDE; P17990; -.
DR   ExpressionAtlas; P17990; 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   2: Evidence at transcript level;
KW   Cytoplasm; Seed storage protein; Signal; Storage protein; Vacuole.
FT   SIGNAL          1..19
FT   CHAIN           20..305
FT                   /note="Gamma-hordein-1"
FT                   /id="PRO_0000032281"
FT   REGION          27..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..146
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   305 AA;  34737 MW;  6D8038533EFB24AD CRC64;
     MKILIILTIL AMATTFATSE MQVNPSVQVQ PTQQQPYPES QQPFISQSQQ QFPQPQQPFP
     QQPQQPFPQS QQQCLQQPQH QFPQPTQQFP QRPLLPFTHP FLTFPDQLLP QPPHQSFPQP
     PQSYPQPPLQ PFPQPPQQKY PEQPQQPFPW QQPTIQLYLQ QQLNPCKEFL LQQCRPVSLL
     SYIWSKIVQQ SSCRVMQQQC CLQLAQIPEQ YKCTAIDSIV HAIFMQQGQR QGVQIVQQQP
     QPQQVGQCVL VQGQGVVQPQ QLAQMEAIRT LVLQSVPSMC NFNVPPNCST IKAPFVGVVT
     GVGGQ
 
 
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