ID   AVE3_AVESA              Reviewed;         220 AA.
AC   P80356;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Avenin-3;
DE   AltName: Full=Prolamin;
DE   Flags: Precursor;
OS   Avena sativa (Oat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Aveninae; Avena.
OX   NCBI_TaxID=4498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=2535531; DOI=10.2307/3868938;
RA   Chesnut R.S., Shotwell M.A., Boyer S.K., Larkins B.A.;
RT   "Analysis of avenin proteins and the expression of their mRNAs in
RT   developing oat seeds.";
RL   Plant Cell 1:913-924(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-220, AND PYROGLUTAMATE FORMATION AT GLN-20.
RC   STRAIN=cv. Narymsky 943; TISSUE=Endosperm;
RX   PubMed=7925380; DOI=10.1111/j.1432-1033.1994.00631.x;
RA   Egorov T.A., Musolyamov A.K., Andersen J.S., Roepstorff P.;
RT   "The complete amino acid sequence and disulphide bond arrangement of oat
RT   alcohol-soluble avenin-3.";
RL   Eur. J. Biochem. 224:631-638(1994).
CC   -!- FUNCTION: Seed storage protein. Serves as a source of nitrogen, carbon,
CC       and sulfur for the young developing seedling.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Vacuole. Note=Protein bodies inside vacuoles.
CC   -!- DEVELOPMENTAL STAGE: First found between 4-6 days after anthesis (daa).
CC       Peaks at 8 daa when the seeds are in the milky endosperm stages.
CC   -!- SIMILARITY: Belongs to the gliadin/glutenin family. {ECO:0000305}.
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DR   EMBL; M38722; AAA32715.1; -; mRNA.
DR   PIR; JQ1046; JQ1046.
DR   AlphaFoldDB; P80356; -.
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   Direct protein sequencing; Disulfide bond; Pyrrolidone carboxylic acid;
KW   Repeat; Seed storage protein; Signal; Storage protein; Vacuole.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:7925380"
FT   CHAIN           20..220
FT                   /note="Avenin-3"
FT                   /id="PRO_0000032284"
FT   REPEAT          41..48
FT                   /note="1-1"
FT   REPEAT          49..56
FT                   /note="1-2"
FT   REPEAT          128..137
FT                   /note="2-1"
FT   REPEAT          138..146
FT                   /note="2-2; approximate"
FT   REGION          41..56
FT                   /note="2 X 8 AA tandem repeats of Q-Q-M-L-L-Q-Q-Q"
FT   REGION          128..146
FT                   /note="2 X 10 AA tandem repeats of M-Q-Q-Q-Q-F-F-Q-P-Q"
FT   MOD_RES         20
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:7925380"
FT   DISULFID        69..202
FT   DISULFID        77..96
FT   DISULFID        103..104
FT   DISULFID        116..210
SQ   SEQUENCE   220 AA;  25275 MW;  72E6B18C1FB5F3B2 CRC64;
     MKTFLIFALL AMAATMATAQ FDPSEQYQPY PEQQQPILQQ QQMLLQQQQQ MLLQQQPLLQ
     VLQQQLNPCR QFLVQQCSPV AVVPFLRSQI LQQSSCQVMR QQCCRQLEQI PEQLRCPAIH
     SVVQAIIMQQ QQFFQPQMQQ QFFQPQMQQV TQGIFQPQMQ QVTQGIFQPQ LQQVTQGIFQ
     PQMQGQIEGM RAFALQALPA MCDVYVPPHC PVATAPLGGF