ID   2SS2_BRANA              Reviewed;         178 AA.
AC   P01090;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Napin-2;
DE   AltName: Full=1.7S seed storage protein;
DE   Contains:
DE     RecName: Full=Napin-2 small chain;
DE   Contains:
DE     RecName: Full=Napin-2 large chain;
DE   Flags: Precursor;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3624251; DOI=10.1016/s0021-9258(18)45336-7;
RA   Josefsson L.-G., Lenman M., Ericson M.L., Rask L.;
RT   "Structure of a gene encoding the 1.7 S storage protein, napin, from
RT   Brassica napus.";
RL   J. Biol. Chem. 262:12196-12201(1987).
RN   [2]
RP   SEQUENCE REVISION.
RA   Josefsson L.-G.;
RL   Submitted (JUL-1987) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3771543; DOI=10.1016/s0021-9258(18)66909-1;
RA   Ericson M.L., Roedin J., Lenman M., Glimelius K., Josefsson L.-G., Rask L.;
RT   "Structure of the rapeseed 1.7 S storage protein, napin, and its
RT   precursor.";
RL   J. Biol. Chem. 261:14576-14581(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Tower;
RX   PubMed=6689334;
RA   Crouch M.L., Tenbarge K.M., Simon A.E., Ferl R.;
RT   "cDNA clones for Brassica napus seed storage proteins: evidence from
RT   nucleotide sequence analysis that both subunits of napin are cleaved from a
RT   precursor polypeptide.";
RL   J. Mol. Appl. Genet. 2:273-283(1983).
CC   -!- FUNCTION: The small, basic, water-soluble napins are one of the two
CC       major kinds of storage proteins synthesized in the seed during its
CC       maturation.
CC   -!- SUBUNIT: The mature protein consists of a small and a large chain
CC       linked by disulfide bonds.
CC   -!- TISSUE SPECIFICITY: Cotyledons and the axis.
CC   -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC       {ECO:0000305}.
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DR   EMBL; K01545; AAA33006.1; -; mRNA.
DR   EMBL; J02586; AAA32997.1; -; mRNA.
DR   EMBL; J02798; AAA87348.1; -; Genomic_DNA.
DR   PIR; A01329; NWRP2.
DR   PIR; A29801; A25997.
DR   AlphaFoldDB; P01090; -.
DR   SMR; P01090; -.
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; IPR000617; Napin/2SS/CON.
DR   PANTHER; PTHR35496; PTHR35496; 1.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PRINTS; PR00496; NAPIN.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Seed storage protein; Signal; Storage protein.
FT   SIGNAL          1..21
FT   PROPEP          22..38
FT                   /id="PRO_0000032114"
FT   CHAIN           39..74
FT                   /note="Napin-2 small chain"
FT                   /id="PRO_0000032115"
FT   PROPEP          75..94
FT                   /id="PRO_0000032116"
FT   CHAIN           95..175
FT                   /note="Napin-2 large chain"
FT                   /id="PRO_0000032117"
FT   PROPEP          176..178
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000032118"
FT   CONFLICT        37
FT                   /note="D -> N (in Ref. 4; AAA33006)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        76
FT                   /note="S -> N (in Ref. 4; AAA33006)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   178 AA;  20104 MW;  734E561971B539FF CRC64;
     MANKLFLVSA TLAFFFLLTN ASIYRTVVEF DEDDATDSAG PFRIPKCRKE FQQAQHLRAC
     QQWLHKQAMQ SGGGPSWTLD GEFDFEDDME NPQGPQQRPP LLQQCCNELH QEEPLCVCPT
     LKGASKAVKQ QIQQQGQQQG KQQMVSRIYQ TATHLPKVCN IPQVSVCPFQ KTMPGPSY