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2SSI_BRANA
ID   2SSI_BRANA              Reviewed;         110 AA.
AC   P24565;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Napin-1A;
DE   AltName: Full=Napin BnIa;
DE   Contains:
DE     RecName: Full=Napin-1A small chain;
DE   Contains:
DE     RecName: Full=Napin-1A large chain;
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   PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-32.
RC   TISSUE=Seed;
RX   PubMed=1765156; DOI=10.1016/0014-5793(91)81419-9;
RA   Monsalve R.I., Lopez-Otin C., Villalba M., Rodriguez R.;
RT   "A new distinct group of 2 S albumins from rapeseed. Amino acid sequence of
RT   two low molecular weight napins.";
RL   FEBS Lett. 295:207-210(1991).
RN   [2]
RP   STRUCTURE BY NMR OF 1-106, AND DISULFIDE BONDS.
RX   PubMed=8961930; DOI=10.1021/bi961748q;
RA   Rico M., Bruix M., Gonzalez C., Monsalve R.I., Rodriguez R.;
RT   "1H NMR assignment and global fold of napin BnIb, a representative 2S
RT   albumin seed protein.";
RL   Biochemistry 35:15672-15682(1996).
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   -!- MISCELLANEOUS: Napin 1A and 1B are minor component of the seed 2S
CC       albumin.
CC   -!- MISCELLANEOUS: The sequence shown is that of napin IA.
CC   -!- SIMILARITY: Belongs to the 2S seed storage albumins family.
CC       {ECO:0000305}.
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DR   PIR; S20350; S20350.
DR   PIR; S26636; S26636.
DR   PDB; 1PNB; NMR; -; A=1-31, B=32-106.
DR   PDBsum; 1PNB; -.
DR   AlphaFoldDB; P24565; -.
DR   SMR; P24565; -.
DR   EvolutionaryTrace; P24565; -.
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   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Pyrrolidone carboxylic acid; Seed storage protein; Storage protein.
FT   CHAIN           1..31
FT                   /note="Napin-1A small chain"
FT                   /id="PRO_0000032131"
FT   CHAIN           32..110
FT                   /note="Napin-1A large chain"
FT                   /id="PRO_0000032132"
FT   MOD_RES         32
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:1765156"
FT   DISULFID        5..56
FT                   /note="Interchain (between small and large chains)"
FT                   /evidence="ECO:0000269|PubMed:8961930"
FT   DISULFID        18..45
FT                   /note="Interchain (between small and large chains)"
FT                   /evidence="ECO:0000269|PubMed:8961930"
FT   DISULFID        46..93
FT                   /evidence="ECO:0000269|PubMed:8961930"
FT   DISULFID        58..101
FT                   /evidence="ECO:0000269|PubMed:8961930"
FT   VARIANT         31
FT                   /note="Missing (in minor form SM, less than 7%)"
FT   VARIANT         37
FT                   /note="E -> Q (in napin-1B)"
FT   VARIANT         107..110
FT                   /note="Missing (in napin-1B)"
FT   NON_CONS        31..32
FT                   /evidence="ECO:0000305"
FT   HELIX           3..12
FT                   /evidence="ECO:0007829|PDB:1PNB"
FT   HELIX           19..24
FT                   /evidence="ECO:0007829|PDB:1PNB"
FT   HELIX           43..50
FT                   /evidence="ECO:0007829|PDB:1PNB"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:1PNB"
FT   HELIX           58..69
FT                   /evidence="ECO:0007829|PDB:1PNB"
FT   HELIX           71..73
FT                   /evidence="ECO:0007829|PDB:1PNB"
FT   HELIX           79..85
FT                   /evidence="ECO:0007829|PDB:1PNB"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:1PNB"
SQ   SEQUENCE   110 AA;  12691 MW;  3A2938ADA2C1E995 CRC64;
     QPQKCQREFQ QEQHLRACQQ WIRQQLAGSP FQSGPQEGPW LREQCCNELY QEDQVCVCPT
     LKQAAKSVRV QGQHGPFQST RIYQIAKNLP NVCNMKQIGT CPFIAIPFFP
 
 
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