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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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