ID   ALB1A_PEA               Reviewed;         130 AA.
AC   P62926; P08687; Q40999; Q9M3X4;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Albumin-1 A;
DE   AltName: Full=PA1 A;
DE   Contains:
DE     RecName: Full=Albumin-1 A chain b;
DE     AltName: Full=Leginsulin A;
DE     AltName: Full=PA1b A;
DE   Contains:
DE     RecName: Full=Albumin-1 A chain a;
DE     AltName: Full=PA1a A;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. Greenfeast; TISSUE=Seed;
RX   PubMed=3755437; DOI=10.1016/s0021-9258(18)67357-0;
RA   Higgins T.J.V., Chandler P.M., Randall P.J., Spencer D., Beach L.R.,
RA   Blagrove R.J., Kortt A.A., Inglis A.S.;
RT   "Gene structure, protein structure, and regulation of the synthesis of a
RT   sulfur-rich protein in pea seeds.";
RL   J. Biol. Chem. 261:11124-11130(1986).
CC   -!- FUNCTION: PA1b binds to basic 7S globulin (BG) and stimulates its
CC       phosphorylation activity. Involved in the signal transduction system to
CC       regulate the growth and differentiation as a hormone peptide. Toxic to
CC       various insects through binding to a high affinity binding site in the
CC       insect gut (By similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Major component of both the cotyledons and
CC       embryonic axes of mature seeds. {ECO:0000269|PubMed:3755437}.
CC   -!- DEVELOPMENTAL STAGE: Increasing expression during seed development
CC       followed by a rapid degradation during the first days of seed
CC       germination. {ECO:0000269|PubMed:3755437}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
CC   -!- PTM: The C-terminal glycine may be removed from PA1b.
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DR   EMBL; M13709; AAA33638.1; -; Genomic_DNA.
DR   PIR; A25014; A25014.
DR   AlphaFoldDB; P62926; -.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012512; Albumin_I.
DR   InterPro; IPR032000; Albumin_I_a.
DR   Pfam; PF08027; Albumin_I; 1.
DR   Pfam; PF16720; Albumin_I_a; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Knottin; Seed storage protein; Signal; Storage protein;
KW   Toxin.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..63
FT                   /note="Albumin-1 A chain b"
FT                   /id="PRO_0000032215"
FT   PROPEP          64..69
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000032216"
FT   CHAIN           70..122
FT                   /note="Albumin-1 A chain a"
FT                   /id="PRO_0000032217"
FT   PROPEP          123..130
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000032218"
FT   DISULFID        29..46
FT                   /evidence="ECO:0000250"
FT   DISULFID        33..48
FT                   /evidence="ECO:0000250"
FT   DISULFID        41..58
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   130 AA;  13912 MW;  1371D80F333E0EFF CRC64;
     MASVKLASLI VLFATLGMFL TKNVGAASCN GVCSPFEMPP CGTSACRCIP VGLVVGYCRN
     PSGVFLRTND EHPNLCESDA DCRKKGSGNF CGHYPNPDIE YGWCFASKSE AEDFFSKITP
     KDLLKSVSTA