ID   ALB1C_PEA               Reviewed;         130 AA.
AC   P62928; P08687; Q40999; Q7XZC0; Q9M3X4;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Albumin-1 C;
DE   AltName: Full=PA1 C;
DE   AltName: Full=PsaA1b015;
DE   Contains:
DE     RecName: Full=Albumin-1 C chain b;
DE     AltName: Full=Leginsulin C;
DE     AltName: Full=PA1b C;
DE   Contains:
DE     RecName: Full=Albumin-1 C chain a;
DE     AltName: Full=PA1a C;
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].
RC   STRAIN=cv. Frisson; TISSUE=Seed;
RX   AGRICOLA=IND43645431; DOI=10.1016/j.plantsci.2004.04.018;
RA   Louis S., Delobel B., Gressent F., Rahioui I., Quillien L., Vallier A.,
RA   Rahbe Y.;
RT   "Molecular and biological screening for insect-toxic seed albumins from
RT   four legume species.";
RL   Plant Sci. 167:705-714(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 27-63, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   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.
CC   -!- MISCELLANEOUS: The protein sequenced in PubMed:3755437 was probably a
CC       mixture of the products of genes C and D, PA1b being of C origin while
CC       PA1a is of D origin.
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DR   EMBL; AJ574796; CAE00468.1; -; Genomic_DNA.
DR   AlphaFoldDB; P62928; -.
DR   SMR; P62928; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Knottin; Seed storage protein;
KW   Signal; Storage protein; Toxin.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:3755437"
FT   CHAIN           27..63
FT                   /note="Albumin-1 C chain b"
FT                   /id="PRO_0000032223"
FT   PROPEP          64..69
FT                   /id="PRO_0000032224"
FT   CHAIN           70..122
FT                   /note="Albumin-1 C chain a"
FT                   /id="PRO_0000032225"
FT   PROPEP          123..130
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000032226"
FT   DISULFID        29..46
FT                   /evidence="ECO:0000250"
FT   DISULFID        33..48
FT                   /evidence="ECO:0000250"
FT   DISULFID        41..58
FT                   /evidence="ECO:0000250"
FT   CONFLICT        60
FT                   /note="N -> H (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   130 AA;  13912 MW;  12C8EA2B8300A723 CRC64;
     MASVKLASLI VLFATLGMFL TKNVGAISCN GVCSPFDIPP CGSPLCRCIP AGLVIGNCRN
     PYGVFLRTND EHPNLCESDA DCRKKGSGTF CGHYPNPDIE YGWCFASKSE AEDVFSKITP
     KDLLKSVSTA