ALB1E_PEA
ID ALB1E_PEA Reviewed; 130 AA.
AC P62930; P08687; Q40999; Q7XZC1; Q9M3X4;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Albumin-1 E;
DE AltName: Full=PA1 E;
DE AltName: Full=PsaA1b014;
DE Short=Psa;
DE Contains:
DE RecName: Full=Albumin-1 E chain b;
DE AltName: Full=Leginsulin E;
DE AltName: Full=PA1b E;
DE Contains:
DE RecName: Full=Albumin-1 E chain a;
DE AltName: Full=PA1a E;
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. Greenfeast;
RX PubMed=9749674; DOI=10.1007/s004380050817;
RA Morton R.L., Ellery A.J., Higgins T.J.;
RT "Downstream elements from the pea albumin 1 gene confer sulfur
RT responsiveness on a reporter gene.";
RL Mol. Gen. Genet. 259:309-316(1998).
RN [2]
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).
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 -!- 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; M81864; AAC61879.1; -; Genomic_DNA.
DR EMBL; AJ574795; CAE00467.1; -; Genomic_DNA.
DR AlphaFoldDB; P62930; -.
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 3: Inferred from homology;
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 E chain b"
FT /id="PRO_0000032231"
FT PROPEP 64..69
FT /evidence="ECO:0000255"
FT /id="PRO_0000032232"
FT CHAIN 70..122
FT /note="Albumin-1 E chain a"
FT /id="PRO_0000032233"
FT PROPEP 123..130
FT /evidence="ECO:0000255"
FT /id="PRO_0000032234"
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; 13778 MW; C534DE67A304F749 CRC64;
MASVKLASLI VLFATLGMFL TKNVGAASCN GVCSPFEMPP CGSSACRCIP VGLLIGYCRN
PSGVFLKGND EHPNLCESDA DCKKKGSGNF CGHYPNPDIE YGWCFASKSE AEDVFSKITP
KDLLKSVSTA