ALB1B_PEA
ID ALB1B_PEA Reviewed; 130 AA.
AC P62927; P08687; Q40999; Q9M3X4;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Albumin-1 B;
DE AltName: Full=PA1 B;
DE Contains:
DE RecName: Full=Albumin-1 B chain b;
DE AltName: Full=Leginsulin B;
DE AltName: Full=PA1b B;
DE Contains:
DE RecName: Full=Albumin-1 B chain a;
DE AltName: Full=PA1a B;
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 [MRNA], DEVELOPMENTAL STAGE, AND TISSUE 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Birte; TISSUE=Cotyledon;
RA Domoney C., Ellis N., Welham T.;
RT "Genetic loci controlling albumin synthesis in Pisum.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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 EMBL; M13790; AAA33639.1; -; mRNA.
DR EMBL; AJ276882; CAB82859.1; -; mRNA.
DR AlphaFoldDB; P62927; -.
DR SMR; P62927; -.
DR PRIDE; P62927; -.
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 B chain b"
FT /id="PRO_0000032219"
FT PROPEP 64..69
FT /evidence="ECO:0000255"
FT /id="PRO_0000032220"
FT CHAIN 70..122
FT /note="Albumin-1 B chain a"
FT /id="PRO_0000032221"
FT PROPEP 123..130
FT /evidence="ECO:0000255"
FT /id="PRO_0000032222"
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 10
FT /note="M -> I (in Ref. 2; CAB82859)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="Q -> P (in Ref. 2; CAB82859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 130 AA; 13970 MW; F8B134A334490F5F CRC64;
MASVKLASLM VLFATLGMFL TKNVGAASCN GVCSPFEMPP CGSSACRCIP VGLVVGYCRH
PSGVFLRTND EHPNLCESDA DCRKKGSGNF CGHYPNPDIE YGWCFASKSE AEDFFSKITQ
KDLLKSVSTA