ALB1_SOYBN
ID ALB1_SOYBN Reviewed; 119 AA.
AC Q39837; O49854;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Albumin-1;
DE Short=A1;
DE Contains:
DE RecName: Full=Albumin-1 chain b;
DE Short=A1b;
DE AltName: Full=Leginsulin;
DE Contains:
DE RecName: Full=Albumin-1 chain a;
DE Short=A1a;
DE Flags: Precursor;
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Miyagishirome; TISSUE=Radicle;
RX PubMed=8076638; DOI=10.1111/j.1432-1033.1994.tb20008.x;
RA Watanabe Y., Barbashov S.F., Komatsu S., Hemmings A.M., Miyagi M.,
RA Tsunasawa S., Hirano H.;
RT "A peptide that stimulates phosphorylation of the plant insulin-binding
RT protein. Isolation, primary structure and cDNA cloning.";
RL Eur. J. Biochem. 224:167-172(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Miyagishirome;
RA Tan J.Z., Lou C.F., Hirano H.;
RT "Analysis of leginsulin gene in soybean cultivar (Glycine max) and wild
RT species (Glycine soja).";
RL Ying Yong Yu Huan Jing Sheng Wu Xue Bao 5:259-263(1999).
RN [3]
RP SEQUENCE REVISION TO 64.
RA Hirano H.;
RL Submitted (JUN-2001) to UniProtKB.
RN [4]
RP STRUCTURE BY NMR OF 20-56, MUTAGENESIS OF ARG-35; VAL-48 AND PHE-50, AND
RP FUNCTION.
RC TISSUE=Radicle;
RX PubMed=12631285; DOI=10.1046/j.1432-1033.2003.03489.x;
RA Yamazaki T., Takaoka M., Katoh E., Hanada K., Sakita M., Sakata K.,
RA Nishiuchi Y., Hirano H.;
RT "A possible physiological function and the tertiary structure of a 4-kDa
RT peptide in legumes.";
RL Eur. J. Biochem. 270:1269-1276(2003).
CC -!- FUNCTION: A1b 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.
CC {ECO:0000269|PubMed:12631285}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC -!- PTM: The C-terminal glycine may be removed from A1b.
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; D17396; BAA04219.1; -; mRNA.
DR EMBL; AJ223037; CAA11040.1; -; Genomic_DNA.
DR PIR; S48192; S48192.
DR RefSeq; NP_001237714.1; NM_001250785.1.
DR PDB; 1JU8; NMR; -; A=20-56.
DR PDBsum; 1JU8; -.
DR AlphaFoldDB; Q39837; -.
DR SMR; Q39837; -.
DR STRING; 3847.GLYMA13G26340.1; -.
DR PRIDE; Q39837; -.
DR GeneID; 547776; -.
DR KEGG; gmx:547776; -.
DR OrthoDB; 1619392at2759; -.
DR EvolutionaryTrace; Q39837; -.
DR Proteomes; UP000008827; Unplaced.
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 3D-structure; Disulfide bond; Knottin; Reference proteome;
KW Seed storage protein; Signal; Storage protein; Toxin.
FT SIGNAL 1..19
FT CHAIN 20..56
FT /note="Albumin-1 chain b"
FT /id="PRO_0000032252"
FT PROPEP 57..64
FT /evidence="ECO:0000255"
FT /id="PRO_0000032253"
FT CHAIN 65..116
FT /note="Albumin-1 chain a"
FT /evidence="ECO:0000255"
FT /id="PRO_0000032254"
FT PROPEP 117..119
FT /evidence="ECO:0000255"
FT /id="PRO_0000032255"
FT DISULFID 22..39
FT DISULFID 26..41
FT DISULFID 34..51
FT MUTAGEN 35
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:12631285"
FT MUTAGEN 48
FT /note="V->A: Decreased binding to globulin."
FT /evidence="ECO:0000269|PubMed:12631285"
FT MUTAGEN 50
FT /note="F->A: Decreased binding to globulin."
FT /evidence="ECO:0000269|PubMed:12631285"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1JU8"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:1JU8"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1JU8"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1JU8"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:1JU8"
SQ SEQUENCE 119 AA; 13046 MW; A054491D7BE1AA70 CRC64;
MAVFLLATST IMFPTKIEAA DCNGACSPFE VPPCRSRDCR CVPIGLFVGF CIHPTGLSSV
AKMIDEHPNL CQSDDECMKK GSGNFCARYP NNYIDYGWCF DSDSEALKGF LAMPRATTK
