PHSB_PHAVU
ID PHSB_PHAVU Reviewed; 421 AA.
AC P02853; P07220; Q84N11;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Phaseolin, beta-type;
DE Flags: Precursor;
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16593301; DOI=10.1073/pnas.80.7.1897;
RA Slightom J.L., Sun S.M., Hall T.C.;
RT "Complete nucleotide sequence of a French bean storage protein gene:
RT phaseolin.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:1897-1901(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3013879; DOI=10.1016/s0021-9258(18)67644-6;
RA Doyle J.J., Schuler M.A., Godette W.D., Zenger V., Beachy R.N.,
RA Slightom J.L.;
RT "The glycosylated seed storage proteins of Glycine max and Phaseolus
RT vulgaris. Structural homologies of genes and proteins.";
RL J. Biol. Chem. 261:9228-9238(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Tendergreen; TISSUE=Cotyledon;
RX PubMed=2997710; DOI=10.1093/nar/13.18.6483;
RA Slightom J.L., Drong R.F., Klassy R.C., Hoffman L.M.;
RT "Nucleotide sequences from phaseolin cDNA clones: the major storage
RT proteins from Phaseolus vulgaris are encoded by two unique gene families.";
RL Nucleic Acids Res. 13:6483-6498(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 142-322.
RA Sun S.M., Slightom J.L., Hall T.C.;
RT "Intervening sequences in a plant gene -- comparison of the partial
RT sequence of cDNA and genomic DNA of French bean phaseolin.";
RL Nature 289:37-41(1981).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 194-221.
RX PubMed=7862642; DOI=10.1073/pnas.92.4.1101;
RA Kami J., Velasquez V.B., Debouck D.G., Gepts P.;
RT "Identification of presumed ancestral DNA sequences of phaseolin in
RT Phaseolus vulgaris.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1101-1104(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=2295315; DOI=10.1002/j.1460-2075.1990.tb08074.x;
RA Lawrence M.C., Suzuki E., Varghese J.N., Davis P.C., van Donkelaar A.,
RA Tuloch P.A., Colman P.M.;
RT "The three-dimensional structure of the seed storage protein phaseolin at
RT 3-A resolution.";
RL EMBO J. 9:9-15(1990).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=8182747; DOI=10.1006/jmbi.1994.1333;
RA Lawrence M.C., Izard T., Beuchat M., Blagrove R.J., Colman P.M.;
RT "Structure of phaseolin at 2.2-A resolution. Implications for a common
RT vicilin/legumin structure and the genetic engineering of seed storage
RT proteins.";
RL J. Mol. Biol. 238:748-776(1994).
CC -!- FUNCTION: Major seed storage protein.
CC -!- SUBUNIT: Homotrimer that associates to form a dodecamer.
CC -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain. Vacuole.
CC Note=Cotyledonary membrane-bound vacuolar protein bodies.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23610.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA24492.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J01263; AAC23610.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X03004; CAA26789.1; -; mRNA.
DR EMBL; V01163; CAA24492.1; ALT_INIT; Genomic_DNA.
DR EMBL; S74637; AAP31811.1; -; Genomic_DNA.
DR PIR; A03343; FSFB.
DR PIR; A24810; A24810.
DR PDB; 1PHS; X-ray; 3.00 A; A=25-421.
DR PDB; 2PHL; X-ray; 2.20 A; A/B/C=25-421.
DR PDBsum; 1PHS; -.
DR PDBsum; 2PHL; -.
DR AlphaFoldDB; P02853; -.
DR SMR; P02853; -.
DR Allergome; 8837; Pha v Phaseolin.
DR GlyConnect; 494; 3 N-Linked glycans (2 sites).
DR EvolutionaryTrace; P02853; -.
DR GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 1.
DR SMART; SM00835; Cupin_1; 1.
DR SUPFAM; SSF51182; SSF51182; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Seed storage protein; Signal; Storage protein;
KW Vacuole.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..421
FT /note="Phaseolin, beta-type"
FT /id="PRO_0000032195"
FT DOMAIN 237..390
FT /note="Cupin type-1"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /id="CAR_000078"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /id="CAR_000079"
FT CONFLICT 194..195
FT /note="FN -> SM (in Ref. 5; AAP31811)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="L -> P (in Ref. 4; CAA24492)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="L -> Q (in Ref. 4; CAA24492)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="L -> P (in Ref. 4; CAA24492)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="D -> G (in Ref. 4; CAA24492)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="Y -> I (in Ref. 3; CAA26789)"
FT /evidence="ECO:0000305"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2PHL"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:2PHL"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 85..113
FT /evidence="ECO:0007829|PDB:2PHL"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 153..166
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2PHL"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:2PHL"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:2PHL"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:2PHL"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:2PHL"
FT HELIX 224..232
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 251..258
FT /evidence="ECO:0007829|PDB:2PHL"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 274..283
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 285..302
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 332..348
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 354..363
FT /evidence="ECO:0007829|PDB:2PHL"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:2PHL"
FT HELIX 374..381
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:2PHL"
FT HELIX 386..393
FT /evidence="ECO:0007829|PDB:2PHL"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:2PHL"
SQ SEQUENCE 421 AA; 47565 MW; 3197A82D90FB3D61 CRC64;
MMRARVPLLL LGILFLASLS ASFATSLREE EESQDNPFYF NSDNSWNTLF KNQYGHIRVL
QRFDQQSKRL QNLEDYRLVE FRSKPETLLL PQQADAELLL VVRSGSAILV LVKPDDRREY
FFLTSDNPIF SDHQKIPAGT IFYLVNPDPK EDLRIIQLAM PVNNPQIHEF FLSSTEAQQS
YLQEFSKHIL EASFNSKFEE INRVLFEEEG QQEGVIVNID SEQIKELSKH AKSSSRKSLS
KQDNTIGNEF GNLTERTDNS LNVLISSIEM EEGALFVPHY YSKAIVILVV NEGEAHVELV
GPKGNKETLE YESYRAELSK DDVFVIPAAY PVAIKATSNV NFTGFGINAN NNNRNLLAGK
TDNVISSIGR ALDGKDVLGL TFSGSGDEVM KLINKQSGSY FVDAHHHQQE QQKGRKGAFV
Y
