PHBP_VIGRR
ID PHBP_VIGRR Reviewed; 155 AA.
AC A0A1S3THR8; Q9ZWP8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=Phytohormone-binding protein CSBP {ECO:0000305};
DE AltName: Full=Cytokinin-specific binding protein {ECO:0000303|PubMed:9874249};
DE Short=VrCSBP {ECO:0000303|PubMed:16998071};
DE AltName: Full=Major pollen allergen Bet v 1-like protein {ECO:0000305};
DE AltName: Full=Pathogenesis-related PR10-like protein {ECO:0000305};
DE AltName: Allergen=Vig r 6 {ECO:0000305};
GN Name=CSBP {ECO:0000303|PubMed:9874249}; ORFNames=LOC106755646;
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; Vigna.
OX NCBI_TaxID=3916;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 33-39; 40-50 AND
RP 118-129.
RX PubMed=9874249; DOI=10.1046/j.1432-1327.1998.2580794.x;
RA Fujimoto Y., Nagata R., Fukasawa H., Yano K., Azuma M., Iida A.,
RA Sugimoto S., Shudo K., Hashimoto Y.;
RT "Purification and cDNA cloning of cytokinin-specific binding protein from
RT mung bean (Vigna radiata).";
RL Eur. J. Biochem. 258:794-802(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. VC1973A;
RX PubMed=25384727; DOI=10.1038/ncomms6443;
RA Kang Y.J., Kim S.K., Kim M.Y., Lestari P., Kim K.H., Ha B.K., Jun T.H.,
RA Hwang W.J., Lee T., Lee J., Shim S., Yoon M.Y., Jang Y.E., Han K.S.,
RA Taeprayoon P., Yoon N., Somta P., Tanya P., Kim K.S., Gwag J.G., Moon J.K.,
RA Lee Y.H., Park B.S., Bombarely A., Doyle J.J., Jackson S.A.,
RA Schafleitner R., Srinives P., Varshney R.K., Lee S.H.;
RT "Genome sequence of mungbean and insights into evolution within Vigna
RT species.";
RL Nat. Commun. 5:5443-5443(2014).
RN [3]
RP SUBUNIT, AND PRELIMINARY CRYSTALLIZATION.
RX PubMed=12595714; DOI=10.1107/s0907444902022916;
RA Bujacz G.D., Pasternak O., Fujimoto Y., Hashimoto Y., Sikorski M.M.,
RA Jaskolski M.;
RT "Crystallization and preliminary crystallographic studies of mung bean
RT cytokinin-specific binding protein.";
RL Acta Crystallogr. D 59:522-525(2003).
RN [4]
RP ALLERGEN.
RX PubMed=21872913; DOI=10.1016/j.jaci.2011.07.007;
RA Dall'Antonia F., Gieras A., Devanaboyina S.C., Valenta R., Keller W.;
RT "Prediction of IgE-binding epitopes by means of allergen surface comparison
RT and correlation to cross-reactivity.";
RL J. Allergy Clin. Immunol. 128:872-879(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH TRANS-ZEATIN,
RP SUBUNIT, AND FUNCTION.
RX PubMed=16998071; DOI=10.1105/tpc.105.037119;
RA Pasternak O., Bujacz G.D., Fujimoto Y., Hashimoto Y., Jelen F.,
RA Otlewski J., Sikorski M.M., Jaskolski M.;
RT "Crystal structure of Vigna radiata cytokinin-specific binding protein in
RT complex with zeatin.";
RL Plant Cell 18:2622-2634(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH TRANS-ZEATIN, AND
RP FUNCTION.
RX PubMed=18453695; DOI=10.1107/s0907444908007853;
RA Pasternak O., Bujacz A., Biesiadka J., Bujacz G., Sikorski M.,
RA Jaskolski M.;
RT "MAD phasing using the (Ta6Br12)2+ cluster: a retrospective study.";
RL Acta Crystallogr. D 64:595-606(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) IN COMPLEX WITH GIBBERELLIN A3, AND
RP FUNCTION.
RX PubMed=25004979; DOI=10.1107/s1399004714010578;
RA Ruszkowski M., Sliwiak J., Ciesielska A., Barciszewski J., Sikorski M.,
RA Jaskolski M.;
RT "Specific binding of gibberellic acid by cytokinin-specific binding
RT proteins: a new aspect of plant hormone-binding proteins with the PR-10
RT fold.";
RL Acta Crystallogr. D 70:2032-2041(2014).
CC -!- FUNCTION: Binds the cytokinin trans-zeatin in vitro (PubMed:16998071,
CC PubMed:18453695). Binds gibberellin A3 (GA3) in vitro
CC (PubMed:25004979). {ECO:0000269|PubMed:16998071,
CC ECO:0000269|PubMed:18453695, ECO:0000269|PubMed:25004979}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12595714,
CC ECO:0000269|PubMed:16998071}.
CC -!- ALLERGEN: May cause an allergic reaction in human.
CC {ECO:0000305|PubMed:21872913}.
CC -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
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DR EMBL; AB012218; BAA74451.1; -; mRNA.
DR RefSeq; XP_014493319.1; XM_014637833.1.
DR PDB; 2FLH; X-ray; 1.20 A; A/B/C/D=1-155.
DR PDB; 3C0V; X-ray; 1.80 A; A/B/C/D=1-155.
DR PDB; 4PSB; X-ray; 1.42 A; A=1-155.
DR PDBsum; 2FLH; -.
DR PDBsum; 3C0V; -.
DR PDBsum; 4PSB; -.
DR AlphaFoldDB; A0A1S3THR8; -.
DR SMR; A0A1S3THR8; -.
DR STRING; 3916.A0A1S3THR8; -.
DR Allergome; 10102; Vig r 6.0101.
DR Allergome; 9728; Vig r 6.
DR EnsemblPlants; Vradi02g11210.1; Vradi02g11210.1; Vradi02g11210.
DR GeneID; 106755646; -.
DR Gramene; Vradi02g11210.1; Vradi02g11210.1; Vradi02g11210.
DR KEGG; vra:106755646; -.
DR Proteomes; UP000087766; Chromosome 2.
DR GO; GO:0010427; F:abscisic acid binding; IEA:InterPro.
DR GO; GO:0044373; F:cytokinin binding; IDA:UniProtKB.
DR GO; GO:0010331; F:gibberellin binding; IDA:UniProtKB.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:InterPro.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR000916; Bet_v_I/MLP.
DR InterPro; IPR024949; Bet_v_I_allergen.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF00407; Bet_v_1; 1.
DR PRINTS; PR00634; BETALLERGEN.
PE 1: Evidence at protein level;
KW 3D-structure; Allergen; Direct protein sequencing; Reference proteome.
FT CHAIN 1..155
FT /note="Phytohormone-binding protein CSBP"
FT /id="PRO_0000446055"
FT BINDING 22
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16998071,
FT ECO:0000269|PubMed:18453695, ECO:0007744|PDB:2FLH,
FT ECO:0007744|PDB:3C0V"
FT BINDING 67
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:25004979,
FT ECO:0007744|PDB:4PSB"
FT BINDING 67
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16998071,
FT ECO:0000269|PubMed:18453695, ECO:0007744|PDB:2FLH,
FT ECO:0007744|PDB:3C0V"
FT BINDING 69
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16998071,
FT ECO:0000269|PubMed:18453695, ECO:0007744|PDB:2FLH,
FT ECO:0007744|PDB:3C0V"
FT BINDING 139..142
FT /ligand="trans-zeatin"
FT /ligand_id="ChEBI:CHEBI:16522"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16998071,
FT ECO:0000269|PubMed:18453695, ECO:0007744|PDB:2FLH,
FT ECO:0007744|PDB:3C0V"
FT BINDING 139
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:25004979,
FT ECO:0007744|PDB:4PSB"
FT CONFLICT 92
FT /note="S -> N (in Ref. 1; BAA74451)"
FT /evidence="ECO:0000305"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:2FLH"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:2FLH"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:2FLH"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2FLH"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:2FLH"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:2FLH"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2FLH"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2FLH"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:2FLH"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:2FLH"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:2FLH"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:2FLH"
FT STRAND 96..108
FT /evidence="ECO:0007829|PDB:2FLH"
FT STRAND 111..121
FT /evidence="ECO:0007829|PDB:2FLH"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:3C0V"
FT HELIX 132..150
FT /evidence="ECO:0007829|PDB:2FLH"
SQ SEQUENCE 155 AA; 17595 MW; 0EB33AAC98A817C3 CRC64;
MVKEFNTQTE LSVRLEALWA VLSKDFITVV PKVLPHIVKD VQLIEGDGGV GTILIFNFLP
EVSPSYQREE ITEFDESSHE IGLQVIEGGY LSQGLSYYKT TFKLSEIEED KTLVNVKISY
DHDSDIEEKV TPTKTSQSTL MYLRRLERYL SNGSA
