PHBP_MEDTR
ID PHBP_MEDTR Reviewed; 156 AA.
AC G7J032;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Phytohormone-binding protein {ECO:0000303|PubMed:25004979};
DE AltName: Full=Major pollen allergen Bet v 1-like protein {ECO:0000305};
DE AltName: Full=Pathogenesis-related PR10-like protein {ECO:0000305};
GN OrderedLocusNames=MTR_3g055120 {ECO:0000312|EMBL:AES70428.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.34 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 gibberellin A3 (GA3) in vitro.
CC {ECO:0000269|PubMed:25004979}.
CC -!- SIMILARITY: Belongs to the BetVI family. {ECO:0000305}.
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DR EMBL; CM001219; AES70428.1; -; Genomic_DNA.
DR EMBL; BT140779; AFK40574.1; -; mRNA.
DR RefSeq; XP_003600177.1; XM_003600129.2.
DR PDB; 4Q0K; X-ray; 1.34 A; A=1-156.
DR PDBsum; 4Q0K; -.
DR AlphaFoldDB; G7J032; -.
DR SMR; G7J032; -.
DR EnsemblPlants; AES70428; AES70428; MTR_3g055120.
DR GeneID; 11418550; -.
DR Gramene; AES70428; AES70428; MTR_3g055120.
DR eggNOG; ENOG502S34N; Eukaryota.
DR OMA; KISYDHE; -.
DR OrthoDB; 1505859at2759; -.
DR Proteomes; UP000002051; Chromosome 3.
DR ExpressionAtlas; G7J032; differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0010427; F:abscisic acid binding; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR000916; Bet_v_I/MLP.
DR InterPro; IPR023393; START-like_dom_sf.
DR Pfam; PF00407; Bet_v_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Gibberellin signaling pathway; Pathogenesis-related protein;
KW Plant defense; Reference proteome.
FT CHAIN 1..156
FT /note="Phytohormone-binding protein"
FT /id="PRO_0000429362"
FT BINDING 22
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:25004979,
FT ECO:0007744|PDB:4Q0K"
FT BINDING 68
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:25004979,
FT ECO:0007744|PDB:4Q0K"
FT BINDING 141
FT /ligand="gibberellin A3"
FT /ligand_id="ChEBI:CHEBI:58590"
FT /evidence="ECO:0000269|PubMed:25004979,
FT ECO:0007744|PDB:4Q0K"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:4Q0K"
FT HELIX 15..22
FT /evidence="ECO:0007829|PDB:4Q0K"
FT TURN 23..25
FT /evidence="ECO:0007829|PDB:4Q0K"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:4Q0K"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4Q0K"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:4Q0K"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4Q0K"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4Q0K"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4Q0K"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:4Q0K"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:4Q0K"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:4Q0K"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:4Q0K"
FT STRAND 97..109
FT /evidence="ECO:0007829|PDB:4Q0K"
FT STRAND 112..122
FT /evidence="ECO:0007829|PDB:4Q0K"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:4Q0K"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4Q0K"
FT HELIX 134..153
FT /evidence="ECO:0007829|PDB:4Q0K"
SQ SEQUENCE 156 AA; 17375 MW; 77BD8DE8181894B6 CRC64;
MIKEFNTQTT LNVGLEALWA AQSKDITLVV PKVLPNIVKD VQVIEGDGGV GTKLIFNFLP
GIAPVNYQRE VITEYDELSH TIGLQVVEGG YLNQGLSYYK TTFQFSAISE NKTLVNVKIS
YDHESELIEE KVKPTKTSES TLFYLGQLEK FLLNGA
