DR206_PEA
ID DR206_PEA Reviewed; 184 AA.
AC P13240;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Disease resistance response protein 206;
DE AltName: Full=Dirigent protein PI206;
DE Flags: Precursor;
GN Name=PI206;
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 [GENOMIC DNA].
RC STRAIN=cv. Alcan;
RX PubMed=7870833; DOI=10.1104/pp.107.1.301;
RA Culley D.E., Horovitz D., Hadwiger L.A.;
RT "Molecular characterization of disease-resistance response gene DRR206-d
RT from Pisum sativum (L.).";
RL Plant Physiol. 107:301-302(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-184.
RC STRAIN=cv. Alaska;
RX AGRICOLA=IND92000015; DOI=10.1007/BF00017470;
RA Fristensky B.W., Horovitz D., Hadwiger L.A.;
RT "cDNA sequences for pea disease resistance response genes.";
RL Plant Mol. Biol. 11:713-715(1988).
CC -!- FUNCTION: Dirigent proteins impart stereoselectivity on the phenoxy
CC radical-coupling reaction, yielding optically active lignans from two
CC molecules of coniferyl alcohol in the biosynthesis of lignans,
CC flavonolignans, and alkaloids and thus plays a central role in plant
CC secondary metabolism. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250}.
CC -!- INDUCTION: Upon contact with the plant pathogens fungus Fusarium
CC solani, Pseudomonas syringae pv pisi, and the fungal elicitor chitosan.
CC -!- SIMILARITY: Belongs to the plant dirigent protein family.
CC {ECO:0000305}.
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DR EMBL; U11716; AAB18669.1; -; Unassigned_DNA.
DR EMBL; M18250; AAA33662.1; -; mRNA.
DR PIR; T06433; T06433.
DR PDB; 4REV; X-ray; 1.95 A; A/B=21-184.
DR PDBsum; 4REV; -.
DR AlphaFoldDB; P13240; -.
DR SMR; P13240; -.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IEA:UniProt.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR Gene3D; 2.40.480.10; -; 1.
DR InterPro; IPR044859; Allene_oxi_cyc_Dirigent.
DR InterPro; IPR004265; Dirigent.
DR PANTHER; PTHR46442; PTHR46442; 1.
DR Pfam; PF03018; Dirigent; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoplast; Disulfide bond; Glycoprotein;
KW Pathogenesis-related protein; Plant defense; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..184
FT /note="Disease resistance response protein 206"
FT /id="PRO_0000080000"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..183
FT /evidence="ECO:0000250"
FT STRAND 31..41
FT /evidence="ECO:0007829|PDB:4REV"
FT STRAND 75..88
FT /evidence="ECO:0007829|PDB:4REV"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:4REV"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:4REV"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:4REV"
FT STRAND 140..150
FT /evidence="ECO:0007829|PDB:4REV"
FT TURN 151..154
FT /evidence="ECO:0007829|PDB:4REV"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:4REV"
FT STRAND 171..182
FT /evidence="ECO:0007829|PDB:4REV"
SQ SEQUENCE 184 AA; 20371 MW; 74D69009356DA343 CRC64;
MGSKLLVLFV FVMLFALSSA IPNKRKPYKP CKNLVFYFHD ILYNGKNAAN ATSAIVAAPE
GVSLTKLAPQ SHFGNIIVFD DPITLSHSLS SKQVGRAQGF YIYDTKNTYT SWLSFTFVLN
STHHQGTITF AGADPIVAKT RDISVTGGTG DFFMHRGIAT ITTDAFEGEA YFRLGVYIKF
FECW