OLPA_TOBAC
ID OLPA_TOBAC Reviewed; 251 AA.
AC P25871;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Osmotin-like protein;
DE AltName: Full=Pathogenesis-related protein PR-5d;
DE Flags: Precursor;
GN Name=OLPA; Synonyms=OLP1;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun NN;
RX PubMed=16668481; DOI=10.1104/pp.97.2.844;
RA Takeda S., Sato F., Ida K., Yamada Y.;
RT "Nucleotide sequence of a cDNA for osmotin-like protein from cultured
RT tobacco cells.";
RL Plant Physiol. 97:844-846(1991).
RN [2]
RP PROTEIN SEQUENCE OF 22-60.
RA Takeda S., Sato F., Ida K., Yamada Y.;
RT "Characterization of polypeptides that accumulate in cultured Nicotiana
RT tabacum cells.";
RL Plant Cell Physiol. 31:215-221(1990).
RN [3]
RP CHARACTERIZATION, AND CRYSTALLIZATION.
RC STRAIN=cv. Samsun NN;
RX PubMed=9297844; DOI=10.1093/oxfordjournals.pcp.a029236;
RA Koiwa H., Kato H., Nakatsu T., Oda J., Yamada Y., Sato F.;
RT "Purification and characterization of tobacco pathogenesis-related protein
RT PR-5d, an antifungal thaumatin-like protein.";
RL Plant Cell Physiol. 38:783-791(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-229.
RC STRAIN=cv. Samsun NN;
RX PubMed=10047487; DOI=10.1006/jmbi.1998.2540;
RA Koiwa H., Kato H., Nakatsu T., Oda J., Yamada Y., Sato F.;
RT "Crystal structure of tobacco PR-5d protein at 1.8-A resolution reveals a
RT conserved acidic cleft structure in antifungal thaumatin-like proteins.";
RL J. Mol. Biol. 286:1137-1145(1999).
CC -!- INDUCTION: By tobacco mosaic virus infection and wounding.
CC -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00699}.
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; M64081; AAA34087.1; -; mRNA.
DR RefSeq; NP_001312513.1; NM_001325584.1.
DR PDB; 1AUN; X-ray; 1.80 A; A=22-229.
DR PDBsum; 1AUN; -.
DR AlphaFoldDB; P25871; -.
DR SMR; P25871; -.
DR GeneID; 107794478; -.
DR KEGG; nta:107794478; -.
DR OMA; NCHRILC; -.
DR EvolutionaryTrace; P25871; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0009607; P:response to biotic stimulus; IEA:UniProtKB-KW.
DR Gene3D; 2.60.110.10; -; 1.
DR InterPro; IPR037176; Osmotin/thaumatin-like_sf.
DR InterPro; IPR001938; Thaumatin.
DR InterPro; IPR017949; Thaumatin_CS.
DR PANTHER; PTHR31048; PTHR31048; 1.
DR Pfam; PF00314; Thaumatin; 1.
DR PIRSF; PIRSF002703; Thaumatin; 1.
DR PRINTS; PR00347; THAUMATIN.
DR SMART; SM00205; THN; 1.
DR SUPFAM; SSF49870; SSF49870; 1.
DR PROSITE; PS00316; THAUMATIN_1; 1.
DR PROSITE; PS51367; THAUMATIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Pathogenesis-related protein; Plant defense; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 22..251
FT /note="Osmotin-like protein"
FT /id="PRO_0000034042"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..226
FT DISULFID 73..83
FT DISULFID 88..94
FT DISULFID 142..214
FT DISULFID 147..197
FT DISULFID 155..165
FT DISULFID 169..178
FT DISULFID 179..184
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1AUN"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 64..75
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:1AUN"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:1AUN"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:1AUN"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:1AUN"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1AUN"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1AUN"
FT HELIX 188..196
FT /evidence="ECO:0007829|PDB:1AUN"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1AUN"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:1AUN"
SQ SEQUENCE 251 AA; 27652 MW; B743FDE634EDD004 CRC64;
MSHLTTFLVF FLLAFVTYTY ASGVFEVHNN CPYTVWAAAT PVGGGRRLER GQSWWFWAPP
GTKMARIWGR TNCNFDGAGR GWCQTGDCGG VLECKGWGKP PNTLAEYALN QFSNLDFWDI
SVIDGFNIPM SFGPTKPGPG KCHGIQCTAN INGECPGSLR VPGGCNNPCT TFGGQQYCCT
QGPCGPTELS RWFKQRCPDA YSYPQDDPTS TFTCTSWTTD YKVMFCPYGS AHNETTNFPL
EMPTSTHEVA K
