ID THM2_THADA Reviewed; 235 AA. AC P02884; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 22-FEB-2023, entry version 91. DE RecName: Full=Thaumatin II {ECO:0000303|PubMed:7049841}; DE AltName: Full=Thaumatin-2 {ECO:0000305}; DE Flags: Precursor; OS Thaumatococcus daniellii (Katemfe) (Phrynium daniellii). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Marantaceae; OC Thaumatococcus. OX NCBI_TaxID=4621; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=7049841; DOI=10.1016/0378-1119(82)90050-6; RA Edens L., Heslinga L., Klok R., Ledeboer A.M., Maat J., Toonen M.Y., RA Visser C., Verrips C.T.; RT "Cloning of cDNA encoding the sweet-tasting plant protein thaumatin and its RT expression in Escherichia coli."; RL Gene 18:1-12(1982). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF 23-229, AND DISULFIDE BONDS. RX PubMed=21672520; DOI=10.1016/j.bbrc.2011.05.158; RA Masuda T., Ohta K., Tani F., Mikami B., Kitabatake N.; RT "Crystal structure of the sweet-tasting protein thaumatin II at 1.27A."; RL Biochem. Biophys. Res. Commun. 410:457-460(2011). RN [3] RP X-RAY CRYSTALLOGRAPHY (0.99 ANGSTROMS) OF 23-229, AND DISULFIDE BONDS. RX PubMed=25066915; DOI=10.1016/j.biochi.2014.07.016; RA Masuda T., Mikami B., Tani F.; RT "Atomic structure of recombinant thaumatin II reveals flexible RT conformations in two residues critical for sweetness and three consecutive RT glycine residues."; RL Biochimie 106:33-38(2014). CC -!- FUNCTION: Taste-modifying protein; intensely sweet-tasting. It is CC 100000 times sweeter than sucrose on a molar basis. CC {ECO:0000305|PubMed:7049841}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Note=Thaumatin accumulates CC in vesicle-like organelles. {ECO:0000305}. 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; J01209; AAA93095.1; -; mRNA. DR PIR; A03378; QTTC2. DR PDB; 3AOK; X-ray; 1.27 A; A=23-229. DR PDB; 3WOU; X-ray; 0.99 A; A=23-229. DR PDBsum; 3AOK; -. DR PDBsum; 3WOU; -. DR AlphaFoldDB; P02884; -. DR SMR; P02884; -. DR Allergome; 9233; Tha da TLP. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR CDD; cd09217; TLP-P; 1. DR Gene3D; 2.60.110.10; Thaumatin; 1. DR InterPro; IPR037176; Osmotin/thaumatin-like_sf. DR InterPro; IPR001938; Thaumatin. DR InterPro; IPR017949; Thaumatin_CS. DR PANTHER; PTHR31048; OS03G0233200 PROTEIN; 1. DR PANTHER; PTHR31048:SF47; PROTEIN P21; 1. DR Pfam; PF00314; Thaumatin; 1. DR PIRSF; PIRSF002703; Thaumatin; 1. DR PRINTS; PR00347; THAUMATIN. DR SMART; SM00205; THN; 1. DR SUPFAM; SSF49870; Osmotin, thaumatin-like protein; 1. DR PROSITE; PS00316; THAUMATIN_1; 1. DR PROSITE; PS51367; THAUMATIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasmic vesicle; Disulfide bond; Signal; KW Taste-modifying protein. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..229 FT /note="Thaumatin II" FT /id="PRO_0000034017" FT PROPEP 230..235 FT /note="Removed in mature form" FT /evidence="ECO:0000305" FT /id="PRO_0000034018" FT DISULFID 31..226 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:21672520, ECO:0000269|PubMed:25066915, FT ECO:0007744|PDB:3AOK, ECO:0007744|PDB:3WOU" FT DISULFID 78..88 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:21672520, ECO:0000269|PubMed:25066915, FT ECO:0007744|PDB:3AOK, ECO:0007744|PDB:3WOU" FT DISULFID 93..99 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:21672520, ECO:0000269|PubMed:25066915, FT ECO:0007744|PDB:3AOK, ECO:0007744|PDB:3WOU" FT DISULFID 143..215 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:21672520, ECO:0000269|PubMed:25066915, FT ECO:0007744|PDB:3AOK, ECO:0007744|PDB:3WOU" FT DISULFID 148..199 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:21672520, ECO:0000269|PubMed:25066915, FT ECO:0007744|PDB:3AOK, ECO:0007744|PDB:3WOU" FT DISULFID 156..167 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:21672520, ECO:0000269|PubMed:25066915, FT ECO:0007744|PDB:3AOK, ECO:0007744|PDB:3WOU" FT DISULFID 171..180 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:21672520, ECO:0000269|PubMed:25066915, FT ECO:0007744|PDB:3AOK, ECO:0007744|PDB:3WOU" FT DISULFID 181..186 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699, FT ECO:0000269|PubMed:21672520, ECO:0000269|PubMed:25066915, FT ECO:0007744|PDB:3AOK, ECO:0007744|PDB:3WOU" FT STRAND 24..29 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 42..53 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 69..80 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 84..91 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 96..98 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 109..116 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 119..125 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 134..143 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 146..148 FT /evidence="ECO:0007829|PDB:3WOU" FT HELIX 152..155 FT /evidence="ECO:0007829|PDB:3WOU" FT HELIX 158..160 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:3WOU" FT HELIX 170..174 FT /evidence="ECO:0007829|PDB:3WOU" FT HELIX 177..180 FT /evidence="ECO:0007829|PDB:3WOU" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:3WOU" FT HELIX 190..198 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:3WOU" FT STRAND 221..226 FT /evidence="ECO:0007829|PDB:3WOU" SQ SEQUENCE 235 AA; 25523 MW; 15E9DA82554D7A75 CRC64; MAATTCFFFL FPFLLLLTLS RAATFEIVNR CSYTVWAAAS KGDAALDAGG RQLNSGESWT INVEPGTKGG KIWARTDCYF DDSGRGICRT GDCGGLLQCK RFGRPPTTLA EFSLNQYGKD YIDISNIKGF NVPMDFSPTT RGCRGVRCAA DIVGQCPAKL KAPGGGCNDA CTVFQTSEYC CTTGKCGPTE YSRFFKRLCP DAFSYVLDKP TTVTCPGSSN YRVTFCPTAL ELEDE //