THM2_THADA
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 25-MAY-2022, entry version 89.
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}.
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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 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; 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
