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Protein

Thaumatin-1

Gene
N/A
Organism
Thaumatococcus daniellii (Katemfe) (Phrynium daniellii)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Taste-modifying protein; intensely sweet-tasting. It is 100000 times sweeter than sucrose on a molar basis.

Keywords - Molecular functioni

Taste-modifying protein

Names & Taxonomyi

Protein namesi
Recommended name:
Thaumatin-1
Alternative name(s):
Thaumatin I
OrganismiThaumatococcus daniellii (Katemfe) (Phrynium daniellii)
Taxonomic identifieri4621 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaZingiberalesMarantaceaeThaumatococcus

Subcellular locationi

  1. Cytoplasmic vesicle

  2. Note: Thaumatin accumulates in vesicle-like organelles.

GO - Cellular componenti

  1. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle

Pathology & Biotechi

Protein family/group databases

Allergomei9233. Tha da TLP.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 207207Thaumatin-1PRO_0000096221Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi9 ↔ 204PROSITE-ProRule annotation1 Publication
Disulfide bondi56 ↔ 66PROSITE-ProRule annotation1 Publication
Disulfide bondi71 ↔ 77PROSITE-ProRule annotation1 Publication
Disulfide bondi121 ↔ 193PROSITE-ProRule annotation1 Publication
Disulfide bondi126 ↔ 177PROSITE-ProRule annotation1 Publication
Disulfide bondi134 ↔ 145PROSITE-ProRule annotation1 Publication
Disulfide bondi149 ↔ 158PROSITE-ProRule annotation1 Publication
Disulfide bondi159 ↔ 164PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
207
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Beta strandi9 – 113Combined sources
Beta strandi13 – 186Combined sources
Beta strandi20 – 3112Combined sources
Beta strandi36 – 405Combined sources
Beta strandi47 – 559Combined sources
Beta strandi62 – 654Combined sources
Beta strandi67 – 693Combined sources
Beta strandi74 – 763Combined sources
Beta strandi87 – 948Combined sources
Beta strandi97 – 1037Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi112 – 1209Combined sources
Beta strandi124 – 1263Combined sources
Helixi130 – 1334Combined sources
Helixi136 – 1383Combined sources
Beta strandi143 – 1453Combined sources
Helixi148 – 1525Combined sources
Helixi155 – 1584Combined sources
Turni159 – 1613Combined sources
Helixi168 – 1769Combined sources
Beta strandi180 – 1834Combined sources
Beta strandi191 – 1944Combined sources
Beta strandi199 – 2046Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KWNX-ray1.20A1-207[»]
1LR2X-ray1.80A1-207[»]
1LR3X-ray1.80A1-207[»]
1LXZX-ray1.25A1-207[»]
1LY0X-ray1.36A1-207[»]
1PP3X-ray1.60A/B1-207[»]
1RQWX-ray1.05A1-207[»]
1THIX-ray3.20A1-207[»]
1THUX-ray2.60A1-207[»]
1THVX-ray1.75A1-207[»]
1THWX-ray1.75A1-207[»]
2A7IX-ray1.75X1-207[»]
2BLRX-ray1.40A1-206[»]
2BLUX-ray1.40A1-206[»]
2D8OX-ray2.38A1-207[»]
2D8PX-ray2.30A1-207[»]
2G4YX-ray1.98A1-207[»]
2OQNX-ray1.90A1-207[»]
2PE7X-ray1.46A1-207[»]
2VHKX-ray0.94A1-206[»]
2VHRX-ray0.95A1-207[»]
2VI1X-ray1.04A1-207[»]
2VI2X-ray1.08A1-207[»]
2VI3X-ray0.98A1-207[»]
2VI4X-ray1.10A1-207[»]
2VU6X-ray0.95A1-207[»]
2VU7X-ray1.08A1-207[»]
2WBZX-ray1.60A1-206[»]
3AL7X-ray1.10A1-207[»]
3ALDX-ray1.10A1-207[»]
3DZNX-ray1.51A1-207[»]
3DZPX-ray1.51A1-207[»]
3DZRX-ray1.51A1-207[»]
3E0AX-ray1.51A1-207[»]
3E3SX-ray1.73A1-207[»]
3N02X-ray1.50A1-206[»]
3N03X-ray1.50A1-206[»]
3QY5X-ray1.25A1-207[»]
3V7VX-ray2.30A1-207[»]
3V82X-ray2.30A1-207[»]
3V84X-ray2.30A1-207[»]
3V87X-ray2.30A1-207[»]
3V88X-ray2.30A1-207[»]
3V8AX-ray2.30A1-207[»]
3VCEX-ray2.30A1-207[»]
3VCGX-ray2.30A1-207[»]
3VCHX-ray2.30A1-207[»]
3VCIX-ray2.30A1-207[»]
3VCJX-ray2.30A1-207[»]
3VCKX-ray2.30A1-207[»]
3VHFX-ray1.39A1-207[»]
3VHGX-ray1.00A1-207[»]
3VJQX-ray1.00A1-207[»]
3ZEJX-ray1.55A1-207[»]
4AXRX-ray1.38A1-207[»]
4AXUX-ray1.38A1-206[»]
4BALX-ray1.30A1-207[»]
4BARX-ray1.20A1-207[»]
4C3CX-ray1.80A1-207[»]
4DC5X-ray1.48A1-207[»]
4DC6X-ray1.48A1-207[»]
4DIYX-ray1.98A1-207[»]
4DIZX-ray1.98A1-207[»]
4DJ0X-ray1.98A1-207[»]
4DJ1X-ray1.98A1-207[»]
4EK0X-ray1.52A1-207[»]
4EKAX-ray1.55A1-207[»]
4EKBX-ray1.52A1-207[»]
4EKHX-ray1.75A1-207[»]
4EKOX-ray1.52A1-207[»]
4EKTX-ray1.75A1-207[»]
4EL2X-ray1.52A1-207[»]
4EL3X-ray1.95A1-207[»]
4EL7X-ray1.52A1-207[»]
4ELAX-ray2.00A1-207[»]
4TVTX-ray1.20A1-207[»]
ProteinModelPortaliP02883.
SMRiP02883. Positions 1-207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02883.

Family & Domainsi

Sequence similaritiesi

Belongs to the thaumatin family.PROSITE-ProRule annotation

Family and domain databases

Gene3Di2.60.110.10. 1 hit.
InterProiIPR001938. Thaumatin.
IPR017949. Thaumatin_CS.
[Graphical view]
PANTHERiPTHR31048. PTHR31048. 1 hit.
PfamiPF00314. Thaumatin. 1 hit.
[Graphical view]
PIRSFiPIRSF002703. Thaumatin. 1 hit.
PRINTSiPR00347. THAUMATIN.
SMARTiSM00205. THN. 1 hit.
[Graphical view]
SUPFAMiSSF49870. SSF49870. 1 hit.
PROSITEiPS00316. THAUMATIN_1. 1 hit.
PS51367. THAUMATIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P02883-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ATFEIVNRCS YTVWAAASKG DAALDAGGRQ LNSGESWTIN VEPGTNGGKI
60 70 80 90 100
WARTDCYFDD SGSGICKTGD CGGLLRCKRF GRPPTTLAEF SLNQYGKDYI
110 120 130 140 150
DISNIKGFNV PMNFSPTTRG CRGVRCAADI VGQCPAKLKA PGGGCNDACT
160 170 180 190 200
VFQTSEYCCT TGKCGPTEYS RFFKRLCPDA FSYVLDKPTT VTCPGSSNYR

VTFCPTA
Length:207
Mass (Da):22,204
Last modified:July 21, 1986 - v1
Checksum:i9C3288F1873FB32B
GO

Sequence databases

PIRiA03377. QTTC1.

Cross-referencesi

Sequence databases

PIRiA03377. QTTC1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KWNX-ray1.20A1-207[»]
1LR2X-ray1.80A1-207[»]
1LR3X-ray1.80A1-207[»]
1LXZX-ray1.25A1-207[»]
1LY0X-ray1.36A1-207[»]
1PP3X-ray1.60A/B1-207[»]
1RQWX-ray1.05A1-207[»]
1THIX-ray3.20A1-207[»]
1THUX-ray2.60A1-207[»]
1THVX-ray1.75A1-207[»]
1THWX-ray1.75A1-207[»]
2A7IX-ray1.75X1-207[»]
2BLRX-ray1.40A1-206[»]
2BLUX-ray1.40A1-206[»]
2D8OX-ray2.38A1-207[»]
2D8PX-ray2.30A1-207[»]
2G4YX-ray1.98A1-207[»]
2OQNX-ray1.90A1-207[»]
2PE7X-ray1.46A1-207[»]
2VHKX-ray0.94A1-206[»]
2VHRX-ray0.95A1-207[»]
2VI1X-ray1.04A1-207[»]
2VI2X-ray1.08A1-207[»]
2VI3X-ray0.98A1-207[»]
2VI4X-ray1.10A1-207[»]
2VU6X-ray0.95A1-207[»]
2VU7X-ray1.08A1-207[»]
2WBZX-ray1.60A1-206[»]
3AL7X-ray1.10A1-207[»]
3ALDX-ray1.10A1-207[»]
3DZNX-ray1.51A1-207[»]
3DZPX-ray1.51A1-207[»]
3DZRX-ray1.51A1-207[»]
3E0AX-ray1.51A1-207[»]
3E3SX-ray1.73A1-207[»]
3N02X-ray1.50A1-206[»]
3N03X-ray1.50A1-206[»]
3QY5X-ray1.25A1-207[»]
3V7VX-ray2.30A1-207[»]
3V82X-ray2.30A1-207[»]
3V84X-ray2.30A1-207[»]
3V87X-ray2.30A1-207[»]
3V88X-ray2.30A1-207[»]
3V8AX-ray2.30A1-207[»]
3VCEX-ray2.30A1-207[»]
3VCGX-ray2.30A1-207[»]
3VCHX-ray2.30A1-207[»]
3VCIX-ray2.30A1-207[»]
3VCJX-ray2.30A1-207[»]
3VCKX-ray2.30A1-207[»]
3VHFX-ray1.39A1-207[»]
3VHGX-ray1.00A1-207[»]
3VJQX-ray1.00A1-207[»]
3ZEJX-ray1.55A1-207[»]
4AXRX-ray1.38A1-207[»]
4AXUX-ray1.38A1-206[»]
4BALX-ray1.30A1-207[»]
4BARX-ray1.20A1-207[»]
4C3CX-ray1.80A1-207[»]
4DC5X-ray1.48A1-207[»]
4DC6X-ray1.48A1-207[»]
4DIYX-ray1.98A1-207[»]
4DIZX-ray1.98A1-207[»]
4DJ0X-ray1.98A1-207[»]
4DJ1X-ray1.98A1-207[»]
4EK0X-ray1.52A1-207[»]
4EKAX-ray1.55A1-207[»]
4EKBX-ray1.52A1-207[»]
4EKHX-ray1.75A1-207[»]
4EKOX-ray1.52A1-207[»]
4EKTX-ray1.75A1-207[»]
4EL2X-ray1.52A1-207[»]
4EL3X-ray1.95A1-207[»]
4EL7X-ray1.52A1-207[»]
4ELAX-ray2.00A1-207[»]
4TVTX-ray1.20A1-207[»]
ProteinModelPortaliP02883.
SMRiP02883. Positions 1-207.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei9233. Tha da TLP.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02883.

Family and domain databases

Gene3Di2.60.110.10. 1 hit.
InterProiIPR001938. Thaumatin.
IPR017949. Thaumatin_CS.
[Graphical view]
PANTHERiPTHR31048. PTHR31048. 1 hit.
PfamiPF00314. Thaumatin. 1 hit.
[Graphical view]
PIRSFiPIRSF002703. Thaumatin. 1 hit.
PRINTSiPR00347. THAUMATIN.
SMARTiSM00205. THN. 1 hit.
[Graphical view]
SUPFAMiSSF49870. SSF49870. 1 hit.
PROSITEiPS00316. THAUMATIN_1. 1 hit.
PS51367. THAUMATIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: PROTEIN SEQUENCE.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  3. "X-ray analysis of new crystal forms of the sweet protein thaumatin."
    McPherson A., Weickmann J.
    J. Biomol. Struct. Dyn. 7:1053-1060(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  4. "Crystal structure of a sweet tasting protein thaumatin I, at 1.65-A resolution."
    Ogata C.M., Gordon P.F., de Vos A.M., Kim S.-H.
    J. Mol. Biol. 228:893-908(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).

Entry informationi

Entry nameiTHM1_THADA
AccessioniPrimary (citable) accession number: P02883
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 7, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.