TLP_PRUAV
ID TLP_PRUAV Reviewed; 245 AA.
AC P50694;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Glucan endo-1,3-beta-glucosidase;
DE EC=3.2.1.39;
DE AltName: Full=(1->3)-beta-glucan endohydrolase;
DE Short=(1->3)-beta-glucanase;
DE AltName: Full=Allergen Pru a 2;
DE AltName: Full=Beta-1,3-endoglucanase;
DE AltName: Full=Thaumatin-like protein;
DE Short=TLP;
DE AltName: Allergen=Pru av 2;
DE Flags: Precursor;
OS Prunus avium (Cherry) (Cerasus avium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=42229;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Summit; TISSUE=Fruit;
RX PubMed=8685266; DOI=10.1104/pp.111.1.269;
RA Fils-Lycaon B.R., Wiersma P.A., Eastwell K.C., Sautiere P.;
RT "A cherry protein and its gene, abundantly expressed in ripening fruit,
RT have been identified as thaumatin-like.";
RL Plant Physiol. 111:269-273(1996).
RN [2]
RP PROTEIN SEQUENCE OF 24-45, AND ALLERGEN.
RX PubMed=9623505; DOI=10.1159/000023920;
RA Inschlag C., Hoffmann-Sommergruber K., O'Riordain G., Ahorn H., Ebner C.,
RA Scheiner O., Breiteneder H.;
RT "Biochemical characterization of Pru a 2, a 23-kD thaumatin-like protein
RT representing a potential major allergen in cherry (Prunus avium).";
RL Int. Arch. Allergy Immunol. 116:22-28(1998).
RN [3]
RP ENZYMATIC ACTIVITY.
RX PubMed=16499648; DOI=10.1111/j.1365-2222.2006.02439.x;
RA Fuchs H.C., Bohle B., Dall'Antonia Y., Radauer C.,
RA Hoffmann-Sommergruber K., Mari A., Scheiner O., Keller W., Breiteneder H.;
RT "Natural and recombinant molecules of the cherry allergen Pru av 2 show
RT diverse structural and B cell characteristics but similar T cell
RT reactivity.";
RL Clin. Exp. Allergy 36:359-368(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 24-245, AND DISULFIDE BONDS.
RX PubMed=16510989; DOI=10.1107/s1744309104033822;
RA Dall'Antonia Y., Pavkov T., Fuchs H., Breiteneder H., Keller W.;
RT "Crystallization and preliminary structure determination of the plant food
RT allergen Pru av 2.";
RL Acta Crystallogr. F 61:186-188(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000269|PubMed:16499648};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in ripening fruit.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds IgE in 50% of
CC cherry-allergic patients. {ECO:0000269|PubMed:9623505}.
CC -!- MISCELLANEOUS: Most abundant soluble protein in ripe cherries.
CC -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00699}.
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DR EMBL; U32440; AAB38064.1; -; mRNA.
DR PDB; 2AHN; X-ray; 1.30 A; A=24-245.
DR PDBsum; 2AHN; -.
DR AlphaFoldDB; P50694; -.
DR SMR; P50694; -.
DR Allergome; 3448; Pru av 2.0101.
DR Allergome; 598; Pru av 2.
DR EvolutionaryTrace; P50694; -.
DR Proteomes; UP000515124; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; 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; Allergen; Direct protein sequencing; Disulfide bond;
KW Glycosidase; Hydrolase; IgE-binding protein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:9623505"
FT CHAIN 24..245
FT /note="Glucan endo-1,3-beta-glucosidase"
FT /id="PRO_0000034021"
FT DISULFID 32..244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699,
FT ECO:0000269|PubMed:16510989"
FT DISULFID 80..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699,
FT ECO:0000269|PubMed:16510989"
FT DISULFID 95..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699,
FT ECO:0000269|PubMed:16510989"
FT DISULFID 150..233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699,
FT ECO:0000269|PubMed:16510989"
FT DISULFID 155..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699,
FT ECO:0000269|PubMed:16510989"
FT DISULFID 163..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699,
FT ECO:0000269|PubMed:16510989"
FT DISULFID 183..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699,
FT ECO:0000269|PubMed:16510989"
FT DISULFID 193..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699,
FT ECO:0000269|PubMed:16510989"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2AHN"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 68..82
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:2AHN"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:2AHN"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:2AHN"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:2AHN"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:2AHN"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:2AHN"
FT HELIX 207..215
FT /evidence="ECO:0007829|PDB:2AHN"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:2AHN"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:2AHN"
SQ SEQUENCE 245 AA; 25707 MW; BE045DF46FCEA7CE CRC64;
MMKTLVVVLS LSLTILSFGG AHAATISFKN NCPYMVWPGT LTSDQKPQLS TTGFELASQA
SFQLDTPVPW NGRFWARTGC STDASGKFVC ATADCASGQV MCNGNGAIPP ATLAEFNIPA
GGGQDFYDVS LVDGFNLPMS VTPQGGTGDC KTASCPANVN AVCPSELQKK GSDGSVVACL
SACVKFGTPQ YCCTPPQNTP ETCPPTNYSE IFHNACPDAY SYAYDDKRGT FTCNGGPNYA
ITFCP
