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TLP1_MANZA
ID   TLP1_MANZA              Reviewed;         207 AA.
AC   G5DC91; B3EWX8;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 2.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Thaumatin-like protein 1 {ECO:0000250|UniProtKB:P83332};
DE            EC=3.2.1.-;
DE   AltName: Full=Acidic thaumatin-like protein {ECO:0000312|EMBL:AEP84104.1};
DE   AltName: Full=Beta-1,3-glucanase;
DE   AltName: Full=Thaumatin-like protein 1b;
GN   Name=TLP1; Synonyms=TLP 1b;
OS   Manilkara zapota (Sapodilla plum) (Achras zapota).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Sapotaceae; Sapotoideae; Manilkara.
OX   NCBI_TaxID=3741;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-25, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-207,
RP   FUNCTION, SUBUNIT, ALLERGENICITY, AND LACK OF GLYCOSYLATION.
RC   STRAIN=cv. Cricket Ball; TISSUE=Fruit, and Leaf;
RX   PubMed=24060761; DOI=10.2332/allergolint.12-oa-0522;
RA   Ashok Kumar H.G., Hegde V.L., Shetty S.M., Venkatesh Y.P.;
RT   "Characterization and gene cloning of an acidic thaumatin-like protein (TLP
RT   1), an allergen from sapodilla fruit (Manilkara zapota).";
RL   Allergol. Int. 62:447-462(2013).
RN   [2]
RP   3D-STRUCTURE MODELING, AND ALLERGENICITY.
RX   PubMed=24091295; DOI=10.1016/j.molimm.2013.08.010;
RA   Ashok Kumar H.G., Venkatesh Y.P.;
RT   "In silico analyses of structural and allergenicity features of sapodilla
RT   (Manilkara zapota) acidic thaumatin-like protein in comparison with
RT   allergenic plant TLPs.";
RL   Mol. Immunol. 57:119-128(2014).
CC   -!- FUNCTION: Acidic thaumatin-like protein. Exhibits weak beta-1,3-
CC       glucanase activity with laminarin as substrate.
CC       {ECO:0000269|PubMed:24060761}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:24060761}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: Not glycosylated.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:24060761, ECO:0000269|PubMed:24091295}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 4.4.
CC   -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00699}.
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DR   EMBL; JN624813; AEP84104.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5DC91; -.
DR   SMR; G5DC91; -.
DR   Allergome; 11650; Man za TLP.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
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   Allergen; Direct protein sequencing; Disulfide bond; Glycosidase;
KW   Hydrolase; Pathogenesis-related protein; Plant defense; Secreted.
FT   CHAIN           1..207
FT                   /note="Thaumatin-like protein 1"
FT                   /id="PRO_0000415951"
FT   DISULFID        9..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        50..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        65..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        117..191
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        122..174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        130..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        144..153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT   DISULFID        154..161
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
SQ   SEQUENCE   207 AA;  21922 MW;  932278F6CC883424 CRC64;
     ATFDVVNQCT FTVWAGASPG GGKQLDQGQT WTITVAPGST KARIWGRTGC NFDANGQGKC
     QTGDCNGLLQ CQGYGSPPNT LAEFSLNQPN NLDYVDISLV DGFNIPMDFS PAAAGVCKDI
     RCATDITAQC PAELQAPGGC NNPCTVYKTN EYCCTNGQGT CGPTALSKFF KDRCPDAYSY
     PQDDPTSLFT CPAGTNYKVV FCPNLDA
 
 
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