TLP1_PYRPY
ID TLP1_PYRPY Reviewed; 244 AA.
AC O80327;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Thaumatin-like protein 1;
DE Flags: Precursor;
GN Name=TL1;
OS Pyrus pyrifolia (Chinese pear) (Pyrus serotina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX NCBI_TaxID=3767 {ECO:0000312|EMBL:BAA28872.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-32, DEVELOPMENTAL STAGE,
RP TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC STRAIN=cv. Hosui; TISSUE=Style;
RX PubMed=9684355; DOI=10.1007/s004250050350;
RA Sassa H., Hirano H.;
RT "Style-specific and developmentally regulated accumulation of a
RT glycosylated thaumatin/PR5-like protein in Japanese pear (Pyrus serotina
RT Rehd.).";
RL Planta 205:514-521(1998).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Style. {ECO:0000269|PubMed:9684355}.
CC -!- DEVELOPMENTAL STAGE: Accumulates following maturation of flower buds.
CC {ECO:0000269|PubMed:9684355}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9684355}.
CC -!- SIMILARITY: Belongs to the thaumatin family.
CC {ECO:0000250|UniProtKB:P02883, ECO:0000255|PROSITE-ProRule:PRU00699}.
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DR EMBL; AB006009; BAA28872.1; -; mRNA.
DR AlphaFoldDB; O80327; -.
DR SMR; O80327; -.
DR iPTMnet; O80327; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Direct protein sequencing; Disulfide bond; Glycoprotein; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:9684355"
FT CHAIN 23..244
FT /note="Thaumatin-like protein 1"
FT /evidence="ECO:0000269|PubMed:9684355"
FT /id="PRO_0000034024"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:9684355"
FT DISULFID 31..243
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 79..89
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 94..101
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 149..232
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 154..215
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 162..178
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 182..191
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 192..202
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
SQ SEQUENCE 244 AA; 25308 MW; AC9C1372EB0763CD CRC64;
MKFEALIGLV LVFLSEHAGV YSAKFTFTNK CPNTVWPGTL TGGGGPQLLS TGFELASGAS
TSLTVQAPWS GRFWGRSHCS IDSSGKFKCS TGDCGSGQIS CNGAGASPPA SLVELTLATN
GGQDFYDVSL VDGFNLPIKL APRGGSGDCN STSCAANINT VCPAELSDKG SDGSVIGCKS
ACLALNQPQY CCTGAYGTPD TCPPTDFSKV FKNQCPQAYS YAYDDKSSTF TCFGGPNYEI
TFCP
