TLP1_PRUPE
ID TLP1_PRUPE Reviewed; 246 AA.
AC P83332;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Thaumatin-like protein 1;
DE AltName: Full=PpAZ44;
DE Flags: Precursor;
OS Prunus persica (Peach) (Amygdalus persica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3760 {ECO:0000312|EMBL:AAM00216.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=cv. Springcrest; TISSUE=Abscission zone;
RX PubMed=11847241; DOI=10.1093/jexbot/53.368.429;
RA Ruperti B., Cattivelli L., Pagni S., Ramina A.;
RT "Ethylene-responsive genes are differentially regulated during abscission,
RT organ senescence and wounding in peach (Prunus persica).";
RL J. Exp. Bot. 53:429-437(2002).
CC -!- FUNCTION: May be involved in protecting plant tissues from pathogen
CC infection. {ECO:0000303|PubMed:11847241}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Equally expressed in the abscission zone and
CC surrounding tissues of both fruitlets and leaves.
CC {ECO:0000269|PubMed:11847241}.
CC -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening but absent in
CC senescent leaves. {ECO:0000269|PubMed:11847241}.
CC -!- INDUCTION: Up-regulated in a tissue-independent manner following
CC treatment with propylene and wounding due to embryoctomy.
CC {ECO:0000269|PubMed:11847241}.
CC -!- SIMILARITY: Belongs to the thaumatin family.
CC {ECO:0000250|UniProtKB:P02883, ECO:0000255|PROSITE-ProRule:PRU00699}.
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DR EMBL; AF362988; AAM00216.1; -; mRNA.
DR AlphaFoldDB; P83332; -.
DR SMR; P83332; -.
DR STRING; 3760.EMJ17063; -.
DR Allergome; 5977; Pru p 2.
DR eggNOG; ENOG502QQ6D; Eukaryota.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006952; P:defense response; IEP:UniProtKB.
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 2: Evidence at transcript level;
KW Disulfide bond; Plant defense; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..246
FT /note="Thaumatin-like protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000034022"
FT DISULFID 33..245
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 81..91
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 96..103
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 151..234
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 156..217
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 164..180
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 184..193
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 194..204
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
SQ SEQUENCE 246 AA; 25765 MW; EDEEBB6004314B82 CRC64;
MMKSQAALLG LTTLAILFFS GAHAAKITFT NKCSYTVWPG TLTGDQKPQL SLTGFELATG
ISRSVDAPSP WSGRFFGRTR CSTDASGKFT CATADCGSGQ VSCNGNGAAP PATLVEITIA
SNGGQDFYDV SLVDGFNLPM SVAPQGGTGK CKASTCPADI NKVCPAPLQV KGSDGSVIAC
KSACLAFNQP KYCCTPPNDK PETCPPPDYS KLFKTQCPQA YSYAYDDKSS TFTCSGRPAY
LITFCP