TLP2_PRUPE
ID TLP2_PRUPE Reviewed; 242 AA.
AC P83335;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Thaumatin-like protein 2;
DE AltName: Full=PpAZ8;
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:AAM00215.1};
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: Preferentially expressed in the abscission zone of
CC fruit. Also expressed in leaf abscission zone.
CC {ECO:0000269|PubMed:11847241}.
CC -!- DEVELOPMENTAL STAGE: Expressed during leaf senescence but not during
CC fruit ripening. {ECO:0000269|PubMed:11847241}.
CC -!- INDUCTION: Up-regulated in the abscission zone following treatment with
CC propylene and in both the abscission zone and surrounding tissues after
CC wounding due to embryoctomy. {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; AAM00215.1; -; mRNA.
DR AlphaFoldDB; P83335; -.
DR SMR; P83335; -.
DR STRING; 3760.EMJ03695; -.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..242
FT /note="Thaumatin-like protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000034023"
FT DISULFID 32..241
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 77..87
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 92..99
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 147..230
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 152..213
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 160..176
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 180..189
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 190..200
FT /evidence="ECO:0000250|UniProtKB:P02883,
FT ECO:0000255|PROSITE-ProRule:PRU00699"
SQ SEQUENCE 242 AA; 25608 MW; 72E0D5CD94F9F3C5 CRC64;
MMKTLGAVLS LSLTLLSFGG AHAATMSFKN NCPYTVWPAS FGNPQLSTTG FELASQASFQ
LDTPVPWSGR FWARTRCSTD ASGKFVCETA DCDSGQLMCN GKTGIPPATL AEFTIAAGGG
QDFYDVSLVD GFNLPMSVTP QGGTGTCKMG SCAANVNLVC PSELQKIGSD GSVVACLSAC
VKFGEPQYCC TPPQETKEKC PPTNYSQIFH EQCPDAYSYA FDDNKGLFTC SGGPNYLITF
CP