TP1A_MALDO
ID TP1A_MALDO Reviewed; 246 AA.
AC Q9FSG7; O82546;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Thaumatin-like protein 1a;
DE AltName: Full=Mdtl1;
DE AltName: Full=Pathogenesis-related protein 5a;
DE Short=PR-5a;
DE AltName: Allergen=Mal d 2;
DE Flags: Precursor;
GN Name=TL1; Synonyms=TL;
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000312|EMBL:CAC10270.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Fuji;
RX PubMed=10737193; DOI=10.1271/bbb.64.355;
RA Oh D.H., Song K.J., Shin Y.U., Chung W.I.;
RT "Isolation of a cDNA encoding a 31-kDa, pathogenesis-related 5/thaumatin-
RT like (PR5/TL) protein abundantly expressed in apple fruit (Nalus domestica
RT cv. Fuji).";
RL Biosci. Biotechnol. Biochem. 64:355-362(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Golden Delicious; TISSUE=Pericarp;
RX PubMed=12787673; DOI=10.1016/s0022-2836(03)00403-0;
RA Krebitz M., Wagner B., Ferreira F., Peterbauer C., Campillo N., Witty M.,
RA Kolarich D., Steinkellner H., Scheiner O., Breiteneder H.;
RT "Plant-based heterologous expression of Mal d 2, a thaumatin-like protein
RT and allergen of apple (Malus domestica), and its characterization as an
RT antifungal protein.";
RL J. Mol. Biol. 329:721-730(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-246.
RC STRAIN=cv. Evereste X MM106; TISSUE=Leaf;
RX PubMed=12481992; DOI=10.1094/mpmi.2002.15.12.1204;
RA Venisse J.-S., Malnoy M., Faize M., Paulin J.-P., Brisset M.-N.;
RT "Modulation of defense responses of Malus spp. during compatible and
RT incompatible interactions with Erwinia amylovora.";
RL Mol. Plant Microbe Interact. 15:1204-1212(2002).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Important allergen of
CC apple fruits that is associated with IgE-mediated symptoms in apple
CC allergic individuals.
CC -!- SIMILARITY: Belongs to the thaumatin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00699}.
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DR EMBL; AF090143; AAC36740.1; -; mRNA.
DR EMBL; AJ243427; CAC10270.1; -; mRNA.
DR EMBL; AF494393; AAM12886.1; -; mRNA.
DR RefSeq; NP_001315714.1; NM_001328785.1.
DR PDB; 3ZS3; X-ray; 1.80 A; A=25-246.
DR PDBsum; 3ZS3; -.
DR AlphaFoldDB; Q9FSG7; -.
DR SMR; Q9FSG7; -.
DR STRING; 3750.XP_008348588.1; -.
DR Allergome; 3360; Mal d 2.0101.
DR Allergome; 465; Mal d 2.
DR GeneID; 103411735; -.
DR KEGG; mdm:103411735; -.
DR OrthoDB; 1135904at2759; -.
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 3D-structure; Allergen; Disulfide bond; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..246
FT /note="Thaumatin-like protein 1a"
FT /id="PRO_0000034048"
FT DISULFID 33..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 81..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 96..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 151..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 156..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 164..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 184..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT DISULFID 194..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00699"
FT CONFLICT 8..17
FT /note="SLLGLTLAIL -> PRPTLAILF (in Ref. 1; AAC36740)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="Y -> F (in Ref. 3; AAM12886)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="V -> A (in Ref. 3; AAM12886)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="P -> Q (in Ref. 3; AAM12886)"
FT /evidence="ECO:0000305"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 69..83
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:3ZS3"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3ZS3"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:3ZS3"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:3ZS3"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:3ZS3"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:3ZS3"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3ZS3"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:3ZS3"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:3ZS3"
SQ SEQUENCE 246 AA; 25700 MW; 3A34CE175DCB9FE4 CRC64;
MMKSQVASLL GLTLAILFFS GAHAAKITFT NNCPNTVWPG TLTGDQKPQL SLTGFELASK
ASRSVDAPSP WSGRFWGRTR CSTDAAGKFT CETADCGSGQ VACNGAGAVP PATLVEITIA
ANGGQDYYDV SLVDGFNLPM SVAPQGGTGE CKPSSCPANV NKVCPAPLQV KAADGSVISC
KSACLAFGDS KYCCTPPNNT PETCPPTEYS EIFEKQCPQA YSYAYDDKNS TFTCSGGPDY
VITFCP
