ID   NLT21_PARJU             Reviewed;         133 AA.
AC   P55958;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Probable non-specific lipid-transfer protein 2;
DE            Short=LTP 2;
DE   AltName: Full=Allergen Par j II;
DE   AltName: Full=Major pollen allergen Par j 2.0101;
DE   AltName: Full=Protein P2;
DE   AltName: Allergen=Par j 2.0101;
DE   Flags: Precursor;
OS   Parietaria judaica (Pellitory-of-the-wall) (Parietaria diffusa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Urticaceae; Parietaria.
OX   NCBI_TaxID=33127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pollen;
RX   PubMed=8985165; DOI=10.1016/s0014-5793(96)01328-2;
RA   Duro G., Colombo P., Costa M.A., Izzo V., Porcasi R., di Fiore R.,
RA   Locorotondo G., Mirisola M.G., Cocchiara R., Geraci D.;
RT   "cDNA cloning, sequence analysis and allergological characterization of Par
RT   j 2.0101, a new major allergen of the Parietaria judaica pollen.";
RL   FEBS Lett. 399:295-298(1996).
RN   [2]
RP   DISULFIDE BONDS.
RX   PubMed=12974385; DOI=10.1515/bc.2003.129;
RA   Amoresano A., Pucci P., Duro G., Colombo P., Costa M.A., Izzo V., Lamba D.,
RA   Geraci D.;
RT   "Assignment of disulphide bridges in Par j 2.0101, a major allergen of
RT   Parietaria judaica pollen.";
RL   Biol. Chem. 384:1165-1172(2003).
CC   -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer
CC       phospholipids as well as galactolipids across membranes. May play a
CC       role in wax or cutin deposition in the cell walls of expanding
CC       epidermal cells and certain secretory tissues.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE and
CC       induces histamine release from basophils of Pj-pollen-allergic
CC       subjects.
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR   EMBL; X95865; CAA65121.1; -; mRNA.
DR   AlphaFoldDB; P55958; -.
DR   SMR; P55958; -.
DR   Allergome; 507; Par j 2.
DR   Allergome; 508; Par j 2.0101.
DR   PRIDE; P55958; -.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR   Gene3D; 1.10.110.10; -; 1.
DR   InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR   InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR   InterPro; IPR000528; Plant_nsLTP.
DR   PANTHER; PTHR33076; PTHR33076; 1.
DR   Pfam; PF14368; LTP_2; 1.
DR   PRINTS; PR00382; LIPIDTRNSFER.
DR   SMART; SM00499; AAI; 1.
DR   SUPFAM; SSF47699; SSF47699; 1.
DR   PROSITE; PS00597; PLANT_LTP; 1.
PE   1: Evidence at protein level;
KW   Allergen; Disulfide bond; Lipid-binding; Signal; Transport.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..133
FT                   /note="Probable non-specific lipid-transfer protein 2"
FT                   /id="PRO_0000018398"
FT   DISULFID        35..83
FT                   /evidence="ECO:0000269|PubMed:12974385"
FT   DISULFID        45..60
FT                   /evidence="ECO:0000269|PubMed:12974385"
FT   DISULFID        61..106
FT                   /evidence="ECO:0000269|PubMed:12974385"
FT   DISULFID        81..121
FT                   /evidence="ECO:0000269|PubMed:12974385"
SQ   SEQUENCE   133 AA;  14336 MW;  7A0E1CC22D59BE74 CRC64;
     MRTVSMAALV VIAAALAWTS SAEPAPAPAP GEEACGKVVQ DIMPCLHFVK GEEKEPSKEC
     CSGTKKLSEE VKTTEQKREA CKCIVRATKG ISGIKNELVA EVPKKCDIKT TLPPITADFD
     CSKIQSTIFR GYY