NLTP2_APIGA
ID NLTP2_APIGA Reviewed; 67 AA.
AC P86809;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Non-specific lipid-transfer protein 2 {ECO:0000303|PubMed:23913675};
DE AltName: Full=Allergen Api g 6.0101 {ECO:0000303|PubMed:23913675};
DE AltName: Allergen=Api g 6 {ECO:0000303|PubMed:23913675};
OS Apium graveolens var. rapaceum (Celeriac).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Apium.
OX NCBI_TaxID=278110;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS,
RP MASS SPECTROMETRY, ALLERGEN, AND IGE-BINDING.
RC TISSUE=Tuber {ECO:0000269|PubMed:23913675};
RX PubMed=23913675; DOI=10.1002/mnfr.201300085;
RA Vejvar E., Himly M., Briza P., Eichhorn S., Ebner C., Hemmer W.,
RA Ferreira F., Gadermaier G.;
RT "Allergenic relevance of nonspecific lipid transfer proteins 2:
RT Identification and characterization of Api g 6 from celery tuber as
RT representative of a novel IgE-binding protein family.";
RL Mol. Nutr. Food Res. 57:2061-2070(2013).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q43748}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Stable at pH 3. {ECO:0000269|PubMed:23913675};
CC Temperature dependence:
CC Stable up to 90 degrees Celsius. {ECO:0000269|PubMed:23913675};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23913675}.
CC -!- PTM: Disulfide bonds. {ECO:0000269|PubMed:23913675}.
CC -!- MASS SPECTROMETRY: Mass=6936.3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:23913675};
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:23913675}.
CC -!- MISCELLANEOUS: Found in celeriac but not in celery. Highly resistant to
CC pepsin and other proteinases. {ECO:0000269|PubMed:23913675}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000255}.
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DR AlphaFoldDB; P86809; -.
DR SMR; P86809; -.
DR Allergome; 9512; Api g 6.
DR Allergome; 9513; Api g 6.0101.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR CDD; cd01959; nsLTP2; 1.
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; IPR033872; nsLTP2.
DR PANTHER; PTHR33214; PTHR33214; 1.
DR Pfam; PF14368; LTP_2; 1.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Disulfide bond; Lipid-binding;
KW Transport.
FT CHAIN 1..67
FT /note="Non-specific lipid-transfer protein 2"
FT /id="PRO_0000424147"
FT DISULFID 3..35
FT /evidence="ECO:0000250|UniProtKB:Q10ST8"
FT DISULFID 11..25
FT /evidence="ECO:0000250|UniProtKB:Q10ST8"
FT DISULFID 26..61
FT /evidence="ECO:0000250|UniProtKB:Q10ST8"
FT DISULFID 37..67
FT /evidence="ECO:0000250|UniProtKB:Q10ST8"
SQ SEQUENCE 67 AA; 6945 MW; F5CEB0B5958F1BA9 CRC64;
ATCSAVQLSP CLAAITKNTP PSAACCNKLK EQKPCLCGYL KDPNLKNYVN SPGARKTASS
CGVALKC
