NLTP1_APIGR
ID NLTP1_APIGR Reviewed; 118 AA.
AC E6Y8S8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Non-specific lipid-transfer protein {ECO:0000303|PubMed:21462324};
DE AltName: Full=Allergen Api g 2.0101 {ECO:0000303|PubMed:21462324};
DE AltName: Allergen=Api g 2 {ECO:0000303|PubMed:21462324};
DE Flags: Precursor;
OS Apium graveolens (Celery).
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=4045;
RN [1] {ECO:0000312|EMBL:ACV04796.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, BIOPHYSICOCHEMICAL
RP PROPERTIES, DISULFIDE BONDS, MASS SPECTROMETRY, ALLERGEN, AND IGE-BINDING.
RX PubMed=21462324; DOI=10.1002/mnfr.201000443;
RA Gadermaier G., Egger M., Girbl T., Erler A., Harrer A., Vejvar E., Liso M.,
RA Richter K., Zuidmeer L., Mari A., Ferreira F.;
RT "Molecular characterization of Api g 2, a novel allergenic member of the
RT lipid-transfer protein 1 family from celery stalks.";
RL Mol. Nutr. Food Res. 55:568-577(2011).
RN [2] {ECO:0000305}
RP IGE-BINDING.
RX PubMed=21897872; DOI=10.1371/journal.pone.0024150;
RA Gadermaier G., Hauser M., Egger M., Ferrara R., Briza P., Santos K.S.,
RA Zennaro D., Girbl T., Zuidmeer-Jongejan L., Mari A., Ferreira F.;
RT "Sensitization prevalence, antibody cross-reactivity and immunogenic
RT peptide profile of Api g 2, the non-specific lipid transfer protein 1 of
RT celery.";
RL PLoS ONE 6:E24150-E24150(2011).
RN [3] {ECO:0000305}
RP IGE-BINDING.
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:21462324};
CC Temperature dependence:
CC Stable up to 84 degrees Celsius. {ECO:0000269|PubMed:21462324};
CC -!- PTM: Disulfide bonds. {ECO:0000269|PubMed:21462324}.
CC -!- MASS SPECTROMETRY: Mass=9024.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:21462324};
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:21462324, ECO:0000269|PubMed:21897872,
CC ECO:0000269|PubMed:23913675}.
CC -!- MISCELLANEOUS: Found in celery but not in celeriac. Highly resistant to
CC pepsin and other proteinases. {ECO:0000269|PubMed:21462324,
CC ECO:0000269|PubMed:23913675}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000255}.
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DR EMBL; FJ643539; ACV04796.1; -; mRNA.
DR AlphaFoldDB; E6Y8S8; -.
DR SMR; E6Y8S8; -.
DR Allergome; 5890; Api g 2.
DR Allergome; 5891; Api g 2.0101.
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; PF00234; Tryp_alpha_amyl; 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; Direct protein sequencing; Disulfide bond; Lipid-binding; Signal;
KW Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:21462324"
FT CHAIN 28..118
FT /note="Non-specific lipid-transfer protein"
FT /evidence="ECO:0000269|PubMed:21462324"
FT /id="PRO_5000680950"
FT DISULFID 30..75
FT /evidence="ECO:0000250|UniProtKB:Q10ST8"
FT DISULFID 40..54
FT /evidence="ECO:0000250|UniProtKB:Q10ST8"
FT DISULFID 55..100
FT /evidence="ECO:0000250|UniProtKB:Q10ST8"
FT DISULFID 77..114
FT /evidence="ECO:0000250|UniProtKB:Q10ST8"
SQ SEQUENCE 118 AA; 11750 MW; DD6BFF82E2BA67B8 CRC64;
MGVSKVAIAV AVMLMVVVIN HPAVVEGLTC GQVTGKLGGC LGYLKGGGYP SPACCGGVKG
LNSLAKTPAD RKQACACLKT LAGSVKGINY GAASALPGKC GIRIPYPISP STDCSRVN
