NLTP1_PEA
ID NLTP1_PEA Reviewed; 120 AA.
AC A0A161AT60; C0HJR7;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Non-specific lipid-transfer protein 1 {ECO:0000303|PubMed:27137920};
DE Short=PsLTP1 {ECO:0000303|PubMed:27137920};
DE AltName: Allergen=Pis s 3 {ECO:0000305};
DE Flags: Precursor;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-119, FUNCTION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISULFIDE BONDS, MASS SPECTROMETRY,
RP ALLERGEN, AND STRUCTURE BY NMR OF 26-120.
RC TISSUE=Seed {ECO:0000269|PubMed:27137920};
RX PubMed=27137920; DOI=10.1186/s12870-016-0792-6;
RA Bogdanov I.V., Shenkarev Z.O., Finkina E.I., Melnikova D.N.,
RA Rumynskiy E.I., Arseniev A.S., Ovchinnikova T.V.;
RT "A novel lipid transfer protein from the pea Pisum sativum: isolation,
RT recombinant expression, solution structure, antifungal activity, lipid
RT binding, and allergenic properties.";
RL BMC Plant Biol. 16:107-107(2016).
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 (Probable). Binds
CC saturated and unsaturated lipids, jasmonic acid and lysolipids
CC (PubMed:27137920). Has antifungal activity against A.niger VKM F-2259
CC (IC(50)=40 uM), F.oxysporum TCXA-4 (IC(50)=20-40), F.solani VKM F-142
CC (IC(50)=20-40 uM) and N.crassa VKM F-184 (IC(50)=40 uM)
CC (PubMed:27137920). Has weak antibacterial activity against
CC A.tumefaciens A281, C.michiganensis VKM Ac-1144 and P.syringae VKM B-
CC 1546 (PubMed:27137920). {ECO:0000269|PubMed:27137920, ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stem, leaves and tendrils of
CC the mature plant. {ECO:0000269|PubMed:27137920}.
CC -!- DEVELOPMENTAL STAGE: Expression drops sharply after germination and
CC increases again in the mature plant. {ECO:0000269|PubMed:27137920}.
CC -!- MASS SPECTROMETRY: Mass=9401.48; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:27137920};
CC -!- ALLERGEN: Causes an allergenic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:27137920}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; KJ569141; AJG44053.1; -; mRNA.
DR PDB; 2N81; NMR; -; A=26-120.
DR PDBsum; 2N81; -.
DR AlphaFoldDB; A0A161AT60; -.
DR SMR; A0A161AT60; -.
DR Allergome; 11950; Pis s 3.
DR Allergome; 11951; Pis s 3.0101.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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 3D-structure; Allergen; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Disulfide bond; Fungicide; Lipid transport;
KW Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:27137920"
FT CHAIN 26..119
FT /note="Non-specific lipid-transfer protein 1"
FT /evidence="ECO:0000269|PubMed:27137920"
FT /id="PRO_0000437169"
FT PROPEP 120
FT /evidence="ECO:0000303|PubMed:27137920"
FT /id="PRO_0000437170"
FT DISULFID 29..78
FT /evidence="ECO:0000269|PubMed:27137920"
FT DISULFID 39..55
FT /evidence="ECO:0000269|PubMed:27137920"
FT DISULFID 56..101
FT /evidence="ECO:0000269|PubMed:27137920"
FT DISULFID 76..115
FT /evidence="ECO:0000269|PubMed:27137920"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:2N81"
SQ SEQUENCE 120 AA; 12160 MW; FCDE59C3D93D4D6F CRC64;
MARSMKLACV ALVICMVVIA PMAEAALSCG TVSADMAPCV TYLQAPNNAS PPPPCCAGVK
KLLAAATTTP DRQAACNCLK SAAGSIPKLN TNNAAALPGK CGVSIPYKIS TSTNCNTVRF
