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NLTP1_FOEVU
ID   NLTP1_FOEVU             Reviewed;          91 AA.
AC   C0HLP9;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 1.
DT   25-MAY-2022, entry version 5.
DE   RecName: Full=Non-specific lipid-transfer protein 1 {ECO:0000303|PubMed:33277525};
DE            Short=FvLTP1 {ECO:0000305};
DE            Short=nsLTP {ECO:0000303|PubMed:33277525};
OS   Foeniculum vulgare (Fennel) (Foeniculum officinale).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Anethum.
OX   NCBI_TaxID=2849586 {ECO:0000303|PubMed:33277525};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Seed {ECO:0000303|PubMed:33277525};
RX   PubMed=33277525; DOI=10.1038/s41598-020-77278-6;
RA   Megeressa M., Siraj B., Zarina S., Ahmed A.;
RT   "Structural characterization and in vitro lipid binding studies of non-
RT   specific lipid transfer protein 1 (nsLTP1) from fennel (Foeniculum vulgare)
RT   seeds.";
RL   Sci. Rep. 10:21243-21243(2020).
CC   -!- FUNCTION: Plant non-specific lipid-transfer proteins transfer
CC       phospholipids as well as galactolipids across membranes (By
CC       similarity). May play a role in wax or cutin deposition in the cell
CC       walls of expanding epidermal cells and certain secretory tissues (By
CC       similarity). Binds to both saturated and unsaturated lipids, with the
CC       highest binding efficiency for linoleic acid, followed by linolenic
CC       acid (PubMed:33277525). {ECO:0000250|UniProtKB:C0HLG2,
CC       ECO:0000269|PubMed:33277525}.
CC   -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level).
CC       {ECO:0000269|PubMed:33277525}.
CC   -!- MASS SPECTROMETRY: Mass=9433.32; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:33277525};
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR   AlphaFoldDB; C0HLP9; -.
DR   SMR; C0HLP9; -.
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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Lipid-binding; Transport.
FT   CHAIN           1..91
FT                   /note="Non-specific lipid-transfer protein 1"
FT                   /id="PRO_0000452471"
FT   DISULFID        4..51
FT                   /evidence="ECO:0000250|UniProtKB:Q42952"
FT   DISULFID        14..28
FT                   /evidence="ECO:0000250|UniProtKB:Q42952"
FT   DISULFID        29..74
FT                   /evidence="ECO:0000250|UniProtKB:Q42952"
FT   DISULFID        49..88
FT                   /evidence="ECO:0000250|UniProtKB:Q42952"
SQ   SEQUENCE   91 AA;  9458 MW;  E501A08253071881 CRC64;
     AIDCKTVDAA LVPCVPYLTG GGTPTTQCCS GVSSIKTMAG TPQDKKDACN CVKAAANRYP
     NIRDDVAQAL PVKCNVQLDI PVSRTTNCDA I
 
 
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