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