NLTP6_LENCU
ID NLTP6_LENCU Reviewed; 118 AA.
AC A0AT32; P84255;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Non-specific lipid-transfer protein 6;
DE Short=LTP6;
DE Flags: Precursor;
OS Lens culinaris (Lentil) (Cicer lens).
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; Lens.
OX NCBI_TaxID=3864;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 26-47.
RC TISSUE=Seed, and Seedling;
RX PubMed=17511608; DOI=10.1134/s0006297907040104;
RA Finkina E.I., Balandin S.V., Serebryakova M.V., Potapenko N.A.,
RA Tagaev A.A., Ovchinnikova T.V.;
RT "Purification and primary structure of novel lipid transfer proteins from
RT germinated lentil (Lens culinaris) seeds.";
RL Biochemistry (Mosc.) 72:430-438(2007).
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.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000255}.
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DR EMBL; AY793557; AAX35810.1; -; mRNA.
DR AlphaFoldDB; A0AT32; -.
DR BMRB; A0AT32; -.
DR SMR; A0AT32; -.
DR Allergome; 8712; Len c 3.
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 Direct protein sequencing; Disulfide bond; Lipid-binding; Signal;
KW Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:17511608"
FT CHAIN 26..118
FT /note="Non-specific lipid-transfer protein 6"
FT /id="PRO_5000147977"
FT DISULFID 29..76
FT /evidence="ECO:0000250|UniProtKB:P23096"
FT DISULFID 39..53
FT /evidence="ECO:0000250|UniProtKB:P23096"
FT DISULFID 54..99
FT /evidence="ECO:0000250|UniProtKB:P23096"
FT DISULFID 74..113
FT /evidence="ECO:0000250|UniProtKB:P23096"
SQ SEQUENCE 118 AA; 11885 MW; B1997CA31E5C6757 CRC64;
MARGMKLACV VLVMCMVVIA PMAEGAISCG AVTSDLSPCL TYLTGGPGPS PQCCGGVKKL
LAAANTTPDR QAACNCLKSA AGSITKLNTN NAAALPGKCG VDIPYKISTS TNCNTVKF