ID NLTP_MAIZE Reviewed; 120 AA. AC P19656; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 24-JAN-2024, entry version 136. DE RecName: Full=Non-specific lipid-transfer protein; DE Short=LTP; DE AltName: Full=Phospholipid transfer protein; DE Short=PLTP; DE AltName: Allergen=Zea m 14; DE Flags: Precursor; OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-120. RC TISSUE=Seed; RX PubMed=3182817; DOI=10.1016/s0021-9258(18)37469-6; RA Tchang F., This P., Stiefel V., Arondel V., Morch M.-D., Pages M., RA Puigdomenech P., Grellet F., Delseny M., Bouillon P., Huet J.-C., RA Guerbette F., Beauvais-Cante F., Duranton H., Pernollet J.-C., Kader J.-C.; RT "Phospholipid transfer protein: full-length cDNA and amino acid sequence in RT maize. Amino acid sequence homologies between plant phospholipid transfer RT proteins."; RL J. Biol. Chem. 263:16849-16855(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2022320; DOI=10.1016/0378-1119(91)90045-d; RA Arondel V., Tchang F., Baillet B., Vignols F., Grellet F., Delseny M., RA Kader J.-C., Puigdomenech P.; RT "Multiple mRNA coding for phospholipid-transfer protein from Zea mays arise RT from alternative splicing."; RL Gene 99:133-136(1991). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 28-120, AND DISULFIDE BONDS. RX PubMed=7735835; DOI=10.1016/s0969-2126(01)00149-6; RA Shin D.H., Lee J.Y., Hwang K.Y., Kim K.K., Suh S.W.; RT "High-resolution crystal structure of the non-specific lipid-transfer RT protein from maize seedlings."; RL Structure 3:189-199(1995). RN [4] RP STRUCTURE BY NMR. RX PubMed=8026483; DOI=10.1111/j.1432-1033.1994.tb18957.x; RA Petit M.-C., Sodano P., Marion D., Ptak M.; RT "Two-dimensional 1H-NMR studies of maize lipid-transfer protein. Sequence- RT specific assignment and secondary structure."; RL Eur. J. Biochem. 222:1047-1054(1994). RN [5] RP STRUCTURE BY NMR. RX PubMed=8845747; DOI=10.1002/pro.5560050402; RA Gomar J., Petit M.-C., Sodano P., Sy D., Marion D., Kader J.-C., RA Vovelle F., Ptak M.; RT "Solution structure and lipid binding of a nonspecific lipid transfer RT protein extracted from maize seeds."; RL Protein Sci. 5:565-577(1996). 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P19656-1; Sequence=Displayed; CC Name=2; Synonyms=long; CC IsoId=P19656-2; Sequence=VSP_003147; CC -!- ALLERGEN: Causes an allergic reaction in human. CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J04176; AAA33493.1; -; mRNA. DR EMBL; M57249; AAA33494.1; -; mRNA. DR PIR; A31779; A31779. DR PIR; S45635; S45635. DR PDB; 1AFH; NMR; -; A=28-120. DR PDB; 1FK0; X-ray; 1.80 A; A=28-120. DR PDB; 1FK1; X-ray; 1.80 A; A=28-120. DR PDB; 1FK2; X-ray; 1.80 A; A=28-120. DR PDB; 1FK3; X-ray; 1.80 A; A=28-120. DR PDB; 1FK4; X-ray; 1.80 A; A=28-120. DR PDB; 1FK5; X-ray; 1.30 A; A=28-120. DR PDB; 1FK6; X-ray; 1.90 A; A=28-120. DR PDB; 1FK7; X-ray; 1.90 A; A=28-120. DR PDB; 1MZL; X-ray; 1.90 A; A=28-120. DR PDB; 1MZM; X-ray; 1.78 A; A=28-120. DR PDBsum; 1AFH; -. DR PDBsum; 1FK0; -. DR PDBsum; 1FK1; -. DR PDBsum; 1FK2; -. DR PDBsum; 1FK3; -. DR PDBsum; 1FK4; -. DR PDBsum; 1FK5; -. DR PDBsum; 1FK6; -. DR PDBsum; 1FK7; -. DR PDBsum; 1MZL; -. DR PDBsum; 1MZM; -. DR AlphaFoldDB; P19656; -. DR SMR; P19656; -. DR STRING; 4577.P19656; -. DR Allergome; 3534; Zea m 14.0101. DR Allergome; 3535; Zea m 14.0102. DR Allergome; 684; Zea m 14. DR PaxDb; 4577-GRMZM2G101958_P01; -. DR MaizeGDB; 25447; -. DR eggNOG; ENOG502S4CI; Eukaryota. DR InParanoid; P19656; -. DR EvolutionaryTrace; P19656; -. DR Proteomes; UP000007305; Unplaced. DR ExpressionAtlas; P19656; baseline and differential. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0006869; P:lipid transport; IEA:InterPro. DR CDD; cd01960; nsLTP1; 1. DR Gene3D; 1.10.110.10; Plant lipid-transfer and hydrophobic proteins; 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:SF161; NON-SPECIFIC LIPID-TRANSFER PROTEIN 1; 1. DR PANTHER; PTHR33076; NON-SPECIFIC LIPID-TRANSFER PROTEIN 2-RELATED; 1. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR PRINTS; PR00382; LIPIDTRNSFER. DR SMART; SM00499; AAI; 1. DR SUPFAM; SSF47699; Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin; 1. DR PROSITE; PS00597; PLANT_LTP; 1. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Alternative splicing; Direct protein sequencing; KW Disulfide bond; Lipid-binding; Reference proteome; Signal; Transport. FT SIGNAL 1..27 FT /evidence="ECO:0000269|PubMed:3182817" FT CHAIN 28..120 FT /note="Non-specific lipid-transfer protein" FT /id="PRO_0000018389" FT DISULFID 31..79 FT /evidence="ECO:0000269|PubMed:7735835, FT ECO:0007744|PDB:1MZM" FT DISULFID 41..56 FT /evidence="ECO:0000269|PubMed:7735835, FT ECO:0007744|PDB:1MZM" FT DISULFID 57..102 FT /evidence="ECO:0000269|PubMed:7735835, FT ECO:0007744|PDB:1MZM" FT DISULFID 77..116 FT /evidence="ECO:0000269|PubMed:7735835, FT ECO:0007744|PDB:1MZM" FT VAR_SEQ 119..120 FT /note="VN -> YSRRMHASAD (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_003147" FT HELIX 31..38 FT /evidence="ECO:0007829|PDB:1FK5" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:1FK5" FT HELIX 42..45 FT /evidence="ECO:0007829|PDB:1FK5" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:1FK5" FT HELIX 54..66 FT /evidence="ECO:0007829|PDB:1FK5" FT HELIX 70..85 FT /evidence="ECO:0007829|PDB:1FK5" FT HELIX 92..101 FT /evidence="ECO:0007829|PDB:1FK5" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:1FK5" SQ SEQUENCE 120 AA; 11705 MW; 28F27EBAE3910218 CRC64; MARTQQLAVV ATAVVALVLL AAATSEAAIS CGQVASAIAP CISYARGQGS GPSAGCCSGV RSLNNAARTT ADRRAACNCL KNAAAGVSGL NAGNAASIPS KCGVSIPYTI STSTDCSRVN //