NLTP_MAIZE
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 03-AUG-2022, entry version 130.
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}.
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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.GRMZM2G101958_P01; -.
DR Allergome; 3534; Zea m 14.0101.
DR Allergome; 3535; Zea m 14.0102.
DR Allergome; 684; Zea m 14.
DR PaxDb; P19656; -.
DR PRIDE; P19656; -.
DR MaizeGDB; 25447; -.
DR eggNOG; ENOG502S4CI; Eukaryota.
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 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; 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
