NLTP1_HORVU
ID NLTP1_HORVU Reviewed; 117 AA.
AC P07597;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Non-specific lipid-transfer protein 1;
DE Short=LTP 1;
DE AltName: Full=Probable amylase/protease inhibitor;
DE Flags: Precursor;
GN Name=LTP1; Synonyms=PAPI;
OS Hordeum vulgare (Barley).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Mundy J., Rogers J.C.;
RT "Selective expression of a probable amylase/protease inhibitor in barley
RT aleurone cells: comparison to the barley amylase/subtilisin inhibitor.";
RL Planta 169:51-63(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Bomi; TISSUE=Seedling;
RX PubMed=16668480; DOI=10.1104/pp.97.2.841;
RA Linnestad C., Loenneborg A., Kalla R., Olsen O.-A.;
RT "Promoter of a lipid transfer protein gene expressed in barley aleurone
RT cells contains similar myb and myc recognition sites as the maize Bz-McC
RT allele.";
RL Plant Physiol. 97:841-843(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Seed;
RX PubMed=1536930; DOI=10.1007/bf00040674;
RA Skriver K., Leah R., Mueller-Uri F., Mundy J., Olsen F.;
RT "Structure and expression of the barley lipid transfer protein gene Ltp1.";
RL Plant Mol. Biol. 18:585-589(1992).
RN [4]
RP PROTEIN SEQUENCE OF 27-117.
RC STRAIN=cv. Hiproly;
RA Svensson B., Asano K., Jonassen I., Poulsen F.M., Mundy J., Svendsen I.;
RT "A 10kD barley seed protein homologous with an alpha-amylase inhibitor from
RT Indian finger millet.";
RL Carlsberg Res. Commun. 51:493-500(1986).
RN [5]
RP IDENTIFICATION AS A LTP.
RX PubMed=2465737; DOI=10.1016/0003-9861(89)90154-9;
RA Bernhard W.R., Somerville C.R.;
RT "Coidentity of putative amylase inhibitors from barley and finger millet
RT with phospholipid transfer proteins inferred from amino acid sequence
RT homology.";
RL Arch. Biochem. Biophys. 269:695-697(1989).
RN [6]
RP LIPIDATION AT ASP-33.
RC STRAIN=cv. Optic;
RX PubMed=11435437; DOI=10.1074/jbc.m104841200;
RA Lindorff-Larsen K., Lerche M.H., Poulsen F.M., Roepstorff P., Winther J.R.;
RT "Barley lipid transfer protein, LTP1, contains a new type of lipid-like
RT post-translational modification.";
RL J. Biol. Chem. 276:33547-33553(2001).
RN [7]
RP BIOTECHNOLOGICAL RELEVANCE.
RX AGRICOLA=IND20411110;
RA Sorensen S.B., Bech L.M., Muldbjerg M., Beenfeldt T., Breddam K.;
RT "Barley lipid transfer protein 1 is involved in beer foam formation.";
RL Master Brew. Assoc. Am. Tech. Q. 30:136-145(1993).
RN [8]
RP STRUCTURE BY NMR OF 27-117, AND DISULFIDE BONDS.
RX PubMed=8771192; DOI=10.1002/pro.5560050103;
RA Heinemann B., Andersen K.V., Nielsen P.R., Bech L.M., Poulsen F.M.;
RT "Structure in solution of a four-helix lipid binding protein.";
RL Protein Sci. 5:13-23(1996).
RN [9]
RP STRUCTURE BY NMR OF 27-117, AND DISULFIDE BONDS.
RX PubMed=9032083; DOI=10.1016/s0969-2126(97)00186-x;
RA Lerche M.H., Kragelund B.B., Bech L.M., Poulsen F.M.;
RT "Barley lipid-transfer protein complexed with palmitoyl CoA: the structure
RT reveals a hydrophobic binding site that can expand to fit both large and
RT small lipid-like ligands.";
RL Structure 5:291-306(1997).
RN [10]
RP STRUCTURE BY NMR OF 27-117, AND DISULFIDE BONDS.
RX PubMed=9865943; DOI=10.1002/pro.5560071202;
RA Lerche M.H., Poulsen F.M.;
RT "Solution structure of barley lipid transfer protein complexed with
RT palmitate. Two different binding modes of palmitate in the homologous maize
RT and barley nonspecific lipid transfer proteins.";
RL Protein Sci. 7:2490-2498(1998).
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 -!- TISSUE SPECIFICITY: Aleurone layer of developing and germinating seeds.
CC {ECO:0000269|PubMed:1536930}.
CC -!- BIOTECHNOLOGY: During brewing process, structural and chemical
CC modifications of the protein occur. Both unfolding of the structure and
CC glycation should increased the amphiphilicity of the protein, leading
CC to foam-promoting forms that concentrate in beer foams.
CC {ECO:0000269|Ref.7}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an inhibitor of alpha-amylase or
CC of a protease and was known as PAPI: probable alpha-amylase/protease
CC inhibitor. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA42832.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=One beer please - Issue 48
CC of July 2004;
CC URL="https://web.expasy.org/spotlight/back_issues/048";
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; M15207; AAA32970.1; -; mRNA.
DR EMBL; X05168; CAA28805.1; -; mRNA.
DR EMBL; X59253; CAA41946.1; -; Genomic_DNA.
DR EMBL; X60292; CAA42832.1; ALT_SEQ; Genomic_DNA.
DR PIR; S20507; S20507.
DR PIR; T05947; T05947.
DR PDB; 1BE2; NMR; -; A=27-117.
DR PDB; 1JTB; NMR; -; A=27-117.
DR PDB; 1LIP; NMR; -; A=27-117.
DR PDB; 1MID; X-ray; 1.71 A; A=27-117.
DR PDB; 3GSH; X-ray; 1.80 A; A/B=27-117.
DR PDBsum; 1BE2; -.
DR PDBsum; 1JTB; -.
DR PDBsum; 1LIP; -.
DR PDBsum; 1MID; -.
DR PDBsum; 3GSH; -.
DR AlphaFoldDB; P07597; -.
DR BMRB; P07597; -.
DR SMR; P07597; -.
DR EnsemblPlants; HORVU.MOREX.r2.5HG0384350.1; HORVU.MOREX.r2.5HG0384350.1; HORVU.MOREX.r2.5HG0384350.
DR EnsemblPlants; HORVU.MOREX.r2.5HG0384350.1.mrna1; HORVU.MOREX.r2.5HG0384350.1.mrna1.cds1; HORVU.MOREX.r2.5HG0384350.1.
DR Gramene; HORVU.MOREX.r2.5HG0384350.1; HORVU.MOREX.r2.5HG0384350.1; HORVU.MOREX.r2.5HG0384350.
DR Gramene; HORVU.MOREX.r2.5HG0384350.1.mrna1; HORVU.MOREX.r2.5HG0384350.1.mrna1.cds1; HORVU.MOREX.r2.5HG0384350.1.
DR EvolutionaryTrace; P07597; -.
DR ExpressionAtlas; P07597; 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; Direct protein sequencing; Disulfide bond; Lipid-binding;
KW Lipoprotein; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 27..117
FT /note="Non-specific lipid-transfer protein 1"
FT /id="PRO_0000018381"
FT LIPID 33
FT /note="Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid
FT aspartate ester"
FT /evidence="ECO:0000269|PubMed:11435437"
FT DISULFID 29..76
FT /evidence="ECO:0000269|PubMed:8771192,
FT ECO:0000269|PubMed:9032083, ECO:0000269|PubMed:9865943,
FT ECO:0007744|PDB:1BE2, ECO:0007744|PDB:1JTB,
FT ECO:0007744|PDB:1LIP"
FT DISULFID 39..53
FT /evidence="ECO:0000269|PubMed:8771192,
FT ECO:0000269|PubMed:9032083, ECO:0000269|PubMed:9865943,
FT ECO:0007744|PDB:1BE2, ECO:0007744|PDB:1JTB,
FT ECO:0007744|PDB:1LIP"
FT DISULFID 54..99
FT /evidence="ECO:0000269|PubMed:8771192,
FT ECO:0000269|PubMed:9032083, ECO:0000269|PubMed:9865943,
FT ECO:0007744|PDB:1BE2, ECO:0007744|PDB:1JTB,
FT ECO:0007744|PDB:1LIP"
FT DISULFID 74..113
FT /evidence="ECO:0000269|PubMed:8771192,
FT ECO:0000269|PubMed:9032083, ECO:0000269|PubMed:9865943,
FT ECO:0007744|PDB:1BE2, ECO:0007744|PDB:1JTB,
FT ECO:0007744|PDB:1LIP"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:1MID"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1MID"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:1MID"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:1MID"
FT HELIX 67..82
FT /evidence="ECO:0007829|PDB:1MID"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1LIP"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1MID"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1LIP"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1MID"
SQ SEQUENCE 117 AA; 12301 MW; 31209513AF00E444 CRC64;
MARAQVLLMA AALVLMLTAA PRAAVALNCG QVDSKMKPCL TYVQGGPGPS GECCNGVRDL
HNQAQSSGDR QTVCNCLKGI ARGIHNLNLN NAASIPSKCN VNVPYTISPD IDCSRIY
