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-NOV-2008, entry version 83.
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; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Pooideae; Triticeae; 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
RT   barley aleurone cells: comparison to the barley amylase/subtilisin
RT   inhibitor.";
RL   Planta 169:51-63(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Bomi; TISSUE=Seedling;
RX   PubMed=16668480;
RA   Linnestad C., Loenneborg A., Kalla R., Olsen O.-A.;
RT   "Promoter of a lipid transfer protein gene expressed in barley
RT   aleurone cells contains similar myb and myc recognition sites as the
RT   maize Bz-McC allele.";
RL   Plant Physiol. 97:841-843(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Seed;
RX   MEDLINE=92163023; 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
RT   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.,
RA   Svendsen I.;
RT   "A 10kD barley seed protein homologous with an alpha-amylase inhibitor
RT   from Indian finger millet.";
RL   Carlsberg Res. Commun. 51:493-500(1986).
RN   [5]
RP   IDENTIFICATION AS A LTP.
RX   MEDLINE=89149117; 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
RT   millet with phospholipid transfer proteins inferred from amino acid
RT   sequence homology.";
RL   Arch. Biochem. Biophys. 269:695-697(1989).
RN   [6]
RP   LIPID MODIFICATION OF ASP-33.
RC   STRAIN=cv. Optic;
RX   MEDLINE=21423968; PubMed=11435437; DOI=10.1074/jbc.M104841200;
RA   Lindorff-Larsen K., Lerche M.H., Poulsen F.M., Roepstorff P.,
RA   Winther J.R.;
RT   "Barley lipid transfer protein, LTP1, contains a new type of lipid-
RT   like 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.
RX   MEDLINE=96367078; PubMed=8771192;
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.
RX   MEDLINE=97184693; 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
RT   structure reveals a hydrophobic binding site that can expand to fit
RT   both large and small lipid-like ligands.";
RL   Structure 5:291-306(1997).
RN   [10]
RP   STRUCTURE BY NMR OF 27-117.
RX   MEDLINE=99081541; PubMed=9865943;
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
RT   maize 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
CC       a 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
CC       seeds.
CC   -!- BIOTECHNOLOGY: During brewing process, structural and chemical
CC       modifications of the protein occur. Both unfolding of the
CC       structure and glycation should increased the amphiphilicity of the
CC       protein, leading to foam-promoting forms that concentrate in beer
CC       foams.
CC   -!- SIMILARITY: Belongs to the plant LTP family.
CC   -!- CAUTION: Was originally thought to be an inhibitor of alpha-
CC       amylase or of a protease and was known as PAPI: probable alpha-
CC       amylase/protease inhibitor.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA42832.1; Type=Erroneous gene model prediction;
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=One beer please - Issue
CC       48 of July 2004;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt048.shtml";
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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   UniGene; Hv.23139; -.
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   PDBsum; 1BE2; -.
DR   PDBsum; 1JTB; -.
DR   PDBsum; 1LIP; -.
DR   PDBsum; 1MID; -.
DR   Gramene; P07597; -.
DR   LinkHub; P07597; -.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR   InterPro; IPR013770; LPT_helical.
DR   InterPro; IPR003612; LTP/seed_store/tryp_amyl_inhib.
DR   InterPro; IPR000528; Plant_LTP.
DR   Gene3D; G3DSA:1.10.110.10; LPT_helical; 1.
DR   Pfam; PF00234; Tryp_alpha_amyl; 1.
DR   PRINTS; PR00382; LIPIDTRNSFER.
DR   SMART; SM00499; AAI; 1.
DR   PROSITE; PS00597; PLANT_LTP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Lipid-binding; Lipoprotein;
KW   Signal; Transport.
FT   SIGNAL        1     26
FT   CHAIN        27    117       Non-specific lipid-transfer protein 1.
FT                                /FTId=PRO_0000018381.
FT   LIPID        33     33       Cis-14-hydroxy-10,13-dioxo-7-
FT                                heptadecenoic acid aspartate ester.
FT   DISULFID     29     76
FT   DISULFID     39     53
FT   DISULFID     54     99
FT   DISULFID     74    113
FT   HELIX        29     36
FT   HELIX        37     39
FT   HELIX        40     43
FT   HELIX        51     63
FT   HELIX        67     82
FT   HELIX        89     98
FT   HELIX       113    115
SQ   SEQUENCE   117 AA;  12301 MW;  31209513AF00E444 CRC64;
     MARAQVLLMA AALVLMLTAA PRAAVALNCG QVDSKMKPCL TYVQGGPGPS GECCNGVRDL
     HNQAQSSGDR QTVCNCLKGI ARGIHNLNLN NAASIPSKCN VNVPYTISPD IDCSRIY
//