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UniProtKB/Swiss-Prot entry P07597


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NLTP1_HORVU
Primary accession number P07597
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1988
Sequence was last modified on April 1, 1988 (Sequence version 1)
Annotations were last modified on    July 1, 2008 (Entry version 81)
Name and origin of the protein
Protein name Non-specific lipid-transfer protein 1 [Precursor]
Synonyms LTP 1
Probable amylase/protease inhibitor
Gene name
Name: LTP1
Synonyms: PAPI
From
Hordeum vulgare (Barley) [TaxID: 4513] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Pooideae; Triticeae; Hordeum.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE.
Mundy J., Rogers J.C.;
"Selective expression of a probable amylase/protease inhibitor in barley aleurone cells: comparison to the barley amylase/subtilisin inhibitor.";
Planta 169:51-63(1986).
[2]
NUCLEOTIDE SEQUENCE.
STRAIN=cv. Bomi;
TISSUE=Seedling;
PubMed=16668480 [NCBI, ExPASy, EBI, Israel, Japan]
Linnestad C., Loenneborg A., Kalla R., Olsen O.-A.;
"Promoter of a lipid transfer protein gene expressed in barley aleurone cells contains similar myb and myc recognition sites as the maize Bz-McC allele.";
Plant Physiol. 97:841-843(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
TISSUE=Seed;
DOI=10.1007/BF00040674; PubMed=1536930 [NCBI, ExPASy, EBI, Israel, Japan]
Skriver K., Leah R., Mueller-Uri F., Mundy J., Olsen F.;
"Structure and expression of the barley lipid transfer protein gene Ltp1.";
Plant Mol. Biol. 18:585-589(1992).
[4]
PROTEIN SEQUENCE OF 27-117.
STRAIN=cv. Hiproly;
Svensson B., Asano K., Jonassen I., Poulsen F.M., Mundy J., Svendsen I.;
"A 10kD barley seed protein homologous with an alpha-amylase inhibitor from Indian finger millet.";
Carlsberg Res. Commun. 51:493-500(1986).
[5]
IDENTIFICATION AS A LTP.
DOI=10.1016/0003-9861(89)90154-9; PubMed=2465737 [NCBI, ExPASy, EBI, Israel, Japan]
Bernhard W.R., Somerville C.R.;
"Coidentity of putative amylase inhibitors from barley and finger millet with phospholipid transfer proteins inferred from amino acid sequence homology.";
Arch. Biochem. Biophys. 269:695-697(1989).
[6]
LIPID MODIFICATION OF ASP-33.
STRAIN=cv. Optic;
DOI=10.1074/jbc.M104841200; PubMed=11435437 [NCBI, ExPASy, EBI, Israel, Japan]
Lindorff-Larsen K., Lerche M.H., Poulsen F.M., Roepstorff P., Winther J.R.;
"Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification.";
J. Biol. Chem. 276:33547-33553(2001).
[7]
BIOTECHNOLOGICAL RELEVANCE.
AGRICOLA=IND20411110
Sorensen S.B., Bech L.M., Muldbjerg M., Beenfeldt T., Breddam K.;
"Barley lipid transfer protein 1 is involved in beer foam formation.";
Master Brew. Assoc. Am. Tech. Q. 30:136-145(1993).
[8]
STRUCTURE BY NMR.
PubMed=8771192 [NCBI, ExPASy, EBI, Israel, Japan]
Heinemann B., Andersen K.V., Nielsen P.R., Bech L.M., Poulsen F.M.;
"Structure in solution of a four-helix lipid binding protein.";
Protein Sci. 5:13-23(1996).
[9]
STRUCTURE BY NMR.
DOI=10.1016/S0969-2126(97)00186-X; PubMed=9032083 [NCBI, ExPASy, EBI, Israel, Japan]
Lerche M.H., Kragelund B.B., Bech L.M., Poulsen F.M.;
"Barley lipid-transfer protein complexed with palmitoyl CoA: the structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands.";
Structure 5:291-306(1997).
[10]
STRUCTURE BY NMR OF 27-117.
PubMed=9865943 [NCBI, ExPASy, EBI, Israel, Japan]
Lerche M.H., Poulsen F.M.;
"Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins.";
Protein Sci. 7:2490-2498(1998).
Comments
  • FUNCTION: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
  • TISSUE SPECIFICITY: Aleurone layer of developing and germinating seeds.
  • BIOTECHNOLOGY: During brewing process, structural and chemical modifications of the protein occur. Both unfolding of the structure and glycation should increased the amphiphilicity of the protein, leading to foam-promoting forms that concentrate in beer foams.
  • SIMILARITY: Belongs to the plant LTP family.
  • CAUTION: Was originally thought to be an inhibitor of alpha-amylase or of a protease and was known as PAPI: probable alpha-amylase/protease inhibitor.
  • SEQUENCE CAUTION:
    • Sequence=CAA42832.1; Type=Erroneous gene model prediction;
  • WEB RESOURCE: Name=Protein Spotlight; Note=One beer please - Issue 48 of July 2004; URL="http://www.expasy.org/spotlight/back_issues/sptlt048.shtml";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M15207; AAA32970.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X05168; CAA28805.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X59253; CAA41946.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X60292; CAA42832.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S20507; S20507.
T05947; T05947.
UniGene Hv.23139
3D structure databases
PDB
1BE2; NMR; -; A=27-117.[ExPASy / RCSB / EBI]
1JTB; NMR; -; A=27-117.[ExPASy / RCSB / EBI]
1LIP; NMR; -; A=27-117.[ExPASy / RCSB / EBI]
1MID; X-ray; 1.71 A; A=27-117.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1BE2; -.
1JTB; -.
1LIP; -.
1MID; -.
ModBase P07597.
Organism-specific databases
Gramene P07597; -.
Family and domain databases
InterPro IPR013770; LPT_helical.
IPR003612; LTP/seed_store/tryp_amyl_inhib.
IPR000528; Plant_LTP.
Graphical view of domain structure.
Gene3D G3DSA:1.10.110.10; LPT_helical; 1.
Pfam PF00234; Tryp_alpha_amyl; 1.
Pfam graphical view of domain structure.
PRINTS PR00382; LIPIDTRNSFER.
SMART SM00499; AAI; 1.
SMART graphical view of domain structure.
PROSITE PS00597; PLANT_LTP; 1.
BLOCKS P07597.
Other
LinkHub P07597; -.
ProtoNet P07597.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Lipid-binding; Lipoprotein; Signal; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    26  26      
CHAIN   27   117  91     Non-specific lipid-transfer protein 1. PRO_0000018381
LIPID   33    33        Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester. 
DISULFID   29    76         
DISULFID   39    53         
DISULFID   54    99         
DISULFID   74   113         
HELIX   29    36  8      
HELIX   37    39  3      
HELIX   40    43  4      
HELIX   51    63  13      
HELIX   67    82  16      
HELIX   89    98  10      
HELIX   113   115  3      
Sequence information
Length: 117 AA [This is the length of the unprocessed precursor] Molecular weight: 12301 Da [This is the MW of the unprocessed precursor] CRC64: 31209513AF00E444 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MARAQVLLMA AALVLMLTAA PRAAVALNCG QVDSKMKPCL TYVQGGPGPS GECCNGVRDL 

        70         80         90        100        110 
HNQAQSSGDR QTVCNCLKGI ARGIHNLNLN NAASIPSKCN VNVPYTISPD IDCSRIY 

P07597 in FASTA format

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