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P07597 (NLTP1_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Non-specific lipid-transfer protein 1

Short name=LTP 1
Alternative name(s):
Probable amylase/protease inhibitor
Gene names
Name:LTP1
Synonyms:PAPI
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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. Ref.3

Biotechnological use

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. Ref.7

Sequence similarities

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

The sequence CAA42832.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTransport
   DomainSignal
   LigandLipid-binding
   PTMDisulfide bond
Lipoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processlipid transport

Inferred from electronic annotation. Source: InterPro

   Molecular_functionlipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.4
Chain27 – 11791Non-specific lipid-transfer protein 1
PRO_0000018381

Amino acid modifications

Lipidation331Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester
Disulfide bond29 ↔ 76
Disulfide bond39 ↔ 53
Disulfide bond54 ↔ 99
Disulfide bond74 ↔ 113

Secondary structure

................. 117
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07597 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 31209513AF00E444

FASTA11712,301
        10         20         30         40         50         60 
MARAQVLLMA AALVLMLTAA PRAAVALNCG QVDSKMKPCL TYVQGGPGPS GECCNGVRDL 

        70         80         90        100        110 
HNQAQSSGDR QTVCNCLKGI ARGIHNLNLN NAASIPSKCN VNVPYTISPD IDCSRIY 

« Hide

References

[1]"Selective expression of a probable amylase/protease inhibitor in barley aleurone cells: comparison to the barley amylase/subtilisin inhibitor."
Mundy J., Rogers J.C.
Planta 169:51-63(1986)
Cited for: NUCLEOTIDE SEQUENCE.
[2]"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."
Linnestad C., Loenneborg A., Kalla R., Olsen O.-A.
Plant Physiol. 97:841-843(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: cv. Bomi.
Tissue: Seedling.
[3]"Structure and expression of the barley lipid transfer protein gene Ltp1."
Skriver K., Leah R., Mueller-Uri F., Mundy J., Olsen F.
Plant Mol. Biol. 18:585-589(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Tissue: Seed.
[4]"A 10kD barley seed protein homologous with an alpha-amylase inhibitor from Indian finger millet."
Svensson B., Asano K., Jonassen I., Poulsen F.M., Mundy J., Svendsen I.
Carlsberg Res. Commun. 51:493-500(1986)
Cited for: PROTEIN SEQUENCE OF 27-117.
Strain: cv. Hiproly.
[5]"Coidentity of putative amylase inhibitors from barley and finger millet with phospholipid transfer proteins inferred from amino acid sequence homology."
Bernhard W.R., Somerville C.R.
Arch. Biochem. Biophys. 269:695-697(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A LTP.
[6]"Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification."
Lindorff-Larsen K., Lerche M.H., Poulsen F.M., Roepstorff P., Winther J.R.
J. Biol. Chem. 276:33547-33553(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: LIPIDATION AT ASP-33.
Strain: cv. Optic.
[7]"Barley lipid transfer protein 1 is involved in beer foam formation."
Sorensen S.B., Bech L.M., Muldbjerg M., Beenfeldt T., Breddam K.
Master Brew. Assoc. Am. Tech. Q. 30:136-145(1993) [AGRICOLA] [Europe PMC]
Cited for: BIOTECHNOLOGICAL RELEVANCE.
[8]"Structure in solution of a four-helix lipid binding protein."
Heinemann B., Andersen K.V., Nielsen P.R., Bech L.M., Poulsen F.M.
Protein Sci. 5:13-23(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[9]"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."
Lerche M.H., Kragelund B.B., Bech L.M., Poulsen F.M.
Structure 5:291-306(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[10]"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."
Lerche M.H., Poulsen F.M.
Protein Sci. 7:2490-2498(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 27-117.
+Additional computationally mapped references.

Web resources

Protein Spotlight

One beer please - Issue 48 of July 2004

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15207 mRNA. Translation: AAA32970.1.
X05168 mRNA. Translation: CAA28805.1.
X59253 Genomic DNA. Translation: CAA41946.1.
X60292 Genomic DNA. Translation: CAA42832.1. Sequence problems.
PIRS20507.
T05947.
UniGeneHv.23091.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BE2NMR-A27-117[»]
1JTBNMR-A27-117[»]
1LIPNMR-A27-117[»]
1MIDX-ray1.71A27-117[»]
3GSHX-ray1.80A/B27-117[»]
ProteinModelPortalP07597.
SMRP07597. Positions 27-117.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome950. Hor v 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneP07597.

Gene expression databases

GenevestigatorP07597.

Family and domain databases

InterProIPR016140. Bifunc_inhib/LTP/seed_store.
IPR000528. Plant_LTP.
[Graphical view]
PfamPF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view]
PRINTSPR00382. LIPIDTRNSFER.
SMARTSM00499. AAI. 1 hit.
[Graphical view]
SUPFAMSSF47699. SSF47699. 1 hit.
PROSITEPS00597. PLANT_LTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07597.

Entry information

Entry nameNLTP1_HORVU
AccessionPrimary (citable) accession number: P07597
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references