Reviewed, UniProtKB/Swiss-Prot P07597 (NLTP1_HORVU)

Names and origin

Protein names

Recommended name:
    Non-specific lipid-transfer protein 1
      Short name=LTP 1
Alternative name(s):
    Probable amylase/protease inhibitor

Gene names

Name:	LTP1
Synonyms:	PAPI

Organism

Hordeum vulgare (Barley)

Taxonomic identifier

4513 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	117 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Transport
Domain	Signal
Ligand	Lipid-binding
PTM	Disulfide bond Lipoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid transport Inferred from electronic annotation. Source: InterPro
Molecular function	lipid binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.4

Chain

27 – 117

91

Non-specific lipid-transfer protein 1

PRO_0000018381

Amino acid modifications

Lipidation

33

1

Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester

Disulfide bond

29 ↔ 76

Disulfide bond

39 ↔ 53

Disulfide bond

54 ↔ 99

Disulfide bond

74 ↔ 113

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

117

Helix Strand Turn

Details...

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

Sequences

	Sequence		Length	Mass (Da)
	P07597-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 31209513AF00E444	FASTA	117	12,301
	10 20 30 40 50 60 MARAQVLLMA AALVLMLTAA PRAAVALNCG QVDSKMKPCL TYVQGGPGPS GECCNGVRDL 70 80 90 100 110 HNQAQSSGDR QTVCNCLKGI ARGIHNLNLN NAASIPSKCN VNVPYTISPD IDCSRIY

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: 16668480] [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: 1536930] [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: 2465737] [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: 11435437] [Abstract] Cited for: LIPID MODIFICATION OF 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: IND20411110] 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: 8771192] [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: 9032083] [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: 9865943] [Abstract] Cited for: STRUCTURE BY NMR OF 27-117.

Web resources

Protein Spotlight

One beer please - Issue 48 of July 2004

Cross-references

Sequence databases

EMBLGenBankDDBJ

M15207 mRNA. Translation: AAA32970.1.
X05168 mRNA. Translation: CAA28805.1.
X59253 Genomic DNA. Translation: CAA41946.1.
X60292 Genomic DNA. Translation: CAA42832.1. Sequence problems.

PIR

S20507.
T05947.

UniGene

Hv.23139

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BE2	NMR	-	A	27-117	[»]
1JTB	NMR	-	A	27-117	[»]
1LIP	NMR	-	A	27-117	[»]
1MID	X-ray	1.71	A	27-117	[»]
3CEE	X-ray	1.80	A/B	27-117	[»]

ModBase

Search...

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]

Gene3D

G3DSA:1.10.110.10. LPT_helical. 1 hit.

Pfam

PF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view]

PRINTS

PR00382. LIPIDTRNSFER.

SMART

SM00499. AAI. 1 hit.
[Graphical view]

PROSITE

PS00597. PLANT_LTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

NLTP1_HORVU

Accession

Primary (citable) accession number: P07597

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)