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P07597

- NLTP1_HORVU

UniProt

P07597 - NLTP1_HORVU

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Protein

Non-specific lipid-transfer protein 1

Gene

LTP1

Organism
Hordeum vulgare (Barley)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. lipid binding Source: UniProtKB-KW

GO - Biological processi

  1. lipid transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-specific lipid-transfer protein 1
Short name:
LTP 1
Alternative name(s):
Probable amylase/protease inhibitor
Gene namesi
Name:LTP1
Synonyms:PAPI
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Organism-specific databases

GrameneiP07597.

Pathology & Biotechi

Biotechnological usei

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.1 Publication

Protein family/group databases

Allergomei950. Hor v 14.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 11791Non-specific lipid-transfer protein 1PRO_0000018381Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 76
Lipidationi33 – 331Cis-14-hydroxy-10,13-dioxo-7-heptadecenoic acid aspartate ester1 Publication
Disulfide bondi39 ↔ 53
Disulfide bondi54 ↔ 99
Disulfide bondi74 ↔ 113

Keywords - PTMi

Disulfide bond, Lipoprotein

Expressioni

Tissue specificityi

Aleurone layer of developing and germinating seeds.1 Publication

Gene expression databases

GenevestigatoriP07597.

Structurei

Secondary structure

1
117
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 368
Helixi37 – 393
Helixi40 – 434
Helixi51 – 6313
Helixi67 – 8216
Beta strandi84 – 863
Helixi89 – 9810
Beta strandi107 – 1104
Helixi113 – 1153

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BE2NMR-A27-117[»]
1JTBNMR-A27-117[»]
1LIPNMR-A27-117[»]
1MIDX-ray1.71A27-117[»]
3GSHX-ray1.80A/B27-117[»]
ProteinModelPortaliP07597.
SMRiP07597. Positions 27-117.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07597.

Family & Domainsi

Sequence similaritiesi

Belongs to the plant LTP family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR016140. Bifunc_inhib/LTP/seed_store.
IPR000528. Plant_LTP.
[Graphical view]
PfamiPF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view]
PRINTSiPR00382. LIPIDTRNSFER.
SMARTiSM00499. AAI. 1 hit.
[Graphical view]
SUPFAMiSSF47699. SSF47699. 1 hit.
PROSITEiPS00597. PLANT_LTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07597-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARAQVLLMA AALVLMLTAA PRAAVALNCG QVDSKMKPCL TYVQGGPGPS
60 70 80 90 100
GECCNGVRDL HNQAQSSGDR QTVCNCLKGI ARGIHNLNLN NAASIPSKCN
110
VNVPYTISPD IDCSRIY
Length:117
Mass (Da):12,301
Last modified:April 1, 1988 - v1
Checksum:i31209513AF00E444
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15207 mRNA. Translation: AAA32970.1.
X05168 mRNA. Translation: CAA28805.1.
X59253 Genomic DNA. Translation: CAA41946.1.
X60292 Genomic DNA. Translation: CAA42832.1. Sequence problems.
PIRiS20507.
T05947.
UniGeneiHv.23091.

Cross-referencesi

Web resourcesi

Protein Spotlight

One beer please - Issue 48 of July 2004

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15207 mRNA. Translation: AAA32970.1 .
X05168 mRNA. Translation: CAA28805.1 .
X59253 Genomic DNA. Translation: CAA41946.1 .
X60292 Genomic DNA. Translation: CAA42832.1 . Sequence problems.
PIRi S20507.
T05947.
UniGenei Hv.23091.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
3GSH X-ray 1.80 A/B 27-117 [» ]
ProteinModelPortali P07597.
SMRi P07597. Positions 27-117.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

Allergomei 950. Hor v 14.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei P07597.

Miscellaneous databases

EvolutionaryTracei P07597.

Gene expression databases

Genevestigatori P07597.

Family and domain databases

InterProi IPR016140. Bifunc_inhib/LTP/seed_store.
IPR000528. Plant_LTP.
[Graphical view ]
Pfami PF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view ]
PRINTSi PR00382. LIPIDTRNSFER.
SMARTi SM00499. AAI. 1 hit.
[Graphical view ]
SUPFAMi SSF47699. SSF47699. 1 hit.
PROSITEi PS00597. PLANT_LTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiNLTP1_HORVU
AccessioniPrimary (citable) accession number: P07597
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: October 1, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3