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P07597

- NLTP1_HORVU

UniProt

P07597 - NLTP1_HORVU

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
  1. 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

    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

    MARAQVLLMA AALVLMLTAA PRAAVALNCG QVDSKMKPCL TYVQGGPGPS    50
    GECCNGVRDL HNQAQSSGDR QTVCNCLKGI ARGIHNLNLN NAASIPSKCN 100
    VNVPYTISPD IDCSRIY 117
    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