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Protein

Non-specific lipid-transfer protein

Gene
N/A
Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 3 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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Non-specific lipid-transfer protein
Short name:
LTP
Alternative name(s):
Phospholipid transfer protein
Short name:
PLTP
Allergen: Zea m 14
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Unplaced

Organism-specific databases

MaizeGDBi25447.

Pathology & Biotechi

Allergenic propertiesi

Causes an allergic reaction in human.

Keywords - Diseasei

Allergen

Protein family/group databases

Allergomei3534. Zea m 14.0101.
3535. Zea m 14.0102.
684. Zea m 14.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 12093Non-specific lipid-transfer proteinPRO_0000018389Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 79By similarity
Disulfide bondi41 ↔ 56By similarity
Disulfide bondi57 ↔ 102By similarity
Disulfide bondi77 ↔ 116By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP19656.
PRIDEiP19656.

Interactioni

Protein-protein interaction databases

STRINGi4577.GRMZM2G101958_P01.

Structurei

Secondary structure

1
120
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 388Combined sources
Helixi39 – 413Combined sources
Helixi42 – 454Combined sources
Beta strandi49 – 513Combined sources
Helixi54 – 6613Combined sources
Helixi70 – 8516Combined sources
Helixi92 – 10110Combined sources
Helixi116 – 1183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AFHNMR-A28-120[»]
1FK0X-ray1.80A28-120[»]
1FK1X-ray1.80A28-120[»]
1FK2X-ray1.80A28-120[»]
1FK3X-ray1.80A28-120[»]
1FK4X-ray1.80A28-120[»]
1FK5X-ray1.30A28-120[»]
1FK6X-ray1.90A28-120[»]
1FK7X-ray1.90A28-120[»]
1MZLX-ray1.90A28-120[»]
1MZMX-ray1.78A28-120[»]
ProteinModelPortaliP19656.
SMRiP19656. Positions 28-120.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19656.

Family & Domainsi

Sequence similaritiesi

Belongs to the plant LTP family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410J475. Eukaryota.
ENOG410YWBC. LUCA.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P19656-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARTQQLAVV ATAVVALVLL AAATSEAAIS CGQVASAIAP CISYARGQGS
60 70 80 90 100
GPSAGCCSGV RSLNNAARTT ADRRAACNCL KNAAAGVSGL NAGNAASIPS
110 120
KCGVSIPYTI STSTDCSRVN
Length:120
Mass (Da):11,705
Last modified:February 1, 1991 - v1
Checksum:i28F27EBAE3910218
GO
Isoform 2 (identifier: P19656-2) [UniParc]FASTAAdd to basket

Also known as: long

The sequence of this isoform differs from the canonical sequence as follows:
     119-120: VN → YSRRMHASAD

Show »
Length:128
Mass (Da):12,667
Checksum:iC9921F66B1F43762
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei119 – 1202VN → YSRRMHASAD in isoform 2. CuratedVSP_003147

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04176 mRNA. Translation: AAA33493.1.
M57249 mRNA. Translation: AAA33494.1.
PIRiA31779.
S45635.
UniGeneiZm.89638.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04176 mRNA. Translation: AAA33493.1.
M57249 mRNA. Translation: AAA33494.1.
PIRiA31779.
S45635.
UniGeneiZm.89638.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AFHNMR-A28-120[»]
1FK0X-ray1.80A28-120[»]
1FK1X-ray1.80A28-120[»]
1FK2X-ray1.80A28-120[»]
1FK3X-ray1.80A28-120[»]
1FK4X-ray1.80A28-120[»]
1FK5X-ray1.30A28-120[»]
1FK6X-ray1.90A28-120[»]
1FK7X-ray1.90A28-120[»]
1MZLX-ray1.90A28-120[»]
1MZMX-ray1.78A28-120[»]
ProteinModelPortaliP19656.
SMRiP19656. Positions 28-120.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G101958_P01.

Protein family/group databases

Allergomei3534. Zea m 14.0101.
3535. Zea m 14.0102.
684. Zea m 14.

Proteomic databases

PaxDbiP19656.
PRIDEiP19656.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MaizeGDBi25447.

Phylogenomic databases

eggNOGiENOG410J475. Eukaryota.
ENOG410YWBC. LUCA.

Miscellaneous databases

EvolutionaryTraceiP19656.

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]
ProtoNetiSearch...

Publicationsi

  1. "Phospholipid transfer protein: full-length cDNA and amino acid sequence in maize. Amino acid sequence homologies between plant phospholipid transfer proteins."
    Tchang F., This P., Stiefel V., Arondel V., Morch M.-D., Pages M., Puigdomenech P., Grellet F., Delseny M., Bouillon P., Huet J.-C., Guerbette F., Beauvais-Cante F., Duranton H., Pernollet J.-C., Kader J.-C.
    J. Biol. Chem. 263:16849-16855(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 28-120.
    Tissue: Seed.
  2. "Multiple mRNA coding for phospholipid-transfer protein from Zea mays arise from alternative splicing."
    Arondel V., Tchang F., Baillet B., Vignols F., Grellet F., Delseny M., Kader J.-C., Puigdomenech P.
    Gene 99:133-136(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings."
    Shin D.H., Lee J.Y., Hwang K.Y., Kim K.K., Suh S.W.
    Structure 3:189-199(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  4. "Two-dimensional 1H-NMR studies of maize lipid-transfer protein. Sequence-specific assignment and secondary structure."
    Petit M.-C., Sodano P., Marion D., Ptak M.
    Eur. J. Biochem. 222:1047-1054(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  5. "Solution structure and lipid binding of a nonspecific lipid transfer protein extracted from maize seeds."
    Gomar J., Petit M.-C., Sodano P., Sy D., Marion D., Kader J.-C., Vovelle F., Ptak M.
    Protein Sci. 5:565-577(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiNLTP_MAIZE
AccessioniPrimary (citable) accession number: P19656
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: February 17, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Allergens
    Nomenclature of allergens and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.