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Q0IQK9 (NLTP1_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 40. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=LTP 1
Short name=PAPI
Gene names
Name:LTP
Ordered Locus Names:Os12g0115100, LOC_Os12g02320
ORF Names:OsJ_033644
OrganismOryza sativa subsp. japonica (Rice)
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Protein attributes

Sequence length116 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 (external part) of the seeds.

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.

Ontologies

Keywords
   Biological processTransport
   DomainSignal
   LigandLipid-binding
   PTMDisulfide bond
   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 – 2525 Ref.5
Chain26 – 11691Non-specific lipid-transfer protein 1
PRO_0000018391

Amino acid modifications

Disulfide bond28 ↔ 75
Disulfide bond38 ↔ 52
Disulfide bond53 ↔ 98
Disulfide bond73 ↔ 112

Secondary structure

............... 116
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q0IQK9 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 54612FE0D79F9D5D

FASTA11611,345
        10         20         30         40         50         60 
MARAQLVLVA LVAALLLAAP HAAVAITCGQ VNSAVGPCLT YARGGAGPSA ACCSGVRSLK 

        70         80         90        100        110 
AAASTTADRR TACNCLKNAA RGIKGLNAGN AASIPSKCGV SVPYTISASI DCSRVS 

« Hide

References

« Hide 'large scale' references
[1]"The sequence of rice chromosomes 11 and 12, rich in disease resistance genes and recent gene duplications."
The rice chromosomes 11 and 12 sequencing consortia
BMC Biol. 3:20-20(2005) [PubMed: 16188032] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[2]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed: 16100779] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"The rice annotation project database (RAP-DB): 2008 update."
The rice annotation project (RAP)
Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed: 18089549] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: cv. Nipponbare.
[4]"The genomes of Oryza sativa: a history of duplications."
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. expand/collapse author list , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
PLoS Biol. 3:266-281(2005) [PubMed: 15685292] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[5]"Amino acid sequence of a probable amylase/protease inhibitor from rice seeds."
Yu Y.G., Chung C.H., Fowler A., Suh S.W.
Arch. Biochem. Biophys. 265:466-475(1988) [PubMed: 2458699] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-116.
Tissue: Seed.
[6]"Rice non-specific lipid transfer protein: the 1.6-A crystal structure in the unliganded state reveals a small hydrophobic cavity."
Lee J.Y., Min K., Cha H., Shin D.H., Hwang K.Y., Suh S.W.
J. Mol. Biol. 276:437-448(1998) [PubMed: 9512714] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
Tissue: Seed.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DP000011 Genomic DNA. Translation: ABA96284.1.
AP008218 Genomic DNA. Translation: BAF29006.1.
CM000149 Genomic DNA. Translation: EAZ19435.1.
RefSeqNP_001065987.1. NM_001072519.1.
UniGeneOs.8629.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BV2NMR-A26-116[»]
1RZLX-ray1.60A26-116[»]
1UVAX-ray2.50A26-116[»]
1UVBX-ray2.10A26-116[»]
1UVCX-ray2.00A/B26-116[»]
ProteinModelPortalQ0IQK9.
SMRQ0IQK9. Positions 26-116.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0IQK9.

Protein family/group databases

Allergome2788. Ory s 14.

Proteomic databases

PRIDEQ0IQK9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsLOC_Os12g02320.1; LOC_Os12g02320.1; LOC_Os12g02320.
GeneID4351318.
KEGGosa:4351318.

Organism-specific databases

GrameneP23096.

Phylogenomic databases

GeneTreeEPGT00050000004582.
HOGENOMHBG744832.
OMATESTIQC.
PhylomeDBQ0IQK9.
ProtClustDBCLSN2698338.

Family and domain databases

InterProIPR016140. Bifunc_inhib/LTP/seed_store.
IPR013770. Lipid_transfer_prot_hlx-dom.
IPR003612. LTP/seed_store/tryp_amyl_inhib.
IPR000528. Plant_LTP.
[Graphical view]
Gene3DG3DSA:1.10.110.10. LPT_helical. 1 hit.
PfamPF00234. Tryp_alpha_amyl. 1 hit.
[Graphical view]
PRINTSPR00382. LIPIDTRNSFER.
SMARTSM00499. AAI. 1 hit.
[Graphical view]
SUPFAMSSF47699. Bifunc_inhib/LTP/seed_store. 1 hit.
PROSITEPS00597. PLANT_LTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNLTP1_ORYSJ
AccessionPrimary (citable) accession number: Q0IQK9
Secondary accession number(s): O22484 expand/collapse secondary AC list , P23096, P93434, Q2QYL1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: October 3, 2006
Last modified: December 14, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families