P13276 (APL3_MANSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 80.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Apolipophorin-3 Alternative name(s): Apolipophorin-III Short name=ApoLp-III |
| Organism | Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm) |
| Taxonomic identifier | 7130 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Sphingidae › Sphinginae › Sphingini › Manduca![]() |
Protein attributes
| Sequence length | 189 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 | Assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It thus plays a critical role in the transport of lipids during flight in several species of insects. |
| Subunit structure | Equilibrium between a soluble monomer and a bound lipoprotein form. Apolipophorin-3 associates with lipophorin during lipid loading until each particle contains 9 or 14 molecules of apolipophorin-3. |
| Subcellular location | |
| Tissue specificity | Hemolymph. |
| Sequence similarities | Belongs to the insect apolipophorin-3 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Lipid transport Transport |
| Cellular component | Secreted |
| Domain | Repeat Signal |
| PTM | Cleavage on pair of basic residues |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | lipid transport Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | lipid binding Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Potential | |||||||||||||||||||||||
| Propeptide | 19 – 23 | 5 | PRO_0000002047 | |||||||||||||||||||||||
| Chain | 24 – 189 | 166 | Apolipophorin-3 | PRO_0000002048 | ||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||
| Beta strand | 26 – 28 | 3 | ||||||||||||||||||||||||
| Helix | 34 – 53 | 20 | ||||||||||||||||||||||||
| Helix | 64 – 88 | 25 | ||||||||||||||||||||||||
| Helix | 95 – 111 | 17 | ||||||||||||||||||||||||
| Helix | 112 – 115 | 4 | ||||||||||||||||||||||||
| Helix | 118 – 122 | 5 | ||||||||||||||||||||||||
| Beta strand | 125 – 127 | 3 | ||||||||||||||||||||||||
| Helix | 128 – 150 | 23 | ||||||||||||||||||||||||
| Helix | 158 – 160 | 3 | ||||||||||||||||||||||||
| Helix | 161 – 185 | 25 | ||||||||||||||||||||||||
Sequences
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References
| [1] | "Primary structure and comparative sequence analysis of an insect apolipoprotein. Apolipophorin-III from Manduca sexta." Cole K.D., Warnakulasuriya F.G.J.P., Boguski M.S., Freeman M., Gordon J.I., Clark W.A., Law J.H., Wells M.A. J. Biol. Chem. 262:11794-11800(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. |
| [2] | "The structure of the apolipophorin-III gene from Manduca sexta." Cole K.D., Smith A.F., Wells M.A. Insect Biochem. 20:381-388(1991) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein." Wang J., Sykes B.D., Ryan R.O. Proc. Natl. Acad. Sci. U.S.A. 99:1188-1193(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 24-189. |
Web resources
| Protein Spotlight Lipid freight - Issue 59 of June 2005 |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M17286 mRNA. Translation: AAA29301.1. M79326 Genomic DNA. Translation: AAA29300.1. | ||||||||||||
| PIR | A29793. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P13276. | ||||||||||||
| SMR | P13276. Positions 24-189. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR010009. ApoLp-III. [Graphical view] | ||||||||||||
| Pfam | PF07464. ApoLp-III. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| EvolutionaryTrace | P13276. | ||||||||||||
Entry information
| Entry name | APL3_MANSE | ||||||||
| Accession | Primary (citable) accession number: P13276 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |
| Protein Spotlight Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries |

Clusters with
