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P10762

- APL3_LOCMI

UniProt

P10762 - APL3_LOCMI

Protein

Apolipophorin-3b

Gene
N/A
Organism
Locusta migratoria (Migratory locust)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.

    GO - Biological processi

    1. lipid transport Source: UniProtKB-KW

    Keywords - Biological processi

    Lipid transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Apolipophorin-3b
    Alternative name(s):
    Apolipophorin-IIIb
    Short name:
    ApoLp-IIIb
    OrganismiLocusta migratoria (Migratory locust)
    Taxonomic identifieri7004 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraOrthopteroideaOrthopteraCaeliferaAcridomorphaAcridoideaAcrididaeOedipodinaeLocusta

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 16161 PublicationAdd
    BLAST
    Chaini17 – 179163Apolipophorin-3bPRO_0000002046Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi34 – 341N-linked (GlcNAc...)
    Glycosylationi101 – 1011N-linked (GlcNAc...)

    Keywords - PTMi

    Glycoprotein

    PTM databases

    UniCarbKBiP10762.

    Expressioni

    Tissue specificityi

    Hemolymph.

    Interactioni

    Subunit structurei

    Equilibrium between a soluble monomer and a bound lipoprotein form. Apolipophorin-3 associates with lipophorin during lipid loading until each particle contains 14 molecules of apolipophorin-3 in L.migratoria (5 molecules of apolipophorin-3a and 9 of apolipophorin-3b).

    Structurei

    Secondary structure

    1
    179
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni20 – 234
    Helixi26 – 4419
    Helixi45 – 495
    Helixi55 – 8228
    Helixi88 – 10215
    Beta strandi105 – 1084
    Helixi113 – 13927
    Helixi146 – 1483
    Helixi149 – 17224

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AEPX-ray2.70A20-179[»]
    1LS4NMR-A1-179[»]
    ProteinModelPortaliP10762.
    SMRiP10762. Positions 17-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10762.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati30 – 4011Add
    BLAST
    Repeati41 – 5212Add
    BLAST
    Repeati53 – 608
    Repeati61 – 7818Add
    BLAST
    Repeati79 – 8911Add
    BLAST
    Repeati90 – 9910
    Repeati100 – 11314Add
    BLAST
    Repeati114 – 12714Add
    BLAST
    Repeati128 – 14013Add
    BLAST
    Repeati141 – 15111Add
    BLAST
    Repeati152 – 16514Add
    BLAST
    Repeati166 – 17914Add
    BLAST

    Sequence similaritiesi

    Belongs to the insect apolipophorin-3 family.Curated

    Keywords - Domaini

    Repeat, Signal

    Sequencei

    Sequence statusi: Complete.

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

    P10762-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNTLLAVLML AVAAQARPDA AGHVNIAEAV QQLNHTIVNA AHELHETLGL    50
    PTPDEALNLL TEQANAFKTK IAEVTTSLKQ EAEKHQGSVA EQLNRFARNL 100
    NNSIHDAATS AQPADQLNSL QSALTNVGHQ WQTSQPRPSV AQEAWAPVQS 150
    ALQEAAEKTK EAAANLQNSI QSAVQKPAN 179
    Length:179
    Mass (Da):19,113
    Last modified:July 1, 1989 - v1
    Checksum:i43F38EA477DF5079
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 951R → A in AAA29282. (PubMed:3392027)Curated
    Sequence conflicti111 – 1144AQPA → LNLQ in AAA29282. (PubMed:3392027)Curated
    Sequence conflicti133 – 1408TSQPRPSV → DIATKTQAS in AAA29282. (PubMed:3392027)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03888 mRNA. Translation: AAA29282.1.
    PIRiA28992.
    S14101.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    Lipid freight - Issue 59 of June 2005

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03888 mRNA. Translation: AAA29282.1 .
    PIRi A28992.
    S14101.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AEP X-ray 2.70 A 20-179 [» ]
    1LS4 NMR - A 1-179 [» ]
    ProteinModelPortali P10762.
    SMRi P10762. Positions 17-179.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    UniCarbKBi P10762.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P10762.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of apolipophorin-III from the migratory locust, Locusta migratoria. Potential amphipathic structures and molecular evolution of an insect apolipoprotein."
      Kanost M.R., Boguski M.S., Freeman M., Gordon J.I., Wyatt G.R., Wells M.A.
      J. Biol. Chem. 263:10568-10573(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Different isoforms of an apoprotein (apolipophorin III) associate with lipoproteins in Locusta migratoria."
      van der Horst D.J., van Doorn J.M., Voshol H., Kanost M.R., Ziegler R., Beenakkers A.M.T.
      Eur. J. Biochem. 196:509-517(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-58.
    3. "Molecular structure of an apolipoprotein determined at 2.5-A resolution."
      Breiter D.R., Kanost M.R., Benning M.M., Wesenberg G., Law J.H., Wells M.A., Rayment I., Holden H.M.
      Biochemistry 30:603-608(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiAPL3_LOCMI
    AccessioniPrimary (citable) accession number: P10762
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

    Two isoforms of apolipophorin-3 (a and b) have been found and occur in a ratio of 5a:9b in the hemolymph.

    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