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Protein

Apolipophorin-3b

Gene
N/A
Organism
Locusta migratoria (Migratory locust)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

Miscellaneous

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

GO - Biological processi

Keywordsi

Biological processLipid 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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraPolyneopteraOrthopteraCaeliferaAcridideaAcridomorphaAcridoideaAcrididaeOedipodinaeLocusta

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 161 PublicationAdd BLAST16
ChainiPRO_000000204617 – 179Apolipophorin-3bAdd BLAST163

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi34N-linked (GlcNAc...) asparagine1
Glycosylationi101N-linked (GlcNAc...) asparagine1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP10762

PTM databases

GlyConnecti55
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

1179
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni20 – 23Combined sources4
Helixi26 – 44Combined sources19
Helixi45 – 49Combined sources5
Helixi55 – 82Combined sources28
Helixi88 – 102Combined sources15
Beta strandi105 – 108Combined sources4
Helixi113 – 140Combined sources28
Helixi146 – 148Combined sources3
Helixi149 – 172Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AEPX-ray2.70A20-179[»]
1LS4NMR-A1-179[»]
ProteinModelPortaliP10762
SMRiP10762
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10762

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati30 – 40Add BLAST11
Repeati41 – 52Add BLAST12
Repeati53 – 608
Repeati61 – 78Add BLAST18
Repeati79 – 89Add BLAST11
Repeati90 – 9910
Repeati100 – 113Add BLAST14
Repeati114 – 127Add BLAST14
Repeati128 – 140Add BLAST13
Repeati141 – 151Add BLAST11
Repeati152 – 165Add BLAST14
Repeati166 – 179Add BLAST14

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

        10         20         30         40         50
MNTLLAVLML AVAAQARPDA AGHVNIAEAV QQLNHTIVNA AHELHETLGL
60 70 80 90 100
PTPDEALNLL TEQANAFKTK IAEVTTSLKQ EAEKHQGSVA EQLNRFARNL
110 120 130 140 150
NNSIHDAATS AQPADQLNSL QSALTNVGHQ WQTSQPRPSV AQEAWAPVQS
160 170
ALQEAAEKTK EAAANLQNSI QSAVQKPAN
Length:179
Mass (Da):19,113
Last modified:July 1, 1989 - v1
Checksum:i43F38EA477DF5079
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti95R → A in AAA29282 (PubMed:3392027).Curated1
Sequence conflicti111 – 114AQPA → LNLQ in AAA29282 (PubMed:3392027).Curated4
Sequence conflicti133 – 140TSQPRPSV → DIATKTQAS in AAA29282 (PubMed:3392027).Curated8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03888 mRNA Translation: AAA29282.1
PIRiA28992
S14101

Entry informationi

Entry nameiAPL3_LOCMI
AccessioniPrimary (citable) accession number: P10762
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 23, 2018
This is version 101 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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

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