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Protein

Apolipophorin-3b

Gene
N/A
Organism
Locusta migratoria (Migratory locust)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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.

GO - Biological processi

Complete GO annotation...

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

Complete GO annotation...

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 – 234Combined sources
Helixi26 – 4419Combined sources
Helixi45 – 495Combined sources
Helixi55 – 8228Combined sources
Helixi88 – 10215Combined sources
Beta strandi105 – 1084Combined sources
Helixi113 – 13927Combined sources
Helixi146 – 1483Combined sources
Helixi149 – 17224Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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)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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
J03888 mRNA. Translation: AAA29282.1.
PIRiA28992.
S14101.

3D structure databases

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

PTM databases

UniCarbKBiP10762.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP10762.

Family and domain databases

ProtoNetiSearch...

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: May 27, 2015
This is version 92 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

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 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.