P10762 (APL3_LOCMI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Apolipophorin-3b Alternative name(s): Apolipophorin-IIIb Short name=ApoLp-IIIb
Organism	Locusta migratoria (Migratory locust)
Taxonomic identifier	7004 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Orthopteroidea › Orthoptera › Caelifera › Acridomorpha › Acridoidea › Acrididae › Oedipodinae › Locusta

Protein attributes

Sequence length	179 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 14 molecules of apolipophorin-3 in L.migratoria (5 molecules of apolipophorin-3a and 9 of apolipophorin-3b).
Subcellular location	Secreted.
Tissue specificity	Hemolymph.
Miscellaneous	Two isoforms of apolipophorin-3 (a and b) have been found and occur in a ratio of 5a:9b in the hemolymph.
Sequence similarities	Belongs to the insect apolipophorin-3 family.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Secreted
Domain	Repeat Signal
PTM	Glycoprotein
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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Ref.2

Chain

17 – 179

163

Apolipophorin-3b

PRO_0000002046

Regions

Repeat

30 – 40

11

Repeat

41 – 52

12

Repeat

53 – 60

8

Repeat

61 – 78

18

Repeat

79 – 89

11

Repeat

90 – 99

10

Repeat

100 – 113

14

Repeat

114 – 127

14

Repeat

128 – 140

13

Repeat

141 – 151

11

Repeat

152 – 165

14

Repeat

166 – 179

14

Amino acid modifications

Glycosylation

34

1

N-linked (GlcNAc...)

Glycosylation

101

1

N-linked (GlcNAc...)

Experimental info

Sequence conflict

95

1

R → A in AAA29282. Ref.1

Sequence conflict

111 – 114

4

AQPA → LNLQ in AAA29282. Ref.1

Sequence conflict

133 – 140

8

TSQPRPSV → DIATKTQAS in AAA29282. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

179

Helix Strand Turn

Details...

Turn

20 – 23

4

Helix

26 – 44

19

Helix

45 – 49

5

Helix

55 – 82

28

Helix

88 – 102

15

Beta strand

105 – 108

4

Helix

113 – 139

27

Helix

146 – 148

3

Helix

149 – 172

24

Sequences

	Sequence		Length	Mass (Da)
	P10762 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 43F38EA477DF5079	FASTA	179	19,113
	10 20 30 40 50 60 MNTLLAVLML AVAAQARPDA AGHVNIAEAV QQLNHTIVNA AHELHETLGL PTPDEALNLL 70 80 90 100 110 120 TEQANAFKTK IAEVTTSLKQ EAEKHQGSVA EQLNRFARNL NNSIHDAATS AQPADQLNSL 130 140 150 160 170 QSALTNVGHQ WQTSQPRPSV AQEAWAPVQS ALQEAAEKTK EAAANLQNSI QSAVQKPAN

References

[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).
+	Additional computationally mapped references.

Web resources

Protein Spotlight

Lipid freight - Issue 59 of June 2005

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03888 mRNA. Translation: AAA29282.1.

PIR

A28992.
S14101.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AEP	X-ray	2.70	A	20-179	[»]
1LS4	NMR	-	A	1-179	[»]

ProteinModelPortal

P10762.

SMR

P10762. Positions 17-179.

ModBase

Search...

PTM databases

GlycoSuiteDB

P10762.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

ProtoNet

Search...

Other

EvolutionaryTrace

P10762.

Entry information

Entry name

APL3_LOCMI

Accession

Primary (citable) accession number: P10762

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)