ID   APL3_MANSE              Reviewed;         189 AA.
AC   P13276;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Apolipophorin-3;
DE   AltName: Full=Apolipophorin-III;
DE            Short=ApoLp-III;
DE   Flags: Precursor;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3040717; DOI=10.1016/s0021-9258(18)60882-8;
RA   Cole K.D., Warnakulasuriya F.G.J.P., Boguski M.S., Freeman M., Gordon J.I.,
RA   Clark W.A., Law J.H., Wells M.A.;
RT   "Primary structure and comparative sequence analysis of an insect
RT   apolipoprotein. Apolipophorin-III from Manduca sexta.";
RL   J. Biol. Chem. 262:11794-11800(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Cole K.D., Smith A.F., Wells M.A.;
RT   "The structure of the apolipophorin-III gene from Manduca sexta.";
RL   Insect Biochem. 20:381-388(1991).
RN   [3]
RP   STRUCTURE BY NMR OF 24-189.
RX   PubMed=11818551; DOI=10.1073/pnas.032565999;
RA   Wang J., Sykes B.D., Ryan R.O.;
RT   "Structural basis for the conformational adaptability of apolipophorin III,
RT   a helix-bundle exchangeable apolipoprotein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:1188-1193(2002).
CC   -!- FUNCTION: Assists in the loading of diacylglycerol, generated from
CC       triacylglycerol stores in the fat body through the action of
CC       adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. It
CC       increases the lipid carrying capacity of lipophorin by covering the
CC       expanding hydrophobic surface resulting from diacylglycerol uptake. It
CC       thus plays a critical role in the transport of lipids during flight in
CC       several species of insects.
CC   -!- SUBUNIT: Equilibrium between a soluble monomer and a bound lipoprotein
CC       form. Apolipophorin-3 associates with lipophorin during lipid loading
CC       until each particle contains 9 or 14 molecules of apolipophorin-3.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Hemolymph.
CC   -!- SIMILARITY: Belongs to the insect apolipophorin-3 family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Lipid freight - Issue 59 of
CC       June 2005;
CC       URL="https://web.expasy.org/spotlight/back_issues/059";
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DR   EMBL; M17286; AAA29301.1; -; mRNA.
DR   EMBL; M79326; AAA29300.1; -; Genomic_DNA.
DR   PIR; A29793; A29793.
DR   PDB; 1EQ1; NMR; -; A=24-189.
DR   PDBsum; 1EQ1; -.
DR   AlphaFoldDB; P13276; -.
DR   SMR; P13276; -.
DR   EvolutionaryTrace; P13276; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010009; ApoLp-III.
DR   Pfam; PF07464; ApoLp-III; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Lipid transport; Repeat; Secreted; Signal;
KW   Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..23
FT                   /id="PRO_0000002047"
FT   CHAIN           24..189
FT                   /note="Apolipophorin-3"
FT                   /id="PRO_0000002048"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:1EQ1"
FT   HELIX           34..53
FT                   /evidence="ECO:0007829|PDB:1EQ1"
FT   HELIX           64..88
FT                   /evidence="ECO:0007829|PDB:1EQ1"
FT   HELIX           95..111
FT                   /evidence="ECO:0007829|PDB:1EQ1"
FT   HELIX           112..115
FT                   /evidence="ECO:0007829|PDB:1EQ1"
FT   HELIX           118..122
FT                   /evidence="ECO:0007829|PDB:1EQ1"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:1EQ1"
FT   HELIX           128..150
FT                   /evidence="ECO:0007829|PDB:1EQ1"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:1EQ1"
FT   HELIX           161..185
FT                   /evidence="ECO:0007829|PDB:1EQ1"
SQ   SEQUENCE   189 AA;  20793 MW;  B1412640AB622169 CRC64;
     MAAKFVVVLA ACVALSHSAM VRRDAPAGGN AFEEMEKHAK EFQKTFSEQF NSLVNSKNTQ
     DFNKALKDGS DSVLQQLSAF SSSLQGAISD ANGKAKEALE QARQNVEKTA EELRKAHPDV
     EKEANAFKDK LQAAVQTTVQ ESQKLAKEVA SNMEETNKKL APKIKQAYDD FVKHAEEVQK
     KLHEAATKQ