APL3_LOCMI
ID APL3_LOCMI Reviewed; 179 AA.
AC P10762;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Apolipophorin-3b;
DE AltName: Full=Apolipophorin-IIIb;
DE Short=ApoLp-IIIb;
DE Flags: Precursor;
OS Locusta migratoria (Migratory locust).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC Acridoidea; Acrididae; Oedipodinae; Locusta.
OX NCBI_TaxID=7004;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3392027; DOI=10.1016/s0021-9258(18)38008-6;
RA Kanost M.R., Boguski M.S., Freeman M., Gordon J.I., Wyatt G.R., Wells M.A.;
RT "Primary structure of apolipophorin-III from the migratory locust, Locusta
RT migratoria. Potential amphipathic structures and molecular evolution of an
RT insect apolipoprotein.";
RL J. Biol. Chem. 263:10568-10573(1988).
RN [2]
RP PROTEIN SEQUENCE OF 17-58.
RX PubMed=2007409; DOI=10.1111/j.1432-1033.1991.tb15843.x;
RA van der Horst D.J., van Doorn J.M., Voshol H., Kanost M.R., Ziegler R.,
RA Beenakkers A.M.T.;
RT "Different isoforms of an apoprotein (apolipophorin III) associate with
RT lipoproteins in Locusta migratoria.";
RL Eur. J. Biochem. 196:509-517(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=1988048; DOI=10.1021/bi00217a002;
RA Breiter D.R., Kanost M.R., Benning M.M., Wesenberg G., Law J.H.,
RA Wells M.A., Rayment I., Holden H.M.;
RT "Molecular structure of an apolipoprotein determined at 2.5-A resolution.";
RL Biochemistry 30:603-608(1991).
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 14 molecules of apolipophorin-3 in
CC L.migratoria (5 molecules of apolipophorin-3a and 9 of apolipophorin-
CC 3b).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Hemolymph.
CC -!- MISCELLANEOUS: Two isoforms of apolipophorin-3 (a and b) have been
CC found and occur in a ratio of 5a:9b in the 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; J03888; AAA29282.1; -; mRNA.
DR PIR; A28992; A28992.
DR PIR; S14101; S14101.
DR PDB; 1AEP; X-ray; 2.70 A; A=20-179.
DR PDB; 1LS4; NMR; -; A=1-179.
DR PDBsum; 1AEP; -.
DR PDBsum; 1LS4; -.
DR AlphaFoldDB; P10762; -.
DR SMR; P10762; -.
DR GlyConnect; 55; 5 N-Linked glycans.
DR EvolutionaryTrace; P10762; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Lipid transport;
KW Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:2007409"
FT CHAIN 17..179
FT /note="Apolipophorin-3b"
FT /id="PRO_0000002046"
FT REPEAT 30..40
FT REPEAT 41..52
FT REPEAT 53..60
FT REPEAT 61..78
FT REPEAT 79..89
FT REPEAT 90..99
FT REPEAT 100..113
FT REPEAT 114..127
FT REPEAT 128..140
FT REPEAT 141..151
FT REPEAT 152..165
FT REPEAT 166..179
FT REGION 152..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT CONFLICT 95
FT /note="R -> A (in Ref. 1; AAA29282)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..114
FT /note="AQPA -> LNLQ (in Ref. 1; AAA29282)"
FT /evidence="ECO:0000305"
FT CONFLICT 133..140
FT /note="TSQPRPSV -> DIATKTQAS (in Ref. 1; AAA29282)"
FT /evidence="ECO:0000305"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:1LS4"
FT HELIX 26..44
FT /evidence="ECO:0007829|PDB:1AEP"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:1AEP"
FT HELIX 55..82
FT /evidence="ECO:0007829|PDB:1AEP"
FT HELIX 88..102
FT /evidence="ECO:0007829|PDB:1AEP"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1AEP"
FT HELIX 113..140
FT /evidence="ECO:0007829|PDB:1AEP"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1AEP"
FT HELIX 149..172
FT /evidence="ECO:0007829|PDB:1AEP"
SQ SEQUENCE 179 AA; 19113 MW; 43F38EA477DF5079 CRC64;
MNTLLAVLML AVAAQARPDA AGHVNIAEAV QQLNHTIVNA AHELHETLGL PTPDEALNLL
TEQANAFKTK IAEVTTSLKQ EAEKHQGSVA EQLNRFARNL NNSIHDAATS AQPADQLNSL
QSALTNVGHQ WQTSQPRPSV AQEAWAPVQS ALQEAAEKTK EAAANLQNSI QSAVQKPAN
