ID   APLP_MANSE              Reviewed;        3305 AA.
AC   Q25490;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 92.
DE   RecName: Full=Apolipophorins;
DE   Contains:
DE     RecName: Full=Apolipophorin-2;
DE     AltName: Full=Apolipophorin II;
DE     AltName: Full=apoLp-2;
DE   Contains:
DE     RecName: Full=Apolipophorin-1;
DE     AltName: Full=Apolipophorin I;
DE     AltName: Full=apoLp-1;
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].
RC   TISSUE=Fat body;
RX   PubMed=9014323; DOI=10.1016/s0965-1748(96)00060-4;
RA   Sundermeyer K., Hendricks J.K., Prasad S.V., Wells M.A.;
RT   "The precursor protein of the structural apolipoproteins of lipophorin:
RT   cDNA and deduced amino acid sequence.";
RL   Insect Biochem. Mol. Biol. 26:735-738(1996).
CC   -!- FUNCTION: Constitutes the major component of lipophorin, which mediates
CC       transport for various types of lipids in hemolymph. Acts by forming
CC       lipoprotein particles that bind lipoproteins and lipids. May be
CC       required for morphogens wingless (wg) and hedgehog (hh) function,
CC       possibly by acting as vehicles for the movement of wg and hh (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Cleaved into 2 chains by furin protease. However, prevention of
CC       cleavage does not impair its function (By similarity). {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
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; U57651; AAB53254.1; -; mRNA.
DR   PIR; T18358; T18358.
DR   SMR; Q25490; -.
DR   PRIDE; Q25490; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.20; -; 1.
DR   Gene3D; 2.20.50.20; -; 1.
DR   Gene3D; 2.30.230.10; -; 1.
DR   InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR   InterPro; IPR009454; Lipid_transpt_open_b-sht.
DR   InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR   InterPro; IPR015816; Vitellinogen_b-sht_N.
DR   InterPro; IPR015255; Vitellinogen_open_b-sht.
DR   InterPro; IPR015817; Vitellinogen_open_b-sht_sub1.
DR   InterPro; IPR001747; Vitellogenin_N.
DR   InterPro; IPR001846; VWF_type-D.
DR   Pfam; PF06448; DUF1081; 1.
DR   Pfam; PF09172; DUF1943; 1.
DR   Pfam; PF01347; Vitellogenin_N; 1.
DR   Pfam; PF00094; VWD; 1.
DR   SMART; SM01169; DUF1943; 1.
DR   SMART; SM00638; LPD_N; 1.
DR   SMART; SM00216; VWD; 1.
DR   SUPFAM; SSF48431; SSF48431; 1.
DR   SUPFAM; SSF56968; SSF56968; 2.
DR   PROSITE; PS51211; VITELLOGENIN; 1.
DR   PROSITE; PS51233; VWFD; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Lipid transport; Lipid-binding; Secreted; Signal; Transport;
KW   Wnt signaling pathway.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..711
FT                   /note="Apolipophorin-2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000041530"
FT   CHAIN           712..3305
FT                   /note="Apolipophorin-1"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000041531"
FT   DOMAIN          39..640
FT                   /note="Vitellogenin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT   DOMAIN          2733..2899
FT                   /note="VWFD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   SITE            711..712
FT                   /note="Cleavage; by furin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        643
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2769
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        2757..2898
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
SQ   SEQUENCE   3305 AA;  366947 MW;  B27D611410285FD7 CRC64;
     MGKSNRLLSV LFVISVLWKA AYGNGKCQIA CKGSSSPSFA AGQKYNYGVE GTVSVYLTGA
     DNQETSLKML GQASVSAISN CELELSVHNM VLSGPDGKKY PCPQGIEKPV RFSYQDGRVG
     PEICAAEDDS RRSLNIKRAI ISLLQAEQKP SVQVDVFGVC PTEVSSSQEG GAVLLHRSRD
     LSRCAHREQG RNDFVNSIAN PDAGIKDLQV LQSMLNVESK VNNGVPEKVS AIEEYLYKPF
     SVGENGARAK VHTKLTLSGK GGAGGGNAHC TESRSIIFDV PHGTSSASGN LNSVISAVKE
     TARTVANDAS SKSAGQFAQL VRIMRTSSKD DLMRIYSQVK AHQLEKRVYL DALLRAGTGE
     SIEASIQILK SKDLSQLEQH LVFLSLGNAR HVNNPALKAA AGLLDMPNLP KEVYLGAGAL
     GGAYCREHDC HNVKPEGIVA LSNKLGSKLQ NCRPKNKPDE DVVVAILKGI RNIRHLEDSL
     IDKLVHCAVD NNVKARVRAV ALEAFHADPC SAKIHKTAMD IMKNRQLDSE IRIKAYLAVI
     ECPCSHSASE IKNLLDSEPV HQVGNFITSS LRHIRSSSNP DKQLAKKHYG QIRTPNKFKV
     DERKYSFYRE MSYKLDALGA GGSVDQTVIY SQTSFLPRSV NFNLTVDLFG QSYNVMELGG
     RQGNLDRVVE HFLGPKSFLR TEDPQALYDN LVKRFQESKK KVEDSLSRGR RSIKSEIDVF
     DKNLKAESAP YNNELDLDIY VKLFGTDAVF LSFGDDKGFD FNKMLDQILG GCNSGINKAK
     HFQQEIRSHL LFMDAELAYP TSVGLPLRLN LIGAATARLD VATNIDIRQI FQSPQNAKAD
     IKFVPSTDFE ISGAFIIDAD AFSTGIKVIT NLHSSTGVHV NAKVLENGRG IDLQIGLPVD
     KQELIAASSD LVFVTAEKGQ KEKQKVIKME KGENEYSACF DQLSGPLGLT MCYDMVLPFP
     IVNRNDKLDS IAKAMGKWPL SGSAKFKLFL EKNDLRGYHI KAVVKEDKDA GRRSFELLLD
     TEGAKTRRSQ LTGEAVYNEN EVGVKLGLEA VGKVIYGHIW AHKKPNELVA SVKGKLDDIE
     YSGKLGFSVQ GNEHRAVYKP IFEYSLPDGS SPGSKKYEVK IDGQVIRECD GRVTKYTFDG
     VHVNLQNAEK PLEICGSVST VAQPREVEFD VEVKHYASLK GSWKGSDVVL AFNNQLNPKI
     NFDLKGKFEN TDSMHNELDI HYGPNRGDNN ARITFSQILK YHVENSKNFN VITKNNLEIR
     AVPFKLVANA DVDPKKIDID IEGQLQDKSA GFNLDARTHI KKEGDYSIKV KANLNNANLE
     AFSRRDIVNA EKSNVENYID MKGVGRYELS GFVLHKTKPN DVNVGFIGHL KINGGGKNED
     FKINIGHIET PAVFSSHATI SGSRGDIIDY LLKIMRTANP NGNFKLVIKD SIAANGQYKV
     TDADGKGNGL IIIDFKKINR KIKGDVRFTA KEPVFNADID LFLNFEKDNS DKVHFSTYNK
     KTDKVMDTKN KLEYAGKRTE VNIHQDGILA VTGKAHTVAE LVLPTERCLS LKIDHDGAFK
     DGLYNGHMDM TISDAPKRGS GASTISYKGK VSNSNLDQEI IDYEGQINFK LKDGKNLQST
     FSLKNNPDGD KFKYEFKSDV NGNLIPKPAN LVATGTYSNS ENEIDETYRL KGSYGSDIGF
     ELAGVGTIKF LDAGDKKYLD DYTLTVRLPF EKAHDIKWVS TVLFLQPQGQ EMTEYTLVES
     VQINADVYKI DANGKVGPKN GYGAVKVLVP HVEPFVLDYN YKSSHEGEKN NNYVELKTKY
     GKGKSASMVV DSSYAPHYST LKVKANTPNN DKFKKLDVTV HSKNPSPDAY SNSVVVDADG
     RVYKIDSSIV LSKAHPVLDI QYHSPSSDKI RRLYLQGSSL SSTQGKLEVK VDNINDICLD
     AVSEANVQKD NVAFKVVANA KELGWKNYGI DISSKDSGSG KRLEFHATND NKNVLSGSTS
     FISKQEGQKT IIEGSGSVKV KEEQKSANFK YIRTVFTDSN EKGVETFFNV ALGERSYVAE
     SRVTNYEYKN SYVYCEEKKQ CAHAEIQSKI DMSTPGMIVN VINAGLDLRK LGVAPELGLQ
     MRDEVSDRRP PRFTLDLHIN KEDRKYHLHA YNTPENGHYA SGVTVRLPSR VMALEYTLTH
     PTSQDLPFPI KGEACLDLDK NRPGHKTSAR FLVDYSNSGS EDKAVAEIGF FHPKIEKEAV
     IRLNAFMKRP ENGCFKIESS ASLCHSALGT DRVAKVMFET TPNSVKFLAD TPFVKAIDVE
     GSFNVNQQQR TQQCLFRICL LEGKPVQMSA LVKDYQYYEF TTEESNRKLS YVGHLIPEKR
     VDISTDIILS GDKKNIAHGA LFLQDNLVKS DYGLSKENFN YFLNALKKDL DTLEDRIKNV
     GEKASKDVEA VTQRAAPYFK KVEDNFRAEW NRFYQEIADD KVFKEISHVF NEIVQYIAKF
     IDEILQGTKR SWTPSCRPTL SHPRNREMYK KQIEPQVKQL YDTLGALMKE YLDGVIDVVA
     HFAAIVTDFF EKHKAELQEL TNVFTEIFKD LTRLVVAQLK ELPPKIAQIY NDIVSQITNM
     PFVVVLQEKW KEFNFAERAV QLVSQAYEAF SKILPTDELK EFAKALNAYL LKKIKEEKME
     ESKELPRAVR EAGQRVLLIT SIPALAVRRP RLRRWTWHHL KLAVGAGASA PSLGAASWSA
     LRQLAAGDGP PALAPRGLPT AQLDPLDEVP NKLRAVVVNG QHIFTFDGRH LTFPGTCRYV
     LIHDHVDRNF TVLMQLANGQ PKALVLEDKS GTIIELKDNG QVILNCQSHG FPVVEQDVFA
     FRQTSGRIGL CSKYGLMAFC TSKFEVCYFE VNGFYLGKLP GLLGDGNNEP YDDFRMPNGK
     ICSSESEFGN SYRLSRSCPA ANAPAHDHHQ MHAPLPKPCE RVFSGTSPLR PLSLMLDIAP
     FRQACIHAVT GADADKDLQQ ACDLARGYRR SRSRGCCPPR CPTPACAART ATGPGSWATP
     TSTNCPTDSL ISSSPLRPLR TTPAHYKNMV VPLVSQLVDM LKGKHCTDIK VFLVGHTSKH
     PYPILYDTDL KLKNAKVSFD DKSRYDRIPF VKTGHEKFDS YSKTVVDFLN YIKIELGITN
     IEASQGQIFD LPLRPGAVKH VIFVTGGPTI SQFFLLETVR ALRNKVIIDE MAMSASLVTS
     TPGLKIGGGK NAAQIVGYEK HGVLLLGEKK QSKDSEAVRA TLEVEDDPFS DAVEFANGVV
     FSASNYAALP AGQQKQFIQT AAHNIIQRMW REQIVQQCTC VFVDPFRVRS VCFNKARTEV
     ARRRK