ID   APLP_LOCMI              Reviewed;        3380 AA.
AC   Q9U943;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   23-FEB-2022, entry version 85.
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   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], PROTEIN SEQUENCE OF 22-33; 100-117; 204-228;
RP   637-645; 668-682; 721-737; 1299-1308; 1489-1498 AND 2232-2242, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Fat body;
RX   PubMed=11056463;
RX   DOI=10.1002/1096-9861(20001127)427:4<546::aid-cne4>3.0.co;2-h;
RA   Bogerd J., Babin P.J., Kooiman F.P., Andre M., Ballagny C.,
RA   van Marrewijk W.J., van der Horst D.J.;
RT   "Molecular characterization and gene expression in the eye of the
RT   apolipophorin II/I precursor from Locusta migratoria.";
RL   J. Comp. Neurol. 427:546-558(2000).
RN   [2]
RP   SEQUENCE REVISION TO 131; 140; 156; 189; 412-413; 494; 1087; 1103; 1559;
RP   1646-1650; 2614; 2736; 2764; 2888; 3263 AND 3302.
RA   Bogerd J.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   CLEAVAGE BY FURIN, AND MUTAGENESIS OF ARG-717; LYS-719 AND ARG-720.
RX   PubMed=15604521; DOI=10.1194/jlr.m400374-jlr200;
RA   Smolenaars M.M.W., Kasperaitis M.A.M., Richardson P.E., Rodenburg K.W.,
RA   Van der Horst D.J.;
RT   "Biosynthesis and secretion of insect lipoprotein: involvement of furin in
RT   cleavage of the apoB homolog, apolipophorin-II/I.";
RL   J. Lipid Res. 46:412-421(2005).
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   -!- TISSUE SPECIFICITY: Present in brain, hemolymph, fat body and eyes.
CC       {ECO:0000269|PubMed:11056463}.
CC   -!- PTM: Cleaved into 2 chains by furin protease. However, prevention of
CC       cleavage does not impair its function. {ECO:0000269|PubMed:15604521}.
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; AJ130944; CAB51918.2; -; mRNA.
DR   SMR; Q9U943; -.
DR   PRIDE; Q9U943; -.
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   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Lipid transport; Lipid-binding; Secreted;
KW   Signal; Transport; Wnt signaling pathway.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:11056463"
FT   CHAIN           22..720
FT                   /note="Apolipophorin-2"
FT                   /id="PRO_0000041528"
FT   CHAIN           721..3380
FT                   /note="Apolipophorin-1"
FT                   /id="PRO_0000041529"
FT   DOMAIN          40..646
FT                   /note="Vitellogenin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT   DOMAIN          2815..2979
FT                   /note="VWFD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   SITE            720..721
FT                   /note="Cleavage; by furin"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        649
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        969
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2851
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        2839..2978
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT   MUTAGEN         717
FT                   /note="R->D: Abolishes cleavage by furin."
FT                   /evidence="ECO:0000269|PubMed:15604521"
FT   MUTAGEN         717
FT                   /note="R->Q: Partially affects cleavage by furin."
FT                   /evidence="ECO:0000269|PubMed:15604521"
FT   MUTAGEN         719
FT                   /note="K->A: Does not affect cleavage by furin."
FT                   /evidence="ECO:0000269|PubMed:15604521"
FT   MUTAGEN         720
FT                   /note="R->Q: Abolishes cleavage by furin."
FT                   /evidence="ECO:0000269|PubMed:15604521"
SQ   SEQUENCE   3380 AA;  371809 MW;  62526A263A041111 CRC64;
     MGTPPHIWFL LILAISSGGL SAAVGGCNHQ CTPQSSVFQY QKGQTYTYSF EGTTLTSLPG
     TQGEPVRLKL KATADLSVAD DCNKVLRLRG VTVSGPDSKN YANLKDLEAH PVLANFKGSS
     INKQLCSEDG DNQSSLNIKR AILSLLQTPN TKSSTASEVD VFGICPTNVR HSQRGDVTVI
     SKTRNLNRYA SRENLIQETL STRFTGQSDL HATPFLDADL HVEQQIKGGL IVSATSRESY
     LFRPFSNQGN GAKTIVETKL TLTSQNAQPA PPLASFTVPK SIVFEAPHAL ASVPGGSSAI
     TAALHAAESS TKDGVTVDAA EKFRTLVSVL RQSSTTDILK VYNDVKAGAG FSNKHSARNL
     LLDALFRTST GDAVEVIARL LKTKEITANH WYLSLAFIQH ASLKSVVSIS SLLDQKNLPT
     EAFLGIGSFI GRYCREHNCE NVAEFDEVLN KFSKHLSGST TSKAGENRAI AALKALGNIR
     HLNNALGEKV KQLALDKSLP PRVRVAALEV IQSDPCRKNI KQAALQILRD QVEDSELRIK
     AYLAVVECPC DNVVKTISNL LENEPIIQVG SFVVSHLKNL QASTDPSKAE AKEKLGQLKP
     KKIFSSDIRK YSQNYELSYA IDAINAGASV ESNVIFSQSS YLPRSVSLNL TADVFGHSYN
     VFEIAARTEN LDHIIESFLG PKGYIETEDD DKFVDEVEEK TKSLYNRITE RFEKTFRQKR
     SVSKDAVDNI RQQAYKSLLP SQRDRSLDVD LSLKTFGSEL AWFNYDGKHE QKSSERVVDE
     IFDAIDEGLK KSKKFNYDFE PHFTFLDSEL SYPTNLGFPL KLAIDGSIAA RLKLNGEVDV
     RSILRQPENA AFRLEFVPSA AVELTGKLLV DAYVVEGGLK LDYNVHSSTG INVAVHNLND
     LGIDIKVGLP VKKQDIIDVK TDVLTTVKER GHPETSTPLH FNLKGNDYKQ YRGCFDQLSP
     VSGLTFCGNV SVPWVSPTQA AAFYPLNGPS HLSVSIEADD VSEYHFRAEI KKDESAFKSA
     AVLFDTPGSS ADRKVLLLVE KKEKPHQGIT AHLKSGWKEI VAEGLLIDDN NEKSVSAKLV
     IESDEYSIKG GVKISGNPSR QVYKPILEYK APAKDSGAKV KKSHKTSEGI TVDGAVVVER
     TSDKGKYTFQ DLSLKTPKGT FVINGQLDIV PRNYAFDLKL SVDKNELLLN GHLNYAEPKS
     IDVALEVTSP QFPDYGSGFQ LINKRGDDYS DTKIILACGR DLKSDGSRLI LEHFIKGKYE
     TPDTFNLETK GEVLGTGHKI FGKFDIDSKP KHLEYDLKLG FDENEVTSDL VAKRDIKSPD
     DYELKFSAKI LDNSIRIESS REVKPKDDSA FLNTLVVLSG KKYEFQVDVK LAAEDEYHTS
     LKAESNLKIE GKTSVRLITD FTTDAQTVNG HVKVSNEGED FFELIYKLNR GSGNPSGNAK
     LFVKNYLDGA ATFKYNNGVG SGTLQIDVLK LHRKIKATGD LTLSGSQRSA AIDLYWDADR
     DQSKQLLFKT ENDVKEKSID SKNTLKILDK LTTLNFKGSL SGAIDDGEVE GQGELILPVG
     TYLGVKFGRA LHLTQADTKV GLHLQAEGRE SASSTQPVWK SDFLLESALT RDSFVGEAKL
     LFETKGKDDL KLFLSGKSLP QGEKKLISGQ FSGQGSLIGG RTSVIKLNSE IDETFIAYNL
     NSECNQGYRA NIVGKINRGY SPVAVKQIEN TLELLLPFDK LKQLKHTIIG TFSSQPESTP
     EFTVSNVIIW NNENTLKLTG EAAGDEKEGR TKWDLILPKE EPRTLETTWS NAGDNKKAGS
     LSFKWGGNKE AKVSTDIEFT SDNQPQILHL KATSPTEKFG IFDLALSLKK NADPADKIDF
     ELTVTADQKK TDVKGSLGLA PGVPIIDVVA VQPSGTSKVF VDFLRKSDSE LHGAIELQWV
     AFGGGHLTAN GDIKLDIDDF YLKLDVDSPK FNFNKWHLEA GQRAAKGSKR IVFTAKSAEK
     VLFSGSTNFH SKAENNKISY SGNGQVRIGD KAHAFNFRSS RQNLIQDANK EIGVEYNLDF
     KIAGHGSLHN ILKVTNKELH ALGKQCSEGK PNCAVVEIKS KVSAADAKET THDLVFLVDL
     KSVGVDTGVA FTAETVRRGF WLIDEQASLT LSHNGETTYK YKGYLKESGS GFTLTLPSRV
     IAAEVKLSSD VKPNHSKQQI SASVWLDKTR LPNSFSSVSI LLEEIEDKNT DKYVSQLRFT
     HPNLEKDLTV KGYVQIGLEN KLFDSNLEID IFKQKNQKIS ISSTVVEQKQ NDVVKYLSTL
     DVKSKGHELD VTGRGEATVK PSLIALQSVL KYKKDKRIKE FKNFQFEVST EKLLVHVKVP
     NHHLLHIDAN TKINDKHASG DASVHIIGLP TSVIHIEGEN KGFPVVKGTI SSEGTPNKLE
     LIADLSDGLL VEADFISESG KKELFYTFLS GKKDSRKPEF RWSVENIQSA LEPHKNDIQE
     VLNKLKEISD EAGNEITKES SRLADSLKAG LPNFRRFVNT YETQLKALKE EIANDKVLKE
     ISENWKEVIG DAAEVVSTLV NGILVTIDAL LKTLNELAES VLDALKKSLP ALKDSYKQAV
     DAIVGIAKSL TQSLVNILSS AAEILKKHEA DIKEYLSVLA DLANDVGKFV TKITGVIYEG
     VVEFSKPIKE KLDGLKFGVA IEFGKVVEQL QNLIVPQELL AFAQEIVSEL KETTLTPEIQ
     DLLQAIEKYL EKVSKKKDAD VEKELKLIFE KAIDAVESVI NFVVSEITGG DHTKDLYDIN
     IPTVLPSFIQ LPRVFSVRFS PLIYLVSNGV PCLSDLLASY RPSLRFDNII PPYDATAILL
     NSHHFFTFDR RHLTFKGICS YILAQDVQDG NFTIIANIEG GSLKSIIVSD QATTFELASD
     KSLLVNGRPT EYPADEGEFH AWREYNRVGI QTKAGVKVTC ETSIELCTFE INGFYFGKTR
     GLLGTINNEP WDDFTKPDGQ VASKANEFGN AWKVDAQCAN VDGVDHHEHS IKVEECEEVF
     SKASLLSPCS LFLDPAPYLE ACSHIAHEAT TKEEKQLAAC RTAAAYVQAC SVENVFVSVP
     PHCVHCSVNG DAAIDIGQSF SVKVPQKSAD ILIVLEQVTG NAETVKDFVS PIVSQLTQEL
     SSRGISDVWI SLLGYGAPGQ EYPHLYTSSG GKLSYDGKQK NIQFGERKVL GPFPFDNFTE
     SIDWLDEFTD QAFHLITTAD TILDYPFRPG AAKSIIYVLD TSCETTLFLK HLPVKALKLK
     DAIGSPGIVL HLVTNVDSVQ SKNIVGFDTN HAYYNQEGKK RVVSEVTGNE KAALKISETA
     CGQIALATSG TVFNKNNLKQ TKKFVAQHIA DSLTNVELTQ DCKCLPVEGI HTRAVCAVTG
     AREKEHLSVK GVKGTKGVKG