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Q9U943 (APLP_LOCMI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Apolipophorins

Cleaved into the following 2 chains:

  1. Apolipophorin-2
    Alternative name(s):
    Apolipophorin II
    apoLp-2
  2. Apolipophorin-1
    Alternative name(s):
    Apolipophorin I
    apoLp-1
OrganismLocusta migratoria (Migratory locust)
Taxonomic identifier7004 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Orthopteroidea › Orthoptera › Caelifera › Acridomorpha › Acridoidea › Acrididae › Oedipodinae › Locusta

Protein attributes

Sequence length3380 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Constitutes the major component of lipophorin, which mediates transport for various types of lipids in hemolymph. Acts by forming lipoprotein particles that bind lipoproteins and lipids. May be required for morphogens wingless (wg) and hedgehog (hh) function, possibly by acting as vehicles for the movement of wg and hh By similarity.

Subcellular location

Secreted.

Tissue specificity

Present in brain, hemolymph, fat body and eyes. Ref.1

Post-translational modification

Cleaved into 2 chains by furin protease. However, prevention of cleavage does not impair its function.

N-glycosylated By similarity.

Sequence similarities

Contains 1 vitellogenin domain.

Contains 1 VWFD domain.

Ontologies

Keywords
   Biological processLipid transport
Transport
Wnt signaling pathway
   Cellular componentSecreted
   DomainSignal
   LigandLipid-binding
   PTMCleavage on pair of basic residues
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processWnt receptor signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

lipid transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.1
Chain22 – 720699Apolipophorin-2
PRO_0000041528
Chain721 – 33802660Apolipophorin-1
PRO_0000041529

Regions

Domain40 – 646607Vitellogenin
Domain2816 – 3012197VWFD

Sites

Site720 – 7212Cleavage; by furin

Amino acid modifications

Glycosylation1321N-linked (GlcNAc...) Potential
Glycosylation6491N-linked (GlcNAc...) Potential
Glycosylation9691N-linked (GlcNAc...) Potential
Glycosylation21741N-linked (GlcNAc...) Potential
Glycosylation28511N-linked (GlcNAc...) Potential
Glycosylation31771N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis7171R → D: Abolishes cleavage by furin. Ref.3
Mutagenesis7171R → Q: Partially affects cleavage by furin. Ref.3
Mutagenesis7191K → A: Does not affect cleavage by furin. Ref.3
Mutagenesis7201R → Q: Abolishes cleavage by furin. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9U943 [UniParc].

Last modified July 10, 2007. Version 2.
Checksum: 62526A263A041111

FASTA3,380371,809
        10         20         30         40         50         60 
MGTPPHIWFL LILAISSGGL SAAVGGCNHQ CTPQSSVFQY QKGQTYTYSF EGTTLTSLPG 

        70         80         90        100        110        120 
TQGEPVRLKL KATADLSVAD DCNKVLRLRG VTVSGPDSKN YANLKDLEAH PVLANFKGSS 

       130        140        150        160        170        180 
INKQLCSEDG DNQSSLNIKR AILSLLQTPN TKSSTASEVD VFGICPTNVR HSQRGDVTVI 

       190        200        210        220        230        240 
SKTRNLNRYA SRENLIQETL STRFTGQSDL HATPFLDADL HVEQQIKGGL IVSATSRESY 

       250        260        270        280        290        300 
LFRPFSNQGN GAKTIVETKL TLTSQNAQPA PPLASFTVPK SIVFEAPHAL ASVPGGSSAI 

       310        320        330        340        350        360 
TAALHAAESS TKDGVTVDAA EKFRTLVSVL RQSSTTDILK VYNDVKAGAG FSNKHSARNL 

       370        380        390        400        410        420 
LLDALFRTST GDAVEVIARL LKTKEITANH WYLSLAFIQH ASLKSVVSIS SLLDQKNLPT 

       430        440        450        460        470        480 
EAFLGIGSFI GRYCREHNCE NVAEFDEVLN KFSKHLSGST TSKAGENRAI AALKALGNIR 

       490        500        510        520        530        540 
HLNNALGEKV KQLALDKSLP PRVRVAALEV IQSDPCRKNI KQAALQILRD QVEDSELRIK 

       550        560        570        580        590        600 
AYLAVVECPC DNVVKTISNL LENEPIIQVG SFVVSHLKNL QASTDPSKAE AKEKLGQLKP 

       610        620        630        640        650        660 
KKIFSSDIRK YSQNYELSYA IDAINAGASV ESNVIFSQSS YLPRSVSLNL TADVFGHSYN 

       670        680        690        700        710        720 
VFEIAARTEN LDHIIESFLG PKGYIETEDD DKFVDEVEEK TKSLYNRITE RFEKTFRQKR 

       730        740        750        760        770        780 
SVSKDAVDNI RQQAYKSLLP SQRDRSLDVD LSLKTFGSEL AWFNYDGKHE QKSSERVVDE 

       790        800        810        820        830        840 
IFDAIDEGLK KSKKFNYDFE PHFTFLDSEL SYPTNLGFPL KLAIDGSIAA RLKLNGEVDV 

       850        860        870        880        890        900 
RSILRQPENA AFRLEFVPSA AVELTGKLLV DAYVVEGGLK LDYNVHSSTG INVAVHNLND 

       910        920        930        940        950        960 
LGIDIKVGLP VKKQDIIDVK TDVLTTVKER GHPETSTPLH FNLKGNDYKQ YRGCFDQLSP 

       970        980        990       1000       1010       1020 
VSGLTFCGNV SVPWVSPTQA AAFYPLNGPS HLSVSIEADD VSEYHFRAEI KKDESAFKSA 

      1030       1040       1050       1060       1070       1080 
AVLFDTPGSS ADRKVLLLVE KKEKPHQGIT AHLKSGWKEI VAEGLLIDDN NEKSVSAKLV 

      1090       1100       1110       1120       1130       1140 
IESDEYSIKG GVKISGNPSR QVYKPILEYK APAKDSGAKV KKSHKTSEGI TVDGAVVVER 

      1150       1160       1170       1180       1190       1200 
TSDKGKYTFQ DLSLKTPKGT FVINGQLDIV PRNYAFDLKL SVDKNELLLN GHLNYAEPKS 

      1210       1220       1230       1240       1250       1260 
IDVALEVTSP QFPDYGSGFQ LINKRGDDYS DTKIILACGR DLKSDGSRLI LEHFIKGKYE 

      1270       1280       1290       1300       1310       1320 
TPDTFNLETK GEVLGTGHKI FGKFDIDSKP KHLEYDLKLG FDENEVTSDL VAKRDIKSPD 

      1330       1340       1350       1360       1370       1380 
DYELKFSAKI LDNSIRIESS REVKPKDDSA FLNTLVVLSG KKYEFQVDVK LAAEDEYHTS 

      1390       1400       1410       1420       1430       1440 
LKAESNLKIE GKTSVRLITD FTTDAQTVNG HVKVSNEGED FFELIYKLNR GSGNPSGNAK 

      1450       1460       1470       1480       1490       1500 
LFVKNYLDGA ATFKYNNGVG SGTLQIDVLK LHRKIKATGD LTLSGSQRSA AIDLYWDADR 

      1510       1520       1530       1540       1550       1560 
DQSKQLLFKT ENDVKEKSID SKNTLKILDK LTTLNFKGSL SGAIDDGEVE GQGELILPVG 

      1570       1580       1590       1600       1610       1620 
TYLGVKFGRA LHLTQADTKV GLHLQAEGRE SASSTQPVWK SDFLLESALT RDSFVGEAKL 

      1630       1640       1650       1660       1670       1680 
LFETKGKDDL KLFLSGKSLP QGEKKLISGQ FSGQGSLIGG RTSVIKLNSE IDETFIAYNL 

      1690       1700       1710       1720       1730       1740 
NSECNQGYRA NIVGKINRGY SPVAVKQIEN TLELLLPFDK LKQLKHTIIG TFSSQPESTP 

      1750       1760       1770       1780       1790       1800 
EFTVSNVIIW NNENTLKLTG EAAGDEKEGR TKWDLILPKE EPRTLETTWS NAGDNKKAGS 

      1810       1820       1830       1840       1850       1860 
LSFKWGGNKE AKVSTDIEFT SDNQPQILHL KATSPTEKFG IFDLALSLKK NADPADKIDF 

      1870       1880       1890       1900       1910       1920 
ELTVTADQKK TDVKGSLGLA PGVPIIDVVA VQPSGTSKVF VDFLRKSDSE LHGAIELQWV 

      1930       1940       1950       1960       1970       1980 
AFGGGHLTAN GDIKLDIDDF YLKLDVDSPK FNFNKWHLEA GQRAAKGSKR IVFTAKSAEK 

      1990       2000       2010       2020       2030       2040 
VLFSGSTNFH SKAENNKISY SGNGQVRIGD KAHAFNFRSS RQNLIQDANK EIGVEYNLDF 

      2050       2060       2070       2080       2090       2100 
KIAGHGSLHN ILKVTNKELH ALGKQCSEGK PNCAVVEIKS KVSAADAKET THDLVFLVDL 

      2110       2120       2130       2140       2150       2160 
KSVGVDTGVA FTAETVRRGF WLIDEQASLT LSHNGETTYK YKGYLKESGS GFTLTLPSRV 

      2170       2180       2190       2200       2210       2220 
IAAEVKLSSD VKPNHSKQQI SASVWLDKTR LPNSFSSVSI LLEEIEDKNT DKYVSQLRFT 

      2230       2240       2250       2260       2270       2280 
HPNLEKDLTV KGYVQIGLEN KLFDSNLEID IFKQKNQKIS ISSTVVEQKQ NDVVKYLSTL 

      2290       2300       2310       2320       2330       2340 
DVKSKGHELD VTGRGEATVK PSLIALQSVL KYKKDKRIKE FKNFQFEVST EKLLVHVKVP 

      2350       2360       2370       2380       2390       2400 
NHHLLHIDAN TKINDKHASG DASVHIIGLP TSVIHIEGEN KGFPVVKGTI SSEGTPNKLE 

      2410       2420       2430       2440       2450       2460 
LIADLSDGLL VEADFISESG KKELFYTFLS GKKDSRKPEF RWSVENIQSA LEPHKNDIQE 

      2470       2480       2490       2500       2510       2520 
VLNKLKEISD EAGNEITKES SRLADSLKAG LPNFRRFVNT YETQLKALKE EIANDKVLKE 

      2530       2540       2550       2560       2570       2580 
ISENWKEVIG DAAEVVSTLV NGILVTIDAL LKTLNELAES VLDALKKSLP ALKDSYKQAV 

      2590       2600       2610       2620       2630       2640 
DAIVGIAKSL TQSLVNILSS AAEILKKHEA DIKEYLSVLA DLANDVGKFV TKITGVIYEG 

      2650       2660       2670       2680       2690       2700 
VVEFSKPIKE KLDGLKFGVA IEFGKVVEQL QNLIVPQELL AFAQEIVSEL KETTLTPEIQ 

      2710       2720       2730       2740       2750       2760 
DLLQAIEKYL EKVSKKKDAD VEKELKLIFE KAIDAVESVI NFVVSEITGG DHTKDLYDIN 

      2770       2780       2790       2800       2810       2820 
IPTVLPSFIQ LPRVFSVRFS PLIYLVSNGV PCLSDLLASY RPSLRFDNII PPYDATAILL 

      2830       2840       2850       2860       2870       2880 
NSHHFFTFDR RHLTFKGICS YILAQDVQDG NFTIIANIEG GSLKSIIVSD QATTFELASD 

      2890       2900       2910       2920       2930       2940 
KSLLVNGRPT EYPADEGEFH AWREYNRVGI QTKAGVKVTC ETSIELCTFE INGFYFGKTR 

      2950       2960       2970       2980       2990       3000 
GLLGTINNEP WDDFTKPDGQ VASKANEFGN AWKVDAQCAN VDGVDHHEHS IKVEECEEVF 

      3010       3020       3030       3040       3050       3060 
SKASLLSPCS LFLDPAPYLE ACSHIAHEAT TKEEKQLAAC RTAAAYVQAC SVENVFVSVP 

      3070       3080       3090       3100       3110       3120 
PHCVHCSVNG DAAIDIGQSF SVKVPQKSAD ILIVLEQVTG NAETVKDFVS PIVSQLTQEL 

      3130       3140       3150       3160       3170       3180 
SSRGISDVWI SLLGYGAPGQ EYPHLYTSSG GKLSYDGKQK NIQFGERKVL GPFPFDNFTE 

      3190       3200       3210       3220       3230       3240 
SIDWLDEFTD QAFHLITTAD TILDYPFRPG AAKSIIYVLD TSCETTLFLK HLPVKALKLK 

      3250       3260       3270       3280       3290       3300 
DAIGSPGIVL HLVTNVDSVQ SKNIVGFDTN HAYYNQEGKK RVVSEVTGNE KAALKISETA 

      3310       3320       3330       3340       3350       3360 
CGQIALATSG TVFNKNNLKQ TKKFVAQHIA DSLTNVELTQ DCKCLPVEGI HTRAVCAVTG 

      3370       3380 
AREKEHLSVK GVKGTKGVKG

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References

[1]"Molecular characterization and gene expression in the eye of the apolipophorin II/I precursor from Locusta migratoria."
Bogerd J., Babin P.J., Kooiman F.P., Andre M., Ballagny C., van Marrewijk W.J., van der Horst D.J.
J. Comp. Neurol. 427:546-558(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-33; 100-117; 204-228; 637-645; 668-682; 721-737; 1299-1308; 1489-1498 AND 2232-2242, TISSUE SPECIFICITY.
Tissue: Fat body.
[2]Bogerd J.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 131; 140; 156; 189; 412-413; 494; 1087; 1103; 1559; 1646-1650; 2614; 2736; 2764; 2888; 3263 AND 3302.
[3]"Biosynthesis and secretion of insect lipoprotein: involvement of furin in cleavage of the apoB homolog, apolipophorin-II/I."
Smolenaars M.M.W., Kasperaitis M.A.M., Richardson P.E., Rodenburg K.W., Van der Horst D.J.
J. Lipid Res. 46:412-421(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY FURIN, MUTAGENESIS OF ARG-717; LYS-719 AND ARG-720.

Web resources

Protein Spotlight

Lipid freight - Issue 59 of June 2005

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ130944 mRNA. Translation: CAB51918.2.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.25.10.20. 1 hit.
2.20.50.20. 2 hits.
2.20.80.10. 1 hit.
2.30.230.10. 1 hit.
InterProIPR015819. Lipid_transp_b-sht_shell.
IPR001747. Lipid_transpt_N.
IPR009454. Lipid_transpt_open_b-sht.
IPR015816. Vitellinogen_b-sht_N.
IPR015255. Vitellinogen_open_b-sht.
IPR015817. Vitellinogen_open_b-sht_sub1.
IPR015818. Vitellinogen_open_b-sht_sub2.
IPR011030. Vitellinogen_superhlx.
IPR001846. VWF_type-D.
[Graphical view]
PfamPF06448. DUF1081. 1 hit.
PF09172. DUF1943. 1 hit.
PF01347. Vitellogenin_N. 1 hit.
PF00094. VWD. 1 hit.
[Graphical view]
SMARTSM00638. LPD_N. 1 hit.
SM00216. VWD. 1 hit.
[Graphical view]
SUPFAMSSF56968. Lipid_transp_b-sht_shell. 2 hits.
SSF48431. LV_superhelical. 1 hit.
PROSITEPS51211. VITELLOGENIN. 1 hit.
PS51233. VWFD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAPLP_LOCMI
AccessionPrimary (citable) accession number: Q9U943
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 10, 2007
Last modified: March 6, 2013
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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