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Protein

Apolipophorins

Gene

apolpp

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. Also involved in the transport of hydrophobic ligands like juvenile hormones, pheromone hydrocarbons and carotenoids. Required for morphogens wingless (wg) and hedgehog (hh) function, probably by acting as vehicles for the movement of wg and hh, explaining how covalently lipidated wg and hh can spread over long distances. May also be involved in transport and/or metabolism of heme.2 Publications

GO - Molecular functioni

  • fatty acid binding Source: UniProtKB
  • heme binding Source: FlyBase
  • lipid transporter activity Source: FlyBase
  • metal ion binding Source: UniProtKB-KW
  • microtubule binding Source: FlyBase
  • retinol binding Source: UniProtKB
  • signaling receptor binding Source: FlyBase

GO - Biological processi

  • lipid transport Source: FlyBase
  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of smoothened signaling pathway Source: UniProtKB
  • Wnt signaling pathway Source: UniProtKB-KW

Keywordsi

Biological processLipid transport, Transport, Wnt signaling pathway
LigandHeme, Iron, Lipid-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipophorins1 Publication
Alternative name(s):
Retinoid- and fatty acid-binding glycoprotein1 Publication
Cleaved into the following 2 chains:
Alternative name(s):
ApoL2
Apolipophorin II1 Publication
Short name:
ApoLII1 Publication
Alternative name(s):
ApoL1
Apolipophorin I1 Publication
Short name:
ApoLI1 Publication
Gene namesi
Name:apolppImported
Synonyms:Rfabg1 Publication, RfaBpImported
ORF Names:CG11064Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 4

Organism-specific databases

FlyBaseiFBgn0087002 apolpp

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 251 PublicationAdd BLAST25
ChainiPRO_000004152626 – 706Apolipophorin-2Add BLAST681
ChainiPRO_0000041527707 – 3351Apolipophorin-1Add BLAST2645

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi67N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi644N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1514N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1744N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1932N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1979N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2822N-linked (GlcNAc...) asparagine1 Publication1

Post-translational modificationi

May be modified covalently by lipidation.1 Publication
Cleaved into 2 chains by furin protease. However, prevention of cleavage does not impair its function (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei706 – 707Cleavage; by furinBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein, Lipoprotein

Proteomic databases

PaxDbiQ9V496
PRIDEiQ9V496

PTM databases

iPTMnetiQ9V496

Expressioni

Tissue specificityi

During stage 12, it is highly present throughout the yolk sac. By late stage 14, it localizes in the lateral fat body cells. Starting at stage 14, it localizes to the apodemes. Component of hemolymph clots (at protein level). Expressed in the amniosera.1 Publication

Gene expression databases

BgeeiFBgn0087002
ExpressionAtlasiQ9V496 baseline and differential
GenevisibleiQ9V496 DM

Interactioni

GO - Molecular functioni

  • microtubule binding Source: FlyBase
  • signaling receptor binding Source: FlyBase

Protein-protein interaction databases

BioGridi68653, 55 interactors
DIPiDIP-19190N
IntActiQ9V496, 9 interactors
STRINGi7227.FBpp0088252

Structurei

3D structure databases

ProteinModelPortaliQ9V496
SMRiQ9V496
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 641VitellogeninPROSITE-ProRule annotationAdd BLAST599
Domaini2787 – 2988VWFDPROSITE-ProRule annotationAdd BLAST202

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4338 Eukaryota
ENOG410Z6MR LUCA
GeneTreeiENSGT00590000083139
InParanoidiQ9V496
OMAiGQVQYQG
OrthoDBiEOG091G006F
PhylomeDBiQ9V496

Family and domain databases

Gene3Di1.25.10.20, 1 hit
2.30.230.10, 1 hit
InterProiView protein in InterPro
IPR015819 Lipid_transp_b-sht_shell
IPR001747 Lipid_transpt_N
IPR009454 Lipid_transpt_open_b-sht
IPR011030 Lipovitellin_superhlx_dom
IPR015816 Vitellinogen_b-sht_N
IPR015255 Vitellinogen_open_b-sht
IPR001846 VWF_type-D
PfamiView protein in Pfam
PF06448 DUF1081, 1 hit
PF09172 DUF1943, 1 hit
PF01347 Vitellogenin_N, 1 hit
PF00094 VWD, 1 hit
SMARTiView protein in SMART
SM01169 DUF1943, 1 hit
SM00638 LPD_N, 1 hit
SM00216 VWD, 1 hit
SUPFAMiSSF48431 SSF48431, 1 hit
SSF56968 SSF56968, 2 hits
PROSITEiView protein in PROSITE
PS51211 VITELLOGENIN, 1 hit
PS51233 VWFD, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9V496-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARMKYNIAL IGILASVLLT IAVNAENACN LGCPKSDNGL LKYIPGNYYD
60 70 80 90 100
YSFDSILTIG ASSDVPNDSD DTSLKVSGSA KIFAKGNCGY TLQLSSVKVT
110 120 130 140 150
NTKESVEKKI LNSIQKPVQF TLVSGILEPQ ICSDSSDLDY SLNIKRAVVS
160 170 180 190 200
LLQSGIEAEH EVDVFGMCPT HTSTSKVGNA NIITKARNLN SCSHREQINS
210 220 230 240 250
GLVSGKVNEK AGITSSLLLQ ANYIKESRIV NHLIENVQLT ETYKFIGNTK
260 270 280 290 300
RNSDISAKVV TILKLKNPSG TKANSPGTGS TVRSLIFQRP ETYTSKNINA
310 320 330 340 350
LKTILSDLVD STGDYVKKET AKKFVEFIRL LRQSDSETLL ELAAFPHPNK
360 370 380 390 400
VLARKVYLDG LFRTSTAESA RVILKQLSKF DEKEKLLAIL SLNIVKSVDK
410 420 430 440 450
ETLNQAASQL LPNAPKELYI AVGNLVAKYC LKNYCQGPEI DAISKKFSDG
460 470 480 490 500
LKHCKPNTKR EEERIVYILK GLGNAKSLSG NTVAALSECA STGRSNRIRV
510 520 530 540 550
AALHAFSKVK CEETLQSKSL ELLKNRNEDS ELRIEAYLSA ISCPNAEVAN
560 570 580 590 600
QISEIVNSET VNQVGGFISS NLKAIRDSTD VSRDQQKYHL ANIRVTKTFP
610 620 630 640 650
VDYRRYSFNN EVSYKLESLG VGASTDYQII YSQHGFLPRS SRINVTTEFF
660 670 680 690 700
GTNYNVFEAS VRQENVEDVL EYYLGPKGLV NKDFDEIVKL IEVGNNGVAA
710 720 730 740 750
GGRARRSIVD DVSKISKKYK MYGVKNVQDL NLDVSLKLFG SELAFLSLGD
760 770 780 790 800
NIPSSLDDII NYFSTSFEKA KQELSSFEKQ FSSHHLFLDT DLAYPTSIGV
810 820 830 840 850
PLELVAQGFA ATKVDLAVSL DINAILEQNW QKAKYRLKFV PSVDINANVQ
860 870 880 890 900
IGFNAQVLST GLRVVSSAHS ATGSDITVAV ISDGEGFNVD LELPREKLEL
910 920 930 940 950
INFNVDTELY VAEQDKQKAI ALKGNKKNKN SQPSEICFNQ LELVGLNICI
960 970 980 990 1000
KSSTSLSEVQ AGNGNVAERG LSVSEKFHLS RPFNFAVYLT TERKFTFKGI
1010 1020 1030 1040 1050
HTQEAFSQKW KLDYSTPGSK VSHDTTVVYE LGNKPKTFSR LSFDNSQCHF
1060 1070 1080 1090 1100
AVEGGINNDK NELVVYGQYE QDKEIKKSKI GFSKNGNEYK PLIEIQDNNG
1110 1120 1130 1140 1150
ISNSINGYHA DGKIVVKKNS NNIERYNFEN FQVSNSNNAH VAVNGWSDVG
1160 1170 1180 1190 1200
TNSLTSELRI SLDHQTFLIK ENLKLENGLY EAGFFINDEH SPENIYGSSI
1210 1220 1230 1240 1250
HLTIADQSYA LKTNGKAAAW SIGSDGSFNF QKLADSNSAR AGSLVENVEI
1260 1270 1280 1290 1300
QYKNKQVGGI KIMSNFDVNK MDVDVEISRE QKIGSIIVKY ESNQRHAQDY
1310 1320 1330 1340 1350
SLEASAKINK HSIDVISKCD FNGNVYVVDN SLVTSWGTLL SAKGEIGQRY
1360 1370 1380 1390 1400
SAQDININIQ GNVQISGKDK VTQWILKVIG TPDKTNSDFR ISRDTSELIK
1410 1420 1430 1440 1450
LTSESQHPQD KISFAKLNLI VKNQLTAKGE FRVAKNGKGD FTASIDTLKT
1460 1470 1480 1490 1500
EPKHKLEIES KFHIQSPKYD IDASLTLDGK RKVHLKSENT IEKLKFSTKN
1510 1520 1530 1540 1550
IGEANDKIIA FEANGSLKGE LRGNGEIQGT FIFNAPDGRV IDGSINRKIS
1560 1570 1580 1590 1600
TNAKSGLSQG NIDAQLSDTP FGSNKKRSIS LIGKLDRLNT KTKEFSANSN
1610 1620 1630 1640 1650
LVYTAFNGEK SEISYQIKQQ PNGDAKNIDF SLKAYGNPLP QPFEIAFALG
1660 1670 1680 1690 1700
DYSAQHAVVS ITSKYGEIFS VSANGNYNNN QALEYGLQAN IEIPKSTLKS
1710 1720 1730 1740 1750
LEINSHGKVL KSLIGNENAA YNVEFFLDSK TSLGQYARVN TVWNGTANDG
1760 1770 1780 1790 1800
SYDFEAQTNN MESPLKFNGK YHRKQTGNIK DGDLTGKQTY VLNAQYGAQY
1810 1820 1830 1840 1850
VKMDASLGYG AEKVDIAYVI DSSFDSVKDI KVNIRTFKPL DDSTYVVTAL
1860 1870 1880 1890 1900
FKQTDKSYGL DTTFYHSAHK KGVDIRLDLL KEKPIIISSI AELLGDRKGK
1910 1920 1930 1940 1950
VLFEILNLAD LDIKINSEAS YVSIDEFYII VNWSSKKLKL DGYELEARAQ
1960 1970 1980 1990 2000
SKNIKIQLKN ENGIIFSGTA TYALKKELNK TIIDGQGKVQ YQGKALSGNF
2010 2020 2030 2040 2050
KLTRQHFDFG TDREVGFSYT FMGNLGSKNG LGTLKITNKE FNTKFSVCEE
2060 2070 2080 2090 2100
KRQCTNLIVQ SIVSIDEQKL DAVEHTTLII VDLRDFGYPY EFELKSQNTR
2110 2120 2130 2140 2150
QGLKYQYHLD SFIITGNNFK YQFTANVQPT SSTIKLALPK RQILFETTQK
2160 2170 2180 2190 2200
IPADGSLFGR YEQTASFFID KLQKPDDVAR FSAIVDVTGT ERVAFNANGK
2210 2220 2230 2240 2250
LKFEHPTIRP LSISGQLNGD VNQQIASAEV IFDIFRLPEQ KVVGNSELRN
2260 2270 2280 2290 2300
SRSQNGFNIA YITTVKSAGL QFQYQINSNA AVDIEAHEYN IGLELNNGEI
2310 2320 2330 2340 2350
DVKAISFLNK EKFEISLSES NKHIIYIVGD FSKQNHYAKL NTKVQILDKN
2360 2370 2380 2390 2400
PIEITSEVQP NSAKIILKRQ DFIDGTAEVK LGKEFKVDVI GSGKQLFNGR
2410 2420 2430 2440 2450
VALDATNFLQ TNYFINEDHL NGFWHIVESE INKDSEYISE NIKERLKKSR
2460 2470 2480 2490 2500
QVTDKIVKLA KEAGPDFSKL QGKLLDYKND IVQELEADQS IAPIIDGIRT
2510 2520 2530 2540 2550
LFKKIAGIVD DINKAISEIL EKAQKSIVDI YDKLQALWKD SLLKAWEDFI
2560 2570 2580 2590 2600
ITVQKLISTL KTEFIKICTQ SFKDLLSALE KYGPALKNYG KAIGEIVKPI
2610 2620 2630 2640 2650
NDAAQEVIKI VVNAAEGVTH EFKQYVASLP SFESIRNEFN DKVKVLKLFE
2660 2670 2680 2690 2700
KATELTNSLF DQINILPQTP ETSEFLQKLH DYLIAKLKQE HIDNEKYIEE
2710 2720 2730 2740 2750
LGQLLIKAVR SIWVSIRSTY PGSSDHVIDF QSWIGSLTHS FDSLAVLPSI
2760 2770 2780 2790 2800
LSFRSSILNC LLNENWDVVF NKKLLYSWIF FNDFELRGHV VDGKHIFTFD
2810 2820 2830 2840 2850
GLNFAYPGNC KYILAQDSVD NNFTIIGQLT NGKLKSITLI DREGSYFEVA
2860 2870 2880 2890 2900
DNLALKLNGN LVEYPQHLSG LHAWRRFYTI HLYSEYGVGI VCTSDLKVCH
2910 2920 2930 2940 2950
ININGFYTSK TRGLLGNGNA EPYDDFLLID GTLAENSAAL GNDYGVGKCT
2960 2970 2980 2990 3000
AIEFDNNQFK SSKRQEMCSE LFGIESTLAF NFITLDSRPY RKACDIALAK
3010 3020 3030 3040 3050
VAEKEKEATA CTFALAYGSA VKQINKWVLL PPRCIKCAGP AGQHDFGDEF
3060 3070 3080 3090 3100
TVKLPNNKVD VVFVVDINVT PGVLSNLIAP AINDIRESLR SRGFSDVQVG
3110 3120 3130 3140 3150
VIVFEETKRY PALLTSDGGK INYKGNVADV KLAGIKSFCD NCVEQIITEK
3160 3170 3180 3190 3200
RILDIYNSLK EIVKGIAPQA DEKAFQLALD YPFRAGAAKS IIGVRSDSLE
3210 3220 3230 3240 3250
YKNWWKFVRA QLTGSITKFD GALIHLIAPV KGLSLEGVLS EKLIGFNSRL
3260 3270 3280 3290 3300
VATVDGKDSK KRTKLQFDND MGIDFVLNNG GWVFATQNFE KLKASDQKKM
3310 3320 3330 3340 3350
LNQITSSLAD TLFKTEIVSD CRCLPIHGLH GQHKCVIKSS TFVANKKAKS

A
Length:3,351
Mass (Da):372,677
Last modified:October 1, 2002 - v2
Checksum:i3B193D725D011B9E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2649F → I in AAC47284 (PubMed:8702812).Curated1
Sequence conflicti2965Q → E in AAC47284 (PubMed:8702812).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti1696S → Y in strain: 253.30. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62892 mRNA Translation: AAC47284.1
AE014135 Genomic DNA Translation: AAF59387.2
AF433843 Genomic DNA Translation: AAM17994.1
AF433844 Genomic DNA Translation: AAM17995.1
AF433845 Genomic DNA Translation: AAM17996.1
AF433846 Genomic DNA Translation: AAM17997.1
AF433847 Genomic DNA Translation: AAM17998.1
AF433848 Genomic DNA Translation: AAM17999.1
AF433849 Genomic DNA Translation: AAM18000.1
AF433850 Genomic DNA Translation: AAM18001.1
AF433851 Genomic DNA Translation: AAM18002.1
AF433852 Genomic DNA Translation: AAM18003.1
PIRiT13812
RefSeqiNP_001259085.1, NM_001272156.1
NP_001284720.1, NM_001297791.1
NP_001284721.1, NM_001297792.1
NP_524634.2, NM_079895.3
UniGeneiDm.1647

Genome annotation databases

EnsemblMetazoaiFBtr0089188; FBpp0088252; FBgn0087002
FBtr0334627; FBpp0306689; FBgn0087002
FBtr0345296; FBpp0311463; FBgn0087002
FBtr0345297; FBpp0311464; FBgn0087002
GeneIDi43827
KEGGidme:Dmel_CG11064

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiAPLP_DROME
AccessioniPrimary (citable) accession number: Q9V496
Secondary accession number(s): Q8ST55, Q8T6S6, Q94907
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: October 1, 2002
Last modified: June 20, 2018
This is version 145 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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