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Protein

Apolipophorins

Gene

Rfabg

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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
  • receptor binding Source: FlyBase
  • retinol binding Source: UniProtKB

GO - Biological processi

  • lipid transport Source: FlyBase
  • smoothened signaling pathway Source: UniProtKB
  • transport Source: FlyBase
  • Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport, Wnt signaling pathway

Keywords - Ligandi

Heme, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

ReactomeiR-DME-171052. LDL-mediated lipid transport.
R-DME-174800. Chylomicron-mediated lipid transport.
R-DME-3000471. Scavenging by Class B Receptors.
R-DME-3000497. Scavenging by Class H Receptors.
R-DME-432142. Platelet sensitization by LDL.
R-DME-5686938. Regulation of TLR by endogenous ligand.
R-DME-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-DME-8856828. Clathrin-mediated endocytosis.
R-DME-8866423. VLDL biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipophorins
Alternative name(s):
Retinoid- and fatty acid-binding glycoprotein
Cleaved into the following 2 chains:
Alternative name(s):
ApoL2
Apolipophorin II
Alternative name(s):
ApoL1
Apolipophorin I
Gene namesi
Name:Rfabg
Synonyms:RfaBp
ORF Names:CG11064
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 4

Organism-specific databases

FlyBaseiFBgn0087002. Rfabg.

Subcellular locationi

GO - Cellular componenti

  • basal part of cell Source: FlyBase
  • endocytic vesicle Source: FlyBase
  • extracellular region Source: UniProtKB
  • extracellular space Source: FlyBase
  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi67N-linked (GlcNAc...)Sequence analysis1
Glycosylationi644N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1514N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1744N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1932N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1979N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2822N-linked (GlcNAc...)1 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.

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.
GenevisibleiQ9V496. DM.

Interactioni

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi68653. 43 interactors.
DIPiDIP-29672N.
IntActiQ9V496. 8 interactors.
MINTiMINT-925481.
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

Sequence similaritiesi

Contains 1 vitellogenin domain.PROSITE-ProRule annotation
Contains 1 VWFD domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4338. Eukaryota.
ENOG410Z6MR. LUCA.
GeneTreeiENSGT00590000083139.
InParanoidiQ9V496.
OMAiGQVQYQG.
OrthoDBiEOG091G006F.
PhylomeDBiQ9V496.

Family and domain databases

Gene3Di1.25.10.20. 1 hit.
2.20.50.20. 2 hits.
2.20.80.10. 1 hit.
2.30.230.10. 1 hit.
InterProiIPR015819. Lipid_transp_b-sht_shell.
IPR001747. Lipid_transpt_N.
IPR009454. Lipid_transpt_open_b-sht.
IPR033340. RFABG.
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]
PANTHERiPTHR23361:SF12. PTHR23361:SF12. 3 hits.
PfamiPF06448. DUF1081. 1 hit.
PF09172. DUF1943. 1 hit.
PF01347. Vitellogenin_N. 1 hit.
PF00094. VWD. 1 hit.
[Graphical view]
SMARTiSM01169. DUF1943. 1 hit.
SM00638. LPD_N. 1 hit.
SM00216. VWD. 1 hit.
[Graphical view]
SUPFAMiSSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 2 hits.
PROSITEiPS51211. VITELLOGENIN. 1 hit.
PS51233. VWFD. 1 hit.
[Graphical view]

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

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ9V496.
SMRiQ9V496.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68653. 43 interactors.
DIPiDIP-29672N.
IntActiQ9V496. 8 interactors.
MINTiMINT-925481.
STRINGi7227.FBpp0088252.

Proteomic databases

PaxDbiQ9V496.
PRIDEiQ9V496.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi43827.
FlyBaseiFBgn0087002. Rfabg.

Phylogenomic databases

eggNOGiKOG4338. Eukaryota.
ENOG410Z6MR. LUCA.
GeneTreeiENSGT00590000083139.
InParanoidiQ9V496.
OMAiGQVQYQG.
OrthoDBiEOG091G006F.
PhylomeDBiQ9V496.

Enzyme and pathway databases

ReactomeiR-DME-171052. LDL-mediated lipid transport.
R-DME-174800. Chylomicron-mediated lipid transport.
R-DME-3000471. Scavenging by Class B Receptors.
R-DME-3000497. Scavenging by Class H Receptors.
R-DME-432142. Platelet sensitization by LDL.
R-DME-5686938. Regulation of TLR by endogenous ligand.
R-DME-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-DME-8856828. Clathrin-mediated endocytosis.
R-DME-8866423. VLDL biosynthesis.

Miscellaneous databases

ChiTaRSiRfabg. fly.
GenomeRNAii43827.
PROiQ9V496.

Gene expression databases

BgeeiFBgn0087002.
ExpressionAtlasiQ9V496. baseline.
GenevisibleiQ9V496. DM.

Family and domain databases

Gene3Di1.25.10.20. 1 hit.
2.20.50.20. 2 hits.
2.20.80.10. 1 hit.
2.30.230.10. 1 hit.
InterProiIPR015819. Lipid_transp_b-sht_shell.
IPR001747. Lipid_transpt_N.
IPR009454. Lipid_transpt_open_b-sht.
IPR033340. RFABG.
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]
PANTHERiPTHR23361:SF12. PTHR23361:SF12. 3 hits.
PfamiPF06448. DUF1081. 1 hit.
PF09172. DUF1943. 1 hit.
PF01347. Vitellogenin_N. 1 hit.
PF00094. VWD. 1 hit.
[Graphical view]
SMARTiSM01169. DUF1943. 1 hit.
SM00638. LPD_N. 1 hit.
SM00216. VWD. 1 hit.
[Graphical view]
SUPFAMiSSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 2 hits.
PROSITEiPS51211. VITELLOGENIN. 1 hit.
PS51233. VWFD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAPLP_DROME
AccessioniPrimary (citable) accession number: Q9V496
Secondary accession number(s): Q8ST55, Q8T6S6, Q94907
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: October 1, 2002
Last modified: November 30, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.