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Protein

Vitellogenin-3

Gene

Yp3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Vitellogenin is the major yolk protein of eggs where it is used as a food source during embryogenesis.

GO - Molecular functioni

GO - Biological processi

  • embryo development Source: UniProtKB
  • neurogenesis Source: FlyBase
  • regulation of embryonic development Source: FlyBase
  • response to bacterium Source: FlyBase
  • sex differentiation Source: FlyBase
  • vitellogenesis Source: FlyBase
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-DME-192456. Digestion of dietary lipid.

Protein family/group databases

ESTHERidrome-3vite. Yolk-Protein_dipter.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitellogenin-3
Alternative name(s):
Vitellogenin III
Yolk protein 3
Gene namesi
Name:Yp3
ORF Names:CG11129
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0004047. Yp3.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • P granule Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi10 – 101A → D in YP3s1; synthesized in the fat body, but not secreted, probably due to the amino acid mutation in the signal peptide. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 420401Vitellogenin-3PRO_0000017816Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371Phosphothreonine1 Publication
Modified residuei177 – 1771Phosphoserine1 Publication
Modified residuei178 – 1781Phosphoserine1 Publication
Modified residuei384 – 3841SulfotyrosineSequence analysis
Modified residuei390 – 3901SulfotyrosineSequence analysis

Post-translational modificationi

Tyrosine sulfation occurs in the female only and plays an essential functional role.1 Publication

Keywords - PTMi

Phosphoprotein, Sulfation

Proteomic databases

PaxDbiP06607.
PRIDEiP06607.

PTM databases

iPTMnetiP06607.

Expressioni

Tissue specificityi

Synthesized in the fat body and ovarian follicle cells and accumulate in the oocyte.1 Publication

Developmental stagei

Expressed in females only.1 Publication

Inductioni

By beta-ecdysone; in males.1 Publication

Gene expression databases

BgeeiP06607.
ExpressionAtlasiP06607. differential.
GenevisibleiP06607. DM.

Interactioni

Protein-protein interaction databases

BioGridi58712. 29 interactions.
DIPiDIP-19265N.
IntActiP06607. 2 interactions.
MINTiMINT-753134.
STRINGi7227.FBpp0073652.

Structurei

3D structure databases

ProteinModelPortaliP06607.
SMRiP06607. Positions 152-400.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. Lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410KB3P. Eukaryota.
ENOG4110NPC. LUCA.
InParanoidiP06607.
OMAiLRGDYIL.
OrthoDBiEOG70ZZNJ.
PhylomeDBiP06607.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013818. Lipase_N.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.

Sequencei

Sequence statusi: Complete.

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

P06607-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMSLRICLLA TCLLVAAHAS KDASNDRLKP TKWLTATELE NVPSLNDITW
60 70 80 90 100
ERLENQPLEQ GAKVIEKIYH VGQIKHDLTP SFVPSPSNVP VWIIKSNGQK
110 120 130 140 150
VECKLNNYVE TAKAQPGFGE DEVTIVLTGL PKTSPAQQKA MRRLIQAYVQ
160 170 180 190 200
KYNLQQLQKN AQEQQQQLKS SDYDYTSSEE AADQWKSAKA ASGDLIIIDL
210 220 230 240 250
GSTLTNFKRY AMLDVLNTGA MIGQTLIDLT NKGVPQEIIH LIGQGISAHV
260 270 280 290 300
AGAAGNKYTA QTGHKLRRIT GLDPAKVLSK RPQILGGLSR GDADFVDAIH
310 320 330 340 350
TSTFAMGTPI RCGDVDFYPN GPSTGVPGSE NVIEAVARAT RYFAESVRPG
360 370 380 390 400
SERNFPAVPA NSLKQYKEQD GFGKRAYMGL QIDYDLRGDY ILEVNAKSPF
410 420
GQRSPAHKQA AYHGMHHAQN
Length:420
Mass (Da):46,101
Last modified:January 1, 1988 - v1
Checksum:i5457C49CAC933B26
GO

Sequence cautioni

The sequence AAM29566.1 differs from that shown. Reason: Frameshift at position 208. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15898 Genomic DNA. Translation: AAA29024.1.
X04754 Genomic DNA. Translation: CAA28451.1.
AE014298 Genomic DNA. Translation: AAF48314.2.
AY113561 mRNA. Translation: AAM29566.1. Frameshift.
PIRiA25876.
RefSeqiNP_001285228.1. NM_001298299.1.
NP_511148.2. NM_078593.4.

Genome annotation databases

EnsemblMetazoaiFBtr0073821; FBpp0073652; FBgn0004047.
FBtr0346090; FBpp0311924; FBgn0004047.
GeneIDi32339.
KEGGidme:Dmel_CG11129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15898 Genomic DNA. Translation: AAA29024.1.
X04754 Genomic DNA. Translation: CAA28451.1.
AE014298 Genomic DNA. Translation: AAF48314.2.
AY113561 mRNA. Translation: AAM29566.1. Frameshift.
PIRiA25876.
RefSeqiNP_001285228.1. NM_001298299.1.
NP_511148.2. NM_078593.4.

3D structure databases

ProteinModelPortaliP06607.
SMRiP06607. Positions 152-400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58712. 29 interactions.
DIPiDIP-19265N.
IntActiP06607. 2 interactions.
MINTiMINT-753134.
STRINGi7227.FBpp0073652.

Protein family/group databases

ESTHERidrome-3vite. Yolk-Protein_dipter.

PTM databases

iPTMnetiP06607.

Proteomic databases

PaxDbiP06607.
PRIDEiP06607.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0073821; FBpp0073652; FBgn0004047.
FBtr0346090; FBpp0311924; FBgn0004047.
GeneIDi32339.
KEGGidme:Dmel_CG11129.

Organism-specific databases

CTDi32339.
FlyBaseiFBgn0004047. Yp3.

Phylogenomic databases

eggNOGiENOG410KB3P. Eukaryota.
ENOG4110NPC. LUCA.
InParanoidiP06607.
OMAiLRGDYIL.
OrthoDBiEOG70ZZNJ.
PhylomeDBiP06607.

Enzyme and pathway databases

ReactomeiR-DME-192456. Digestion of dietary lipid.

Miscellaneous databases

ChiTaRSiYp3. fly.
GenomeRNAii32339.
NextBioi778004.
PROiP06607.

Gene expression databases

BgeeiP06607.
ExpressionAtlasiP06607. differential.
GenevisibleiP06607. DM.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013818. Lipase_N.
IPR000734. TAG_lipase.
[Graphical view]
PANTHERiPTHR11610. PTHR11610. 1 hit.
PfamiPF00151. Lipase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of the gene coding for Drosophila melanogaster yolk protein 3."
    Garabedian M.J., Shirras A.D., Bownes M., Wensink P.C.
    Gene 55:1-8(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S.
  2. "Sequence homologies among the three yolk polypeptide (Yp) genes in Drosophila melanogaster."
    Yan Y.L., Kunert C.J., Postlethwait J.H.
    Nucleic Acids Res. 15:67-85(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Characterization, molecular cloning and sequencing of YP3s1, a fertile yolk protein 3 mutant in Drosophila."
    Liddell S., Bownes M.
    Mol. Gen. Genet. 228:81-88(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, MUTAGENESIS OF ALA-10.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  7. "Tyrosine sulfation of yolk proteins 1, 2, and 3 in Drosophila melanogaster."
    Baeuerle P.A., Huttner W.B.
    J. Biol. Chem. 260:6434-6439(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: SULFATION.
  8. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37; SER-177 AND SER-178, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiVIT3_DROME
AccessioniPrimary (citable) accession number: P06607
Secondary accession number(s): Q8MYV8, Q9VY89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 11, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.