VIT3_DROME
ID VIT3_DROME Reviewed; 420 AA.
AC P06607; Q8MYV8; Q9VY89;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Vitellogenin-3;
DE AltName: Full=Vitellogenin III;
DE AltName: Full=Yolk protein 3;
DE Flags: Precursor;
GN Name=Yp3; ORFNames=CG11129;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=3114046; DOI=10.1016/0378-1119(87)90242-3;
RA Garabedian M.J., Shirras A.D., Bownes M., Wensink P.C.;
RT "The nucleotide sequence of the gene coding for Drosophila melanogaster
RT yolk protein 3.";
RL Gene 55:1-8(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3029679; DOI=10.1093/nar/15.1.67;
RA Yan Y.L., Kunert C.J., Postlethwait J.H.;
RT "Sequence homologies among the three yolk polypeptide (Yp) genes in
RT Drosophila melanogaster.";
RL Nucleic Acids Res. 15:67-85(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION,
RP AND MUTAGENESIS OF ALA-10.
RX PubMed=1909425; DOI=10.1007/bf00282451;
RA Liddell S., Bownes M.;
RT "Characterization, molecular cloning and sequencing of YP3s1, a fertile
RT yolk protein 3 mutant in Drosophila.";
RL Mol. Gen. Genet. 228:81-88(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP SULFATION.
RX PubMed=3922974; DOI=10.1016/s0021-9258(18)88991-8;
RA Baeuerle P.A., Huttner W.B.;
RT "Tyrosine sulfation of yolk proteins 1, 2, and 3 in Drosophila
RT melanogaster.";
RL J. Biol. Chem. 260:6434-6439(1985).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37; SER-177 AND SER-178, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Vitellogenin is the major yolk protein of eggs where it is
CC used as a food source during embryogenesis.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Synthesized in the fat body and ovarian follicle
CC cells and accumulate in the oocyte. {ECO:0000269|PubMed:1909425}.
CC -!- DEVELOPMENTAL STAGE: Expressed in females only.
CC {ECO:0000269|PubMed:1909425}.
CC -!- INDUCTION: By beta-ecdysone; in males. {ECO:0000269|PubMed:1909425}.
CC -!- PTM: Tyrosine sulfation occurs in the female only and plays an
CC essential functional role. {ECO:0000269|PubMed:3922974}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM29566.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M15898; AAA29024.1; -; Genomic_DNA.
DR EMBL; X04754; CAA28451.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48314.2; -; Genomic_DNA.
DR EMBL; AY113561; AAM29566.1; ALT_FRAME; mRNA.
DR PIR; A25876; A25876.
DR RefSeq; NP_001285228.1; NM_001298299.1.
DR RefSeq; NP_511148.2; NM_078593.4.
DR AlphaFoldDB; P06607; -.
DR SMR; P06607; -.
DR BioGRID; 58712; 29.
DR DIP; DIP-19265N; -.
DR IntAct; P06607; 6.
DR MINT; P06607; -.
DR STRING; 7227.FBpp0073652; -.
DR ESTHER; drome-3vite; Yolk-Protein_dipter.
DR iPTMnet; P06607; -.
DR PaxDb; P06607; -.
DR DNASU; 32339; -.
DR EnsemblMetazoa; FBtr0073821; FBpp0073652; FBgn0004047.
DR EnsemblMetazoa; FBtr0346090; FBpp0311924; FBgn0004047.
DR GeneID; 32339; -.
DR KEGG; dme:Dmel_CG11129; -.
DR CTD; 32339; -.
DR FlyBase; FBgn0004047; Yp3.
DR VEuPathDB; VectorBase:FBgn0004047; -.
DR eggNOG; ENOG502SRF1; Eukaryota.
DR HOGENOM; CLU_027171_6_0_1; -.
DR InParanoid; P06607; -.
DR OMA; KAQPGFG; -.
DR OrthoDB; 755257at2759; -.
DR PhylomeDB; P06607; -.
DR Reactome; R-DME-1482801; Acyl chain remodelling of PS.
DR Reactome; R-DME-1483166; Synthesis of PA.
DR Reactome; R-DME-192456; Digestion of dietary lipid.
DR Reactome; R-DME-8963889; Assembly of active LPL and LIPC lipase complexes.
DR Reactome; R-DME-8964058; HDL remodeling.
DR BioGRID-ORCS; 32339; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Yp3; fly.
DR GenomeRNAi; 32339; -.
DR PRO; PR:P06607; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004047; Expressed in head capsule and 29 other tissues.
DR ExpressionAtlas; P06607; baseline and differential.
DR Genevisible; P06607; DM.
DR GO; GO:0005576; C:extracellular region; IMP:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IPI:FlyBase.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:FlyBase.
DR GO; GO:0009617; P:response to bacterium; HEP:FlyBase.
DR GO; GO:0007548; P:sex differentiation; NAS:FlyBase.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR Pfam; PF00151; Lipase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..19
FT CHAIN 20..420
FT /note="Vitellogenin-3"
FT /id="PRO_0000017816"
FT REGION 401..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 384
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 390
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MUTAGEN 10
FT /note="A->D: In YP3s1; synthesized in the fat body, but not
FT secreted, probably due to the amino acid mutation in the
FT signal peptide."
FT /evidence="ECO:0000269|PubMed:1909425"
SQ SEQUENCE 420 AA; 46101 MW; 5457C49CAC933B26 CRC64;
MMSLRICLLA TCLLVAAHAS KDASNDRLKP TKWLTATELE NVPSLNDITW ERLENQPLEQ
GAKVIEKIYH VGQIKHDLTP SFVPSPSNVP VWIIKSNGQK VECKLNNYVE TAKAQPGFGE
DEVTIVLTGL PKTSPAQQKA MRRLIQAYVQ KYNLQQLQKN AQEQQQQLKS SDYDYTSSEE
AADQWKSAKA ASGDLIIIDL GSTLTNFKRY AMLDVLNTGA MIGQTLIDLT NKGVPQEIIH
LIGQGISAHV AGAAGNKYTA QTGHKLRRIT GLDPAKVLSK RPQILGGLSR GDADFVDAIH
TSTFAMGTPI RCGDVDFYPN GPSTGVPGSE NVIEAVARAT RYFAESVRPG SERNFPAVPA
NSLKQYKEQD GFGKRAYMGL QIDYDLRGDY ILEVNAKSPF GQRSPAHKQA AYHGMHHAQN
