VIT1_DROME
ID VIT1_DROME Reviewed; 439 AA.
AC P02843; Q8SXV7; Q9W2Y9;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Vitellogenin-1;
DE AltName: Full=Vitellogenin I;
DE AltName: Full=Yolk protein 1;
DE Flags: Precursor;
GN Name=Yp1; ORFNames=CG2985;
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].
RX PubMed=6275360; DOI=10.1093/nar/9.23.6407;
RA Hung M.-C., Wensink P.C.;
RT "The sequence of the Drosophila melanogaster gene for yolk protein 1.";
RL Nucleic Acids Res. 9:6407-6419(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=6272212; DOI=10.1093/nar/9.18.4721;
RA Hovemann B., Galler R., Walldorf U., Kupper H., Bautz E.K.F.;
RT "Vitellogenin in Drosophila melanogaster: sequence of the yolk protein I
RT gene and its flanking regions.";
RL Nucleic Acids Res. 9:4721-4734(1981).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RX PubMed=6806773; DOI=10.1093/nar/10.7.2261;
RA Hovemann B., Galler R.;
RT "Vitellogenin in Drosophila melanogaster: a comparison of the YPI and YPII
RT genes and their transcription products.";
RL Nucleic Acids Res. 10:2261-2274(1982).
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 TYR-171; SER-175; SER-185;
RP SER-186; TYR-190; SER-191 AND SER-435, AND IDENTIFICATION BY MASS
RP 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:6272212}.
CC -!- DEVELOPMENTAL STAGE: Expressed in females only.
CC {ECO:0000269|PubMed:6272212}.
CC -!- INDUCTION: By beta-ecdysone; in males.
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}.
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DR EMBL; V00248; CAA23502.1; -; Genomic_DNA.
DR EMBL; X01524; CAA25709.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46548.1; -; Genomic_DNA.
DR EMBL; AY075560; AAL68367.1; -; mRNA.
DR PIR; A93744; VJFF1.
DR RefSeq; NP_001285071.1; NM_001298142.1.
DR RefSeq; NP_511103.1; NM_078548.3.
DR AlphaFoldDB; P02843; -.
DR SMR; P02843; -.
DR BioGRID; 58375; 39.
DR DIP; DIP-18442N; -.
DR IntAct; P02843; 1.
DR MINT; P02843; -.
DR STRING; 7227.FBpp0071354; -.
DR ESTHER; drome-1vite; Yolk-Protein_dipter.
DR iPTMnet; P02843; -.
DR PaxDb; P02843; -.
DR DNASU; 31939; -.
DR EnsemblMetazoa; FBtr0071419; FBpp0071354; FBgn0004045.
DR EnsemblMetazoa; FBtr0346261; FBpp0312020; FBgn0004045.
DR GeneID; 31939; -.
DR KEGG; dme:Dmel_CG2985; -.
DR CTD; 31939; -.
DR FlyBase; FBgn0004045; Yp1.
DR VEuPathDB; VectorBase:FBgn0004045; -.
DR eggNOG; ENOG502SRF1; Eukaryota.
DR HOGENOM; CLU_027171_6_0_1; -.
DR InParanoid; P02843; -.
DR OMA; SYHGVHQ; -.
DR OrthoDB; 755257at2759; -.
DR PhylomeDB; P02843; -.
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 SignaLink; P02843; -.
DR BioGRID-ORCS; 31939; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Yp1; fly.
DR GenomeRNAi; 31939; -.
DR PRO; PR:P02843; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004045; Expressed in adult abdomen and 27 other tissues.
DR ExpressionAtlas; P02843; baseline and differential.
DR Genevisible; P02843; DM.
DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0007548; P:sex differentiation; TAS: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..20
FT CHAIN 21..439
FT /note="Vitellogenin-1"
FT /id="PRO_0000017814"
FT REGION 158..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 190
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 41
FT /note="G -> R (in Ref. 5; AAL68367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 439 AA; 48712 MW; DF8A02080D69C522 CRC64;
MNPMRVLSLL ACLAVAALAK PNGRMDNSVN QALKPSQWLS GSQLEAIPAL DDFTIERLEN
MNLERGAELL QQVYHLSQIH HNVEPNYVPS GIQVYVPKPN GDKTVAPLNE MIQRLKQKQN
FGEDEVTIIV TGLPQTSETV KKATRKLVQA YMQRYNLQQQ RQHGKNGNQD YQDQSNEQRK
NQRTSSEEDY SEEVKNAKTQ SGDIIVIDLG SKLNTYERYA MLDIEKTGAK IGKWIVQMVN
ELDMPFDTIH LIGQNVGAHV AGAAAQEFTR LTGHKLRRVT GLDPSKIVAK SKNTLTGLAR
GDAEFVDAIH TSVYGMGTPI RSGDVDFYPN GPAAGVPGAS NVVEAAMRAT RYFAESVRPG
NERSFPAVPA NSLQQYKQND GFGKRAYMGI DTAHDLEGDY ILQVNPKSPF GRNAPAQKQS
SYHGVHQAWN TNQDSKDYQ
