VIT2_DROME
ID VIT2_DROME Reviewed; 442 AA.
AC P02844; Q9W2Z0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Vitellogenin-2;
DE AltName: Full=Vitellogenin II;
DE AltName: Full=Yolk protein 2;
DE Flags: Precursor;
GN Name=Yp2; ORFNames=CG2979;
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=6405043; DOI=10.1016/0022-2836(83)90046-3;
RA Hung M.-C., Wensink P.C.;
RT "Sequence and structure conservation in yolk proteins and their genes.";
RL J. Mol. Biol. 164:481-492(1983).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
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 [6]
RP PROTEIN SEQUENCE OF 168-176, AND SULFATION AT TYR-172.
RX PubMed=3139663; DOI=10.1016/s0021-9258(18)68127-x;
RA Baeuerle P.A., Lottspeich F., Huttner W.B.;
RT "Purification of yolk protein 2 of Drosophila melanogaster and
RT identification of its site of tyrosine sulfation.";
RL J. Biol. Chem. 263:14925-14929(1988).
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 SER-31; SER-33; SER-82; THR-170;
RP SER-173; SER-178; SER-181; SER-182 AND SER-183, 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.
CC -!- DEVELOPMENTAL STAGE: Expressed during late pupal development and in
CC adult females between days 1-3.
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:3139663,
CC ECO:0000269|PubMed:3922974}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; AE014298; AAF46547.3; -; Genomic_DNA.
DR EMBL; AY061042; AAL28590.1; -; mRNA.
DR EMBL; X01524; CAA25710.1; -; Genomic_DNA.
DR PIR; A03333; VJFF2.
DR RefSeq; NP_001285070.1; NM_001298141.1.
DR RefSeq; NP_511102.3; NM_078547.3.
DR AlphaFoldDB; P02844; -.
DR SMR; P02844; -.
DR BioGRID; 58374; 32.
DR DIP; DIP-19994N; -.
DR IntAct; P02844; 3.
DR MINT; P02844; -.
DR STRING; 7227.FBpp0071359; -.
DR ESTHER; drome-2vite; Yolk-Protein_dipter.
DR iPTMnet; P02844; -.
DR PaxDb; P02844; -.
DR DNASU; 31938; -.
DR EnsemblMetazoa; FBtr0071424; FBpp0071359; FBgn0005391.
DR EnsemblMetazoa; FBtr0339648; FBpp0308710; FBgn0005391.
DR GeneID; 31938; -.
DR KEGG; dme:Dmel_CG2979; -.
DR CTD; 31938; -.
DR FlyBase; FBgn0005391; Yp2.
DR VEuPathDB; VectorBase:FBgn0005391; -.
DR eggNOG; ENOG502SRF1; Eukaryota.
DR HOGENOM; CLU_027171_6_0_1; -.
DR InParanoid; P02844; -.
DR OMA; VHQPWRQ; -.
DR OrthoDB; 755257at2759; -.
DR PhylomeDB; P02844; -.
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; P02844; -.
DR BioGRID-ORCS; 31938; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Yp2; fly.
DR GenomeRNAi; 31938; -.
DR PRO; PR:P02844; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0005391; Expressed in head capsule and 23 other tissues.
DR ExpressionAtlas; P02844; baseline and differential.
DR Genevisible; P02844; 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 Direct protein sequencing; Phosphoprotein; Reference proteome; Secreted;
KW Signal; Sulfation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..442
FT /note="Vitellogenin-2"
FT /id="PRO_0000017815"
FT REGION 21..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 172
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:3139663"
FT MOD_RES 173
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 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 68
FT /note="L -> M (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 442 AA; 49660 MW; 7DBD384E37E84F14 CRC64;
MNPLRTLCVM ACLLAVAMGN PQSGNRSGRR SNSLDNVEQP SNWVNPREVE ELPNLKEVTL
KKLQEMSLEE GATLLDKLYH LSQFNHVFKP DYTPEPSQIR GYIVGERGQK IEFNLNTLVE
KVKRQQKFGD DEVTIFIQGL PETNTQVQKA TRKLVQAYQQ RYNLQPYETT DYSNEEQSQR
SSSEEQQTQR RKQNGEQDDT KTGDLIVIQL GNAIEDFEQY ATLNIERLGE IIGNRLVELT
NTVNVPQEII HLIGSGPAAH VAGVAGRQFT RQTGHKLRRI TALDPTKIYG KPEERLTGLA
RGDADFVDAI HTSAYGMGTS QRLANVDFFP NGPSTGVPGA DNVVEATMRA TRYFAESVRP
GNERNFPSVA ASSYQEYKQN KGYGKRGYMG IATDFDLQGD YILQVNSKSP FGRSTPAQKQ
TGYHQVHQPW RQSSSNQGSR RQ
