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   16-JUN-2009, entry version 101.
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; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Canton-S;
RX   MEDLINE=83189120; 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
RT   genes.";
RL   J. Mol. Biol. 164:481-492(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RX   MEDLINE=22426069; PubMed=12537572;
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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   MEDLINE=22426066; PubMed=12537569;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., 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   MEDLINE=82221407; 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
RT   YPII genes and their transcription products.";
RL   Nucleic Acids Res. 10:2261-2274(1982).
RN   [6]
RP   PROTEIN SEQUENCE OF 168-176, AND SULFATION.
RX   MEDLINE=89008370; PubMed=3139663;
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   MEDLINE=85207638; PubMed=3922974;
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;
RP   THR-170; SER-173; SER-178; SER-181; SER-182 AND SER-183, AND 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
CC       is used as a food source during embryogenesis.
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-192398, EBI-192398;
CC       Q9V466:Nup107; NbExp=1; IntAct=EBI-192398, EBI-89961;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Synthesized in the fat body and ovarian
CC       follicle cells and accumulate in the oocyte.
CC   -!- DEVELOPMENTAL STAGE: Expressed during late pupal development and
CC       in 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.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
CC       family.
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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_511102.3; -.
DR   UniGene; Dm.6718; -.
DR   DIP; DIP:19994N; -.
DR   IntAct; P02844; 6.
DR   Ensembl; FBgn0005391; Drosophila melanogaster.
DR   GeneID; 31938; -.
DR   KEGG; dme:Dmel_CG2979; -.
DR   NMPDR; fig|7227.3.peg.17211; -.
DR   FlyBase; FBgn0005391; Yp2.
DR   HOGENOM; P02844; -.
DR   BioCyc; DMEL-XXX-02:DMEL-XXX-02-001287-MON; -.
DR   NextBio; 776039; -.
DR   ArrayExpress; P02844; -.
DR   GermOnline; CG2979; Drosophila melanogaster.
DR   GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR   GO; GO:0005811; C:lipid particle; IDA:FlyBase.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0048477; P:oogenesis; TAS:FlyBase.
DR   GO; GO:0007548; P:sex differentiation; TAS:FlyBase.
DR   InterPro; IPR000734; Lipase.
DR   InterPro; IPR013818; Lipase_N.
DR   PANTHER; PTHR11610; Lipase; 1.
DR   Pfam; PF00151; Lipase; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Phosphoprotein;
KW   Secreted; Signal; Sulfation.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    442       Vitellogenin-2.
FT                                /FTId=PRO_0000017815.
FT   MOD_RES      31     31       Phosphoserine.
FT   MOD_RES      33     33       Phosphoserine.
FT   MOD_RES      82     82       Phosphoserine.
FT   MOD_RES     170    170       Phosphothreonine.
FT   MOD_RES     172    172       Sulfotyrosine.
FT   MOD_RES     173    173       Phosphoserine.
FT   MOD_RES     178    178       Phosphoserine.
FT   MOD_RES     181    181       Phosphoserine.
FT   MOD_RES     182    182       Phosphoserine.
FT   MOD_RES     183    183       Phosphoserine.
FT   CONFLICT     68     68       L -> M (in Ref. 1).
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
//