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UniProtKB/Swiss-Prot entry P02844


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name VIT2_DROME
Primary accession number P02844
Secondary accession number Q9W2Z0
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on June 20, 2001 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 97)
Name and origin of the protein
Protein name Vitellogenin-2 [Precursor]
Synonyms Vitellogenin II
Yolk protein 2
Gene name
Name: Yp2
ORFNames: CG2979
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Canton-S;
DOI=10.1016/0022-2836(83)90046-3; PubMed=6405043 [NCBI, ExPASy, EBI, Israel, Japan]
Hung M.-C., Wensink P.C.;
"Sequence and structure conservation in yolk proteins and their genes.";
J. Mol. Biol. 164:481-492(1983).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Head;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
DOI=10.1093/nar/10.7.2261; PubMed=6806773 [NCBI, ExPASy, EBI, Israel, Japan]
Hovemann B., Galler R.;
"Vitellogenin in Drosophila melanogaster: a comparison of the YPI and YPII genes and their transcription products.";
Nucleic Acids Res. 10:2261-2274(1982).
[6]
PROTEIN SEQUENCE OF 168-176, AND SULFATION.
PubMed=3139663 [NCBI, ExPASy, EBI, Israel, Japan]
Baeuerle P.A., Lottspeich F., Huttner W.B.;
"Purification of yolk protein 2 of Drosophila melanogaster and identification of its site of tyrosine sulfation.";
J. Biol. Chem. 263:14925-14929(1988).
[7]
SULFATION.
PubMed=3922974 [NCBI, ExPASy, EBI, Israel, Japan]
Baeuerle P.A., Huttner W.B.;
"Tyrosine sulfation of yolk proteins 1, 2, and 3 in Drosophila melanogaster.";
J. Biol. Chem. 260:6434-6439(1985).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-33; SER-82; THR-170; SER-173; SER-178; SER-181; SER-182 AND SER-183, AND MASS SPECTROMETRY.
TISSUE=Embryo;
DOI=10.1021/pr700696a; PubMed=18327897 [NCBI, ExPASy, EBI, Israel, Japan]
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE014298; AAF46547.3; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY061042; AAL28590.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X01524; CAA25710.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A03333; VJFF2.
RefSeq NP_511102.3; -.
UniGene Dm.6718
3D structure databases
ModBase P02844.
Protein-protein interaction databases
DIP DIP:19994N; -.
IntAct P02844; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-001287-MON; -.
Organism-specific databases
FlyBase FBgn0005391; Yp2.
Gene expression databases
ArrayExpress P02844; -.
GermOnline CG2979; Drosophila melanogaster.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (traceable author statement from UniProtKB).
GO:0005811; Cellular component: lipid particle (inferred from direct assay from FlyBase).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0048477; Biological process: oogenesis (traceable author statement from FlyBase).
GO:0007548; Biological process: sex differentiation (traceable author statement from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR000734; Lipase.
IPR013818; Lipase_N.
Graphical view of domain structure.
PANTHER PTHR11610; Lipase; 1.
Pfam PF00151; Lipase; 1.
Pfam graphical view of domain structure.
BLOCKS P02844.
ProtoNet P02844.
Genome annotation databases
Ensembl CG2979; Drosophila melanogaster. [Contig view]
GeneID 31938; -.
KEGG dme:Dmel_CG2979; -.
NMPDR fig|7227.3.peg.17211; -.
Phylogenomic databases
HOGENOM P02844; -.
Other
NextBio 776039; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; Phosphoprotein; Secreted; Signal; Sulfation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    19  19     Potential. 
CHAIN   20   442  423     Vitellogenin-2. PRO_0000017815
MOD_RES   31    31        Phosphoserine. 
MOD_RES   33    33        Phosphoserine. 
MOD_RES   82    82        Phosphoserine. 
MOD_RES   170   170        Phosphothreonine. 
MOD_RES   172   172        Sulfotyrosine. 
MOD_RES   173   173        Phosphoserine. 
MOD_RES   178   178        Phosphoserine. 
MOD_RES   181   181        Phosphoserine. 
MOD_RES   182   182        Phosphoserine. 
MOD_RES   183   183        Phosphoserine. 
CONFLICT   68    68        L -> M (in Ref. 1). 
Sequence information
Length: 442 AA [This is the length of the unprocessed precursor] Molecular weight: 49660 Da [This is the MW of the unprocessed precursor] CRC64: 7DBD384E37E84F14 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNPLRTLCVM ACLLAVAMGN PQSGNRSGRR SNSLDNVEQP SNWVNPREVE ELPNLKEVTL 

        70         80         90        100        110        120 
KKLQEMSLEE GATLLDKLYH LSQFNHVFKP DYTPEPSQIR GYIVGERGQK IEFNLNTLVE 

       130        140        150        160        170        180 
KVKRQQKFGD DEVTIFIQGL PETNTQVQKA TRKLVQAYQQ RYNLQPYETT DYSNEEQSQR 

       190        200        210        220        230        240 
SSSEEQQTQR RKQNGEQDDT KTGDLIVIQL GNAIEDFEQY ATLNIERLGE IIGNRLVELT 

       250        260        270        280        290        300 
NTVNVPQEII HLIGSGPAAH VAGVAGRQFT RQTGHKLRRI TALDPTKIYG KPEERLTGLA 

       310        320        330        340        350        360 
RGDADFVDAI HTSAYGMGTS QRLANVDFFP NGPSTGVPGA DNVVEATMRA TRYFAESVRP 

       370        380        390        400        410        420 
GNERNFPSVA ASSYQEYKQN KGYGKRGYMG IATDFDLQGD YILQVNSKSP FGRSTPAQKQ 

       430        440 
TGYHQVHQPW RQSSSNQGSR RQ 

P02844 in FASTA format

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