Reviewed, UniProtKB/Swiss-Prot P02844 (VIT2_DROME)

Names and origin

Protein names

Recommended name:
    Vitellogenin-2
Alternative name(s):
    Vitellogenin II
    Yolk protein 2

Gene names

Name:	Yp2
ORF Names:	CG2979

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	442 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Vitellogenin is the major yolk protein of eggs where it is used as a food source during embryogenesis.
Subcellular location	Secreted.
Tissue specificity	Synthesized in the fat body and ovarian follicle cells and accumulate in the oocyte.
Developmental stage	Expressed during late pupal development and in adult females between days 1-3.
Induction	By beta-ecdysone; in males.
Post-translational modification	Tyrosine sulfation occurs in the female only and plays an essential functional role.
Sequence similarities	Belongs to the AB hydrolase superfamily. Lipase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
PTM	Phosphoprotein Sulfation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	lipid metabolic process Inferred from electronic annotation. Source: InterPro oogenesis Traceable author statement. Source: FlyBase sex differentiation Traceable author statement. Source: FlyBase
Cellular component	extracellular region Ref.7 Traceable author statement. Source: UniProtKB lipid particle Inferred from direct assay. Source: FlyBase
Molecular function	catalytic activity Inferred from electronic annotation. Source: InterPro identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-192398,EBI-192398
Nup107	Q9V466	1	EBI-192398,EBI-89961

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 442	423	Vitellogenin-2		PRO_0000017815
Amino acid modifications
	Modified residue	31	1	Phosphoserine Ref.8
	Modified residue	33	1	Phosphoserine Ref.8
	Modified residue	82	1	Phosphoserine Ref.8
	Modified residue	170	1	Phosphothreonine Ref.8
	Modified residue	172	1	Sulfotyrosine
	Modified residue	173	1	Phosphoserine Ref.8
	Modified residue	178	1	Phosphoserine Ref.8
	Modified residue	181	1	Phosphoserine Ref.8
	Modified residue	182	1	Phosphoserine Ref.8
	Modified residue	183	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	68	1	L → M Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P02844-1 [UniParc]. Last modified June 20, 2001. Version 2. Checksum: 7DBD384E37E84F14	FASTA	442	49,660
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and structure conservation in yolk proteins and their genes." Hung M.-C., Wensink P.C. J. Mol. Biol. 164:481-492(1983) [PubMed: 6405043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Canton-S.
[2]	"The genome sequence of Drosophila melanogaster." 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. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." 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. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"A Drosophila full-length cDNA resource." 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. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[5]	"Vitellogenin in Drosophila melanogaster: a comparison of the YPI and YPII genes and their transcription products." Hovemann B., Galler R. Nucleic Acids Res. 10:2261-2274(1982) [PubMed: 6806773] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
[6]	"Purification of yolk protein 2 of Drosophila melanogaster and identification of its site of tyrosine sulfation." Baeuerle P.A., Lottspeich F., Huttner W.B. J. Biol. Chem. 263:14925-14929(1988) [PubMed: 3139663] [Abstract] Cited for: PROTEIN SEQUENCE OF 168-176, SULFATION.
[7]	"Tyrosine sulfation of yolk proteins 1, 2, and 3 in Drosophila melanogaster." Baeuerle P.A., Huttner W.B. J. Biol. Chem. 260:6434-6439(1985) [PubMed: 3922974] [Abstract] Cited for: SULFATION.
[8]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-33; SER-82; THR-170; SER-173; SER-178; SER-181; SER-182 AND SER-183, MASS SPECTROMETRY. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014298 Genomic DNA. Translation: AAF46547.3. AY061042 mRNA. Translation: AAL28590.1. X01524 Genomic DNA. Translation: CAA25710.1.
PIR	VJFF2. A03333.
RefSeq	NP_511102.3.
UniGene	Dm.6718
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:19994N.
IntAct	P02844. 6 interactions.
Genome annotation databases
Ensembl	FBgn0005391. Drosophila melanogaster. [Contig view]
GeneID	31938.
KEGG	dme:Dmel_CG2979.
NMPDR	fig|7227.3.peg.17211.
Organism-specific databases
FlyBase	FBgn0005391. Yp2.
Phylogenomic databases
HOGENOM	P02844.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-001287-MON.
Gene expression databases
ArrayExpress	P02844.
GermOnline	CG2979. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000734. Lipase. IPR013818. Lipase_N. [Graphical view]
PANTHER	PTHR11610. Lipase. 1 hit.
Pfam	PF00151. Lipase. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	776039.

Entry information

Entry name

VIT2_DROME

Accession

Primary (citable) accession number: P02844
Secondary accession number(s): Q9W2Z0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	June 20, 2001
Last modified:	June 16, 2009
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project