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Q03019 (TWINE_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cdc25-like protein phosphatase twine

EC=3.1.3.48
Gene names
Name:twe
ORF Names:CG4965
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required during meiosis. Regulates the transition from the extended G2 phase to the onset of the first meiotic division.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Tissue specificity

Expressed in developing male and female germ cells.

Sequence similarities

Belongs to the MPI phosphatase family.

Contains 1 rhodanese domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Meiosis
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

cellularization

Inferred from mutant phenotype PubMed 2492966. Source: FlyBase

embryo development

Inferred from mutant phenotype PubMed 2492966. Source: FlyBase

male meiosis

Inferred from mutant phenotype Ref.1. Source: FlyBase

meiotic G2/MI transition

Traceable author statement PubMed 9813190. Source: FlyBase

meiotic nuclear envelope disassembly

Inferred from mutant phenotype PubMed 18052611. Source: FlyBase

peptidyl-tyrosine dephosphorylation

Inferred from sequence or structural similarity Ref.2Ref.6Ref.1. Source: GOC

pole cell formation

Inferred from mutant phenotype PubMed 2492966. Source: FlyBase

protein dephosphorylation

Inferred from sequence or structural similarity Ref.6Ref.1. Source: FlyBase

regulation of meiotic cell cycle

Inferred from mutant phenotype PubMed 18927152. Source: FlyBase

regulation of syncytial blastoderm mitotic cell cycle

Inferred from mutant phenotype Ref.1. Source: FlyBase

spermatogenesis

Inferred from mutant phenotype PubMed 10559904PubMed 23409089. Source: FlyBase

   Cellular_componentintracellular

Inferred from electronic annotation. Source: InterPro

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from sequence or structural similarity Ref.2Ref.6Ref.1. Source: FlyBase

protein tyrosine/serine/threonine phosphatase activity

Non-traceable author statement PubMed 10908587. Source: FlyBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

cdc2P235724EBI-138996,EBI-108689

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Cdc25-like protein phosphatase twine
PRO_0000198659

Regions

Domain265 – 371107Rhodanese

Sites

Active site3181 By similarity

Experimental info

Sequence conflict481L → M in CAA48783. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q03019 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 0F8626692B683D08

FASTA42648,320
        10         20         30         40         50         60 
MASKRLMLDV EEEDDESGAC GQENFDPHDA DMEYQAKRRK SAVQETPLQW MLKRHIPAST 

        70         80         90        100        110        120 
TVLSPITELS QNMNGARLDG TPKSTQRIPA NRTLNNFNSL SSRTLGSFSS SCSSYESGNS 

       130        140        150        160        170        180 
LDDEYMDMFE MESAENHNLE LPDDLEVLLS GQLKSESNLE EMSNKKGSLR RCLSMYPSEQ 

       190        200        210        220        230        240 
PEEAVQEPDQ ETNMPMKKMQ RKTLSMNDAE IMRALGDEPE LIGDLSKPCT LPCLATGIRH 

       250        260        270        280        290        300 
RDLKTISSDT LARLIQGEFD EQLGSQGGYE IIDCRYPYEF LGGHIRGAKN LYTRGQIQEA 

       310        320        330        340        350        360 
FPTLTSNQEN RRIYVFHCEF SSERGPKLLR YLRSNDRSQH THNYPALDYP ELYILHNGYK 

       370        380        390        400        410        420 
EFFGLYSQLC QPSQYVPMLA PAHNDEFRYF RAKTKSWQCG EGGDSGIGGG GSRGLRKSRS 


RLLYAE 

« Hide

References

« Hide 'large scale' references
[1]"Twine, a cdc25 homolog that functions in the male and female germline of Drosophila."
Alphey L.S., Jimenez J., White-Cooper H., Dawson I., Nurse P., Glover D.M.
Cell 69:977-988(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R. expand/collapse author list , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[4]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[6]"The Drosophila cdc25 homolog twine is required for meiosis."
Courtot C., Fankhauser C., Simanis V., Lehner C.F.
Development 116:405-416(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-426.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M94158 mRNA. Translation: AAA28413.1.
AE014134 Genomic DNA. Translation: AAF53508.1.
AY061266 mRNA. Translation: AAL28814.1.
X69018 mRNA. Translation: CAA48783.1.
PIRA41910.
RefSeqNP_001260491.1. NM_001273562.1.
NP_001260492.1. NM_001273563.1.
NP_001260493.1. NM_001273564.1.
NP_476633.1. NM_057285.4.
UniGeneDm.3667.

3D structure databases

ProteinModelPortalQ03019.
SMRQ03019. Positions 221-387.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60966. 6 interactions.
DIPDIP-23538N.
IntActQ03019. 2 interactions.
MINTMINT-942016.
STRING7227.FBpp0080412.

Proteomic databases

PaxDbQ03019.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080855; FBpp0080412; FBgn0002673.
FBtr0331444; FBpp0303861; FBgn0002673.
FBtr0331445; FBpp0303862; FBgn0002673.
FBtr0331446; FBpp0303863; FBgn0002673.
GeneID34954.
KEGGdme:Dmel_CG4965.
UCSCCG4965-RA. d. melanogaster.

Organism-specific databases

CTD34954.
FlyBaseFBgn0002673. twe.

Phylogenomic databases

eggNOGCOG5105.
GeneTreeENSGT00390000018747.
InParanoidQ03019.
OMARAKTKSW.
OrthoDBEOG757D02.
PhylomeDBQ03019.

Gene expression databases

BgeeQ03019.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamPF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSPR00716. MPIPHPHTASE.
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi34954.
NextBio791075.

Entry information

Entry nameTWINE_DROME
AccessionPrimary (citable) accession number: Q03019
Secondary accession number(s): Q9V454
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase