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Q9VVW5

- DUSK3_DROME

UniProt

Q9VVW5 - DUSK3_DROME

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Protein

Dual specificity protein phosphatase Mpk3

Gene

Mkp3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Negatively regulates the activity of members of the MAP kinase family in response to changes in the cellular environment. Has a specificity for the ERK family. Acts as negative regulator in a variety of developmental processes including cell differentiation and proliferation controlled by the Ras/ERK pathway. Suppresses the photoreceptor cell differentiation and wing vein formation. Required for proper oogenesis and early embryogenesis. Functions autonomously in a subset of photoreceptor progenitor cells in eye imaginal disks. Appears also to be required in surrounding non-neuronal cells for ommatidial patterning and photoreceptor differentiation. Plays a role in the maintenance of epithelial integrity during tracheal development.6 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.By similarity
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Enzyme regulationi

Activity abolished by tyrosine phosphatase inhibitor sodium vanadate. Activated by rl.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei302 – 3021Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. phosphatase activity Source: FlyBase
  3. protein tyrosine/serine/threonine phosphatase activity Source: FlyBase
  4. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. imaginal disc-derived wing vein specification Source: FlyBase
  2. maintenance of epithelial integrity, open tracheal system Source: FlyBase
  3. mucosal immune response Source: FlyBase
  4. negative regulation of MAPK cascade Source: FlyBase
  5. primary branching, open tracheal system Source: FlyBase
  6. protein dephosphorylation Source: FlyBase
  7. regulation of cell proliferation Source: FlyBase
  8. single organismal cell-cell adhesion Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SignaLinkiQ9VVW5.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase Mpk3By similarity (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Drosophila MKP31 Publication
Short name:
DMKP31 Publication
Mitogen-activated protein kinase phosphatase 3ImportedBy similarity
Short name:
MAP kinase phosphatase 3By similarity
Short name:
MKP-3By similarity
Gene namesi
Name:Mkp3
ORF Names:CG14080
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036844. Mkp3.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Homozygous embryonic lethal, while hypomorphic alleles (reduction in gene dosage) lead to extra photoreceptor cells in the eye, ectopic veins in wings and severe defects in oogenesis in females. Females with the germ line mutation lay only a small number of eggs. The laid eggs are abnormal, approximately 77% of the laid eggs are shorter and some display severe defects in chorion formation. These embryos could not escape the embryonic stage and progress beyond the two-nuclei stage. Null mutants are viable and fertile exhibiting a mild, but significant increase in wing vein material. They are slightly rough eyed. Null mutation affects the R3 and R4 photoreceptors with a low penetrance resulting in either the loss of one cell of the R3/R4 pair or in the misdifferentiation of these photoreceptors. R3 and R4 are often symmetrically arranged in the eye in opposite to the asymmetrical positions they adopt in wild-type ommatidium. Ommatidia of the null mutants often contain a mystery cell having differentiated as a photoreceptor. Null mutants also exhibit mild delay in tracheal branching. Delay in 12% dorsal branches (DBs) compared with 0.3% in wild-type between metameres 4 to 8 that have reached the dorsal midline at stage 14-15. Null mutants have defects in cell intercalation.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 572RR → AA: Reduces binding affinity to substrate by approximately 18-fold. 1 Publication
Mutagenesisi302 – 3021C → A: Loss of activity. 1 Publication
Mutagenesisi316 – 3161Y → N: Causes the differentiation of ectopic vein stretches in several regions of the wing. Shows elimination of distal stretches of longitunal veins L2-L5. Causes substitution of the wing by proximal hinge tissue. Affects the development of macrochaetae or the formation of the thorax. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Dual specificity protein phosphatase Mpk3PRO_0000408762Add
BLAST

Proteomic databases

PaxDbiQ9VVW5.

Expressioni

Tissue specificityi

Ubiquitous expression in eye and wing imaginal disks. Enriched in ovary.1 Publication

Developmental stagei

Low expression in the various developmental stages, although relatively high levels detected in 8 to 12 h embryos, as well as in pupae and adults, particularly in the head region. Expressed in third-instar eye imaginal disks posterior to the morphogenetic furrow where photoreceptor differentiation occurs. Preferentially detected in wing imaginal disks in two stripes of cells interrupted at the dorsoventral boundary, which correspond to the developing veins L3 and L4. In pupal wings the maximal levels of expression are present in all longitudinal veins, with low levels detected in most intervein cells. Uniformly distributed in the syncytial blastoderm (stage 4). At early stage 5, accumulates at the embryonic poles and is absent from the central region. This pattern evolves very rapidly with the formation of a third central domain of expression from 85% to 40% egg length. In older embryos, the main places where high levels accumulate correspond to the invaginating mesoderm, the tracheal pits at stage 11, the visceral mesoderm at stage 13, the heart, the midline and the apodema. Expression in tracheal branches at later stages.4 Publications

Gene expression databases

BgeeiQ9VVW5.
ExpressionAtlasiQ9VVW5. differential.

Interactioni

Subunit structurei

Interacts (via N-terminal region) with phosphorylated rl.1 Publication

Protein-protein interaction databases

STRINGi7227.FBpp0074802.

Structurei

3D structure databases

ProteinModelPortaliQ9VVW5.
SMRiQ9VVW5. Positions 13-151, 215-358.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 149128RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini215 – 357143Tyrosine-protein phosphataseSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi201 – 2099Poly-HisSequence Analysis

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.Sequence Analysis

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
InParanoidiQ9VVW5.
KOiK04459.
OrthoDBiEOG793B7W.
PhylomeDBiQ9VVW5.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform BImported (identifier: Q9VVW5-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPETEHETCS KEWLQSQLRS LDSKDLILLD CRGSHEYSES HIRGAVNLCI
60 70 80 90 100
PSIVLRRLAV GKIDLASTIK SPELKQRIQS GYKLCWFILY NGEGVPGQNQ
110 120 130 140 150
EIAGAGSLAV AMDSIISILH RRLKQDGCRV VALQDGFNNF RQAFPEWCED
160 170 180 190 200
DNQTHSKEIE SSRNVQTDQL MGLRSLRIST TQSDSACSSS AESSDCESSS
210 220 230 240 250
HHHHHHSHHN YNEAPVEIIP GLLFLGNATH SCDSEALKKY NIKYVLNVTP
260 270 280 290 300
DLPNKFKESG DIKYLQIPIT DHYSQDLAIH FPDAIQFIEE ARSASSVVLV
310 320 330 340 350
HCLAGVSRSV TVTLAYLMHT RGLSLNDAFA MVRDRKPDVS PNFHFMQQLL
360 370 380 390 400
SFESQLRLRP GSRFSCSCIA PDCNCMQTTG FMATHLANAT GVSPDSGIEF
410
DRWTPSDTGL K
Length:411
Mass (Da):45,792
Last modified:October 1, 2002 - v2
Checksum:iD3C689BC953B29E3
GO
Isoform AImported (identifier: Q9VVW5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-170: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:241
Mass (Da):26,639
Checksum:i4B1AD996FA631B2E
GO

Sequence cautioni

The sequence AAO39540.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti208 – 2081H → L in AAK85311. (PubMed:11742539)Curated
Sequence conflicti208 – 2081H → L in AAL25511. (PubMed:12537569)Curated
Sequence conflicti384 – 3841T → A in AAK85311. (PubMed:11742539)Curated
Sequence conflicti384 – 3841T → A in AAL25511. (PubMed:12537569)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 170170Missing in isoform A. 1 PublicationVSP_041148Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY043264 mRNA. Translation: AAK85311.1.
AE014296 Genomic DNA. Translation: AAF49192.2.
AE014296 Genomic DNA. Translation: AAF49193.2.
AY060472 mRNA. Translation: AAL25511.1.
BT003536 mRNA. Translation: AAO39540.1. Different initiation.
RefSeqiNP_001262032.1. NM_001275103.1. [Q9VVW5-1]
NP_649087.1. NM_140830.2. [Q9VVW5-1]
NP_730385.1. NM_168785.1. [Q9VVW5-2]
UniGeneiDm.3967.

Genome annotation databases

EnsemblMetazoaiFBtr0075035; FBpp0074802; FBgn0036844. [Q9VVW5-1]
FBtr0333220; FBpp0305422; FBgn0036844. [Q9VVW5-1]
GeneIDi40081.
KEGGidme:Dmel_CG14080.
UCSCiCG14080-RB. d. melanogaster. [Q9VVW5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY043264 mRNA. Translation: AAK85311.1 .
AE014296 Genomic DNA. Translation: AAF49192.2 .
AE014296 Genomic DNA. Translation: AAF49193.2 .
AY060472 mRNA. Translation: AAL25511.1 .
BT003536 mRNA. Translation: AAO39540.1 . Different initiation.
RefSeqi NP_001262032.1. NM_001275103.1. [Q9VVW5-1 ]
NP_649087.1. NM_140830.2. [Q9VVW5-1 ]
NP_730385.1. NM_168785.1. [Q9VVW5-2 ]
UniGenei Dm.3967.

3D structure databases

ProteinModelPortali Q9VVW5.
SMRi Q9VVW5. Positions 13-151, 215-358.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7227.FBpp0074802.

Proteomic databases

PaxDbi Q9VVW5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0075035 ; FBpp0074802 ; FBgn0036844 . [Q9VVW5-1 ]
FBtr0333220 ; FBpp0305422 ; FBgn0036844 . [Q9VVW5-1 ]
GeneIDi 40081.
KEGGi dme:Dmel_CG14080.
UCSCi CG14080-RB. d. melanogaster. [Q9VVW5-1 ]

Organism-specific databases

CTDi 40081.
FlyBasei FBgn0036844. Mkp3.

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00760000118902.
InParanoidi Q9VVW5.
KOi K04459.
OrthoDBi EOG793B7W.
PhylomeDBi Q9VVW5.

Enzyme and pathway databases

SignaLinki Q9VVW5.

Miscellaneous databases

ChiTaRSi Mkp3. drosophila.
GenomeRNAii 40081.
NextBioi 816901.

Gene expression databases

Bgeei Q9VVW5.
ExpressionAtlasi Q9VVW5. differential.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view ]
PIRSFi PIRSF000939. MAPK_Ptase. 1 hit.
PRINTSi PR01764. MAPKPHPHTASE.
SMARTi SM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a Drosophila homologue of mitogen-activated protein kinase phosphatase-3 which has a high substrate specificity towards extracellular-signal-regulated kinase."
    Kim S.H., Kwon H.B., Kim Y.S., Ryu J.H., Kim K.S., Ahn Y., Lee W.J., Choi K.Y.
    Biochem. J. 361:143-151(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH RL, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF 56-ARG-ARG-57 AND CYS-302.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: BerkeleyImported.
    Tissue: Embryo.
  6. "Regulation of Drosophila MKP-3 by Drosophila ERK."
    Kim S.E., Kim S.H., Choi K.Y.
    Ann. N. Y. Acad. Sci. 1010:51-61(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  7. "The Drosophila dual-specificity ERK phosphatase DMKP3 cooperates with the ERK tyrosine phosphatase PTP-ER."
    Rintelen F., Hafen E., Nairz K.
    Development 130:3479-3490(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  8. "MKP-3 has essential roles as a negative regulator of the Ras/mitogen-activated protein kinase pathway during Drosophila development."
    Kim M., Cha G.H., Kim S., Lee J.H., Park J., Koh H., Choi K.Y., Chung J.
    Mol. Cell. Biol. 24:573-583(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  9. "Conserved cross-interactions in Drosophila and Xenopus between Ras/MAPK signaling and the dual-specificity phosphatase MKP3."
    Gomez A.R., Lopez-Varea A., Molnar C., de la Calle-Mustienes E., Ruiz-Gomez M., Gomez-Skarmeta J.L., de Celis J.F.
    Dev. Dyn. 232:695-708(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, MUTAGENESIS OF TYR-316.
  10. "Egfr is essential for maintaining epithelial integrity during tracheal remodelling in Drosophila."
    Cela C., Llimargas M.
    Development 133:3115-3125(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiDUSK3_DROME
AccessioniPrimary (citable) accession number: Q9VVW5
Secondary accession number(s): Q86P14, Q95SV1, Q9VVW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3