Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q55CS7 (MPL1_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MAP kinase phosphatase with leucine-rich repeats protein 1

EC=3.1.3.16
EC=3.1.3.48
Gene names
Name:mpl1
ORF Names:DDB_G0269918
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length834 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probable phosphatase with dual specificity toward Ser/Thr and Tyr-containing proteins By similarity. Dephosphorylates pNPP, in vitro. Essential for proper regulation of erkB (erk2) and optimal motility during development. Ref.2

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Developmental stage

Expressed (at protein levels). Up-regulated upon starvation, reaching a maximum around 10 hours. Expression subsequently declined but is present throughout development. Ref.2

Disruption phenotype

Cells result in higher prestimulus and persistent stimulation erkB phosphorylation upon cAMP stimulation, display strong defects in motility, and more rapid cAMP production. Cells fail to display aggregates, fruiting bodies, fail to form territorial streams and are defective in cell migration (absence of random and directional migration) and in chemotaxis. Ref.2

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 10 LRR (leucine-rich) repeats.

Contains 1 tyrosine-protein phosphatase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 834834MAP kinase phosphatase with leucine-rich repeats protein 1
PRO_0000332956

Regions

Repeat160 – 18122LRR 1
Repeat183 – 20422LRR 2
Repeat206 – 22621LRR 3
Repeat229 – 25123LRR 4
Repeat252 – 27322LRR 5
Repeat274 – 29219LRR 6
Repeat298 – 31922LRR 7
Repeat321 – 34222LRR 8
Repeat345 – 36622LRR 9
Repeat368 – 38922LRR 10
Domain695 – 833139Tyrosine-protein phosphatase
Coiled coil555 – 61561 Potential
Compositional bias12 – 7059Thr-rich
Compositional bias428 – 4325Poly-Thr
Compositional bias481 – 49010Poly-Thr
Compositional bias518 – 5214Poly-Thr
Compositional bias561 – 5677Poly-Asn

Sites

Active site7781Phosphocysteine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q55CS7 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: 7DEDB07F407771FE

FASTA83494,023
        10         20         30         40         50         60 
MIFKKLFSKG STSPTTRPRG ATFSGTFPTD VLSDDGSGTN TNGLSNSTTN PSSIHSTPTT 

        70         80         90        100        110        120 
PTTTASTNLT NSNKLSTLAP ITNGNRSLRG SKDGSGTTKE SKKKVLTLNE KQKLLLKSME 

       130        140        150        160        170        180 
YIKGSGTYYG NYMEFYEIPI QIYVGTEPSE TYPSLSYNTE LRSLILDFNK ITEIPEQIGL 

       190        200        210        220        230        240 
LPNLKHLSLA ANQLSQVPEF LSQLKSLESL ELGINQFTSF PLNICKIKSL TLLRLETNNI 

       250        260        270        280        290        300 
KSLPDDFINL ENLKDLSLLD NQLKEIPDSL PNNIEKLNLG CNDIINSYSK SLIRISHSLT 

       310        320        330        340        350        360 
TLNLSENKIE VLDESLSCLV NVKTLILDCN MIKVIPGSVL GSWKSLVTLN LPHNFISDLP 

       370        380        390        400        410        420 
AEIVTLDNLR IIDLRGNNFE FCKNYPSSES SSILFKIEEF IKDKEKLKSL ILKENLEILS 

       430        440        450        460        470        480 
KLKDDNSTTT TTNINSNLDV PIIITTNIET IPTTSTTATT TETTNDITFK ISDITEIIEK 

       490        500        510        520        530        540 
TDTTTTTTTT NQTDNVKLEE KVYEKQENDE NNSVTLETTT TISIASDNTD EASIQIPQKE 

       550        560        570        580        590        600 
DGDKENLEND DKLLQESFSE NNNNNNNEKQ QEQQENPLKE SQGKIQQLEE ELEKLEQKQL 

       610        620        630        640        650        660 
ELKDKIRLEK IKYQEIQQQS PRLSQQENNQ EAIVVNTQPS SPPPTIIVNE QKSEKLENEK 

       670        680        690        700        710        720 
PTKREQPMVV VTKNNNKAEV EMTAPNQLIF WQSIVPDLII DKLYLGCREC AMNKSWLKDN 

       730        740        750        760        770        780 
NVTHILTVAN FKPLYPDLFK YLIINIDDVD EANIYQYFKE MNTFIDEGRE KGGVLIHCRA 

       790        800        810        820        830 
GVSRSATATI AYIMMKNSVK FQEAFDITIK GRSRIYPNRG FLNQLKKFEK DLSK 

« Hide

References

« Hide 'large scale' references
[1]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[2]"MPL1, a novel phosphatase with leucine-rich repeats, is essential for proper ERK2 phosphorylation and cell motility."
Rodriguez M., Kim B., Lee N.-S., Veeranki S., Kim L.
Eukaryot. Cell 7:958-966(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFI02000005 Genomic DNA. Translation: EAL72309.1.

3D structure databases

ProteinModelPortalQ55CS7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDBDRAFT_0190671.

Proteomic databases

PRIDEQ55CS7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0238871; DDB0238871; DDB_G0269918.
KEGGddi:DDB_G0269918.

Organism-specific databases

dictyBaseDDB_G0269918. mpl1.

Phylogenomic databases

eggNOGCOG4886.
OMAKGSGTYY.
ProtClustDBCLSZ2431421.

Family and domain databases

InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
PF12799. LRR_4. 1 hit.
[Graphical view]
SMARTSM00195. DSPc. 1 hit.
SM00369. LRR_TYP. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 9 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMPL1_DICDI
AccessionPrimary (citable) accession number: Q55CS7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: May 24, 2005
Last modified: April 16, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase