Q55CS7 (MPL1_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	834 AA.
Sequence status	Complete.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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.

Ontologies

Keywords
Biological process	Chemotaxis
Domain	Coiled coil Leucine-rich repeat Repeat
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chemotaxis to cAMP Inferred from mutant phenotype Ref.2. Source: dictyBase negative regulation of MAP kinase activity Inferred from mutant phenotype Ref.2. Source: dictyBase peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC regulation of cellular component movement Inferred from mutant phenotype Ref.2. Source: dictyBase
Cellular_component	extracellular region Inferred by curator Ref.2. Source: dictyBase
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from mutant phenotype Ref.2. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 834	834	MAP kinase phosphatase with leucine-rich repeats protein 1		PRO_0000332956
Regions
	Repeat	160 – 181	22	LRR 1
	Repeat	183 – 204	22	LRR 2
	Repeat	206 – 226	21	LRR 3
	Repeat	229 – 251	23	LRR 4
	Repeat	252 – 273	22	LRR 5
	Repeat	274 – 292	19	LRR 6
	Repeat	298 – 319	22	LRR 7
	Repeat	321 – 342	22	LRR 8
	Repeat	345 – 366	22	LRR 9
	Repeat	368 – 389	22	LRR 10
	Domain	695 – 833	139	Tyrosine-protein phosphatase
	Coiled coil	555 – 615	61	Potential
	Compositional bias	12 – 70	59	Thr-rich
	Compositional bias	428 – 432	5	Poly-Thr
	Compositional bias	481 – 490	10	Poly-Thr
	Compositional bias	518 – 521	4	Poly-Thr
	Compositional bias	561 – 567	7	Poly-Asn
Sites
	Active site	778	1	Phosphocysteine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q55CS7 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 7DEDB07F407771FE	FASTA	834	94,023
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
RefSeq	XP_646404.1. XM_641312.1.
3D structure databases
HSSP	HSSP built from PDB template 1MKP based on UniProtKB Q16828.
ProteinModelPortal	Q55CS7.
ModBase	Search...
Proteomic databases
PRIDE	Q55CS7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0238871; DDB0238871; DDB_G0269918.
GeneID	8617360.
KEGG	ddi:DDB_G0269918.
Organism-specific databases
dictyBase	DDB_G0269918. mpl1.
Phylogenomic databases
eggNOG	COG4886.
OMA	KGSGTYY.
ProtClustDB	CLSZ2431421.
Family and domain databases
InterPro	IPR000340. 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]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. PF12799. LRR_4. 1 hit. [Graphical view]
SMART	SM00195. DSPc. 1 hit. SM00369. LRR_TYP. 1 hit. [Graphical view]
PROSITE	PS51450. LRR. 9 hits. PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MPL1_DICDI

Accession

Primary (citable) accession number: Q55CS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	May 24, 2005
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)