MPL1_DICDI
ID MPL1_DICDI Reviewed; 834 AA.
AC Q55CS7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=MAP kinase phosphatase with leucine-rich repeats protein 1;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
GN Name=mpl1; ORFNames=DDB_G0269918;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=18408056; DOI=10.1128/ec.00442-07;
RA Rodriguez M., Kim B., Lee N.-S., Veeranki S., Kim L.;
RT "MPL1, a novel phosphatase with leucine-rich repeats, is essential for
RT proper ERK2 phosphorylation and cell motility.";
RL Eukaryot. Cell 7:958-966(2008).
CC -!- FUNCTION: Probable phosphatase with dual specificity toward Ser/Thr and
CC Tyr-containing proteins (By similarity). Dephosphorylates pNPP, in
CC vitro. Essential for proper regulation of erkB (erk2) and optimal
CC motility during development. {ECO:0000250,
CC ECO:0000269|PubMed:18408056}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- DEVELOPMENTAL STAGE: Expressed (at protein levels). Up-regulated upon
CC starvation, reaching a maximum around 10 hours. Expression subsequently
CC declined but is present throughout development.
CC {ECO:0000269|PubMed:18408056}.
CC -!- DISRUPTION PHENOTYPE: Cells result in higher prestimulus and persistent
CC stimulation erkB phosphorylation upon cAMP stimulation, display strong
CC defects in motility, and more rapid cAMP production. Cells fail to
CC display aggregates, fruiting bodies, fail to form territorial streams
CC and are defective in cell migration (absence of random and directional
CC migration) and in chemotaxis. {ECO:0000269|PubMed:18408056}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72309.1; -; Genomic_DNA.
DR RefSeq; XP_646404.1; XM_641312.1.
DR AlphaFoldDB; Q55CS7; -.
DR SMR; Q55CS7; -.
DR STRING; 44689.DDB0238871; -.
DR PaxDb; Q55CS7; -.
DR EnsemblProtists; EAL72309; EAL72309; DDB_G0269918.
DR GeneID; 8617360; -.
DR KEGG; ddi:DDB_G0269918; -.
DR dictyBase; DDB_G0269918; mpl1.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_396611_0_0_1; -.
DR InParanoid; Q55CS7; -.
DR OMA; KGSGTYY; -.
DR Reactome; R-DDI-202670; ERKs are inactivated.
DR PRO; PR:Q55CS7; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IC:dictyBase.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IMP:dictyBase.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; TAS:dictyBase.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006171; P:cAMP biosynthetic process; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:dictyBase.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51450; LRR; 9.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 2: Evidence at transcript level;
KW Chemotaxis; Coiled coil; Hydrolase; Leucine-rich repeat;
KW Protein phosphatase; Reference proteome; Repeat.
FT CHAIN 1..834
FT /note="MAP kinase phosphatase with leucine-rich repeats
FT protein 1"
FT /id="PRO_0000332956"
FT REPEAT 160..181
FT /note="LRR 1"
FT REPEAT 183..204
FT /note="LRR 2"
FT REPEAT 206..226
FT /note="LRR 3"
FT REPEAT 229..251
FT /note="LRR 4"
FT REPEAT 252..273
FT /note="LRR 5"
FT REPEAT 274..292
FT /note="LRR 6"
FT REPEAT 298..319
FT /note="LRR 7"
FT REPEAT 321..342
FT /note="LRR 8"
FT REPEAT 345..366
FT /note="LRR 9"
FT REPEAT 368..389
FT /note="LRR 10"
FT DOMAIN 695..834
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 555..615
FT /evidence="ECO:0000255"
FT COMPBIAS 8..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 778
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 834 AA; 94023 MW; 7DEDB07F407771FE CRC64;
MIFKKLFSKG STSPTTRPRG ATFSGTFPTD VLSDDGSGTN TNGLSNSTTN PSSIHSTPTT
PTTTASTNLT NSNKLSTLAP ITNGNRSLRG SKDGSGTTKE SKKKVLTLNE KQKLLLKSME
YIKGSGTYYG NYMEFYEIPI QIYVGTEPSE TYPSLSYNTE LRSLILDFNK ITEIPEQIGL
LPNLKHLSLA ANQLSQVPEF LSQLKSLESL ELGINQFTSF PLNICKIKSL TLLRLETNNI
KSLPDDFINL ENLKDLSLLD NQLKEIPDSL PNNIEKLNLG CNDIINSYSK SLIRISHSLT
TLNLSENKIE VLDESLSCLV NVKTLILDCN MIKVIPGSVL GSWKSLVTLN LPHNFISDLP
AEIVTLDNLR IIDLRGNNFE FCKNYPSSES SSILFKIEEF IKDKEKLKSL ILKENLEILS
KLKDDNSTTT TTNINSNLDV PIIITTNIET IPTTSTTATT TETTNDITFK ISDITEIIEK
TDTTTTTTTT NQTDNVKLEE KVYEKQENDE NNSVTLETTT TISIASDNTD EASIQIPQKE
DGDKENLEND DKLLQESFSE NNNNNNNEKQ QEQQENPLKE SQGKIQQLEE ELEKLEQKQL
ELKDKIRLEK IKYQEIQQQS PRLSQQENNQ EAIVVNTQPS SPPPTIIVNE QKSEKLENEK
PTKREQPMVV VTKNNNKAEV EMTAPNQLIF WQSIVPDLII DKLYLGCREC AMNKSWLKDN
NVTHILTVAN FKPLYPDLFK YLIINIDDVD EANIYQYFKE MNTFIDEGRE KGGVLIHCRA
GVSRSATATI AYIMMKNSVK FQEAFDITIK GRSRIYPNRG FLNQLKKFEK DLSK
