ID MPL2_DICDI Reviewed; 695 AA. AC Q55CS8; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 2. DT 27-MAR-2024, entry version 109. DE RecName: Full=MAP kinase phosphatase with leucine-rich repeats protein 2; DE EC=3.1.3.16; DE EC=3.1.3.48; GN Name=mpl2; ORFNames=DDB_G0270688; OS Dictyostelium discoideum (Social amoeba). 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). CC -!- FUNCTION: Probable phosphatase with dual specificity toward Ser/Thr and CC Tyr-containing proteins. {ECO:0000250}. 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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class dual specificity subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAFI02000005; EAL72694.2; -; Genomic_DNA. DR RefSeq; XP_646403.2; XM_641311.2. DR AlphaFoldDB; Q55CS8; -. DR SMR; Q55CS8; -. DR STRING; 44689.Q55CS8; -. DR PaxDb; 44689-DDB0238870; -. DR EnsemblProtists; EAL72694; EAL72694; DDB_G0270688. DR GeneID; 8617359; -. DR KEGG; ddi:DDB_G0270688; -. DR dictyBase; DDB_G0270688; mpl2. DR eggNOG; KOG0619; Eukaryota. DR eggNOG; KOG1716; Eukaryota. DR HOGENOM; CLU_396611_0_0_1; -. DR InParanoid; Q55CS8; -. DR OMA; QDQCDIL; -. DR PhylomeDB; Q55CS8; -. DR PRO; PR:Q55CS8; -. DR Proteomes; UP000002195; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. 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; IEA:InterPro. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR CDD; cd14498; DSP; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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 PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR10159:SF515; MAP KINASE PHOSPHATASE WITH LEUCINE-RICH REPEATS PROTEIN 1-RELATED; 1. DR Pfam; PF00782; DSPc; 1. DR Pfam; PF00560; LRR_1; 1. DR Pfam; PF13855; LRR_8; 2. DR SMART; SM00195; DSPc; 1. DR SMART; SM00364; LRR_BAC; 5. DR SMART; SM00369; LRR_TYP; 7. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR SUPFAM; SSF52058; L domain-like; 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 3: Inferred from homology; KW Hydrolase; Leucine-rich repeat; Protein phosphatase; Reference proteome; KW Repeat. FT CHAIN 1..695 FT /note="MAP kinase phosphatase with leucine-rich repeats FT protein 2" FT /id="PRO_0000332955" FT REPEAT 101..122 FT /note="LRR 1" FT REPEAT 124..145 FT /note="LRR 2" FT REPEAT 147..167 FT /note="LRR 3" FT REPEAT 170..191 FT /note="LRR 4" FT REPEAT 193..214 FT /note="LRR 5" FT REPEAT 215..235 FT /note="LRR 6" FT REPEAT 239..260 FT /note="LRR 7" FT REPEAT 262..283 FT /note="LRR 8" FT REPEAT 286..307 FT /note="LRR 9" FT REPEAT 309..330 FT /note="LRR 10" FT DOMAIN 556..695 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 413..438 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 492..519 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 413..429 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 639 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" SQ SEQUENCE 695 AA; 79425 MW; 8E8B6432645BDC30 CRC64; MFLKKLLKGS SNSTRPRGAT FNGIYTGGDN LSGSSEQNYN NSLTTSTKQT NRQTLLLKSM EYINGSSTYY GNYMDYFDIP VQLFVGGEQS EIYPMLSYNQ SLKSLILDFN KITEIPDCIT LLPNLNHLSL AANQLTHVPE FLSQLKSLET FEIGINQFTC FPLNVCKIKS LTSLHLETNN IKSLPEEFLN LVNLKDLSLF DNQLKEIPDS LPNNIEKLNL GCNDISSSKS DSLIRISHSL TTLNLSENKI EELDESLSCL VNVKTLMLDC NMIKVIPGSV LGSWKSLVTL NLPHNLISDL PPEVILLSNL RIIDLRGNNF ENCKKLIPTE SSTPISFKIE DFIQNKERIN SLKFDNIEIL PTTNSIINSN NNNYEVITTT ATTKNIIENK EDNDEKLLNN STISIVLDSN NKSENNEINE NNQLLTTDDD YNTDKNDSFT ESEDIIKKIQ IELDSIEIQQ KQLLLKQIKL KEKMKKEKNK LFKFQQQEII HQEQLPQSKP ENEKLTNIPE QQQKQQQQQQ QQEVQQPIIT LTKSTSSKVE VEMIVPNQLI FWQSIVPDLI IDKLYLGCRE CAMNKSWLKD NNVTHILTVA NFKPLYPDLF KYLIINIEDV DEANIYQHFK EMNAFIDEGR EKGGVLIHCR AGVSRSASAT MAFIMMKNSL KFQEAFDITI KGRPRIYPNI GFINQLKKFE KDLFK //