MPL2_DICDI
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 03-AUG-2022, entry version 102.
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 (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).
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}.
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DR EMBL; AAFI02000005; EAL72694.2; -; Genomic_DNA.
DR RefSeq; XP_646403.2; XM_641311.2.
DR AlphaFoldDB; Q55CS8; -.
DR SMR; Q55CS8; -.
DR STRING; 44689.DDB0238870; -.
DR PaxDb; Q55CS8; -.
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; YENISMY; -.
DR PhylomeDB; Q55CS8; -.
DR Reactome; R-DDI-202670; ERKs are inactivated.
DR PRO; PR:Q55CS8; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
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 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
