MPL3_DICDI
ID MPL3_DICDI Reviewed; 856 AA.
AC Q54Y32;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=MAP kinase phosphatase with leucine-rich repeats protein 3;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
GN Name=mpl3; ORFNames=DDB_G0278445;
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; AAFI02000023; EAL68395.1; -; Genomic_DNA.
DR RefSeq; XP_642370.1; XM_637278.1.
DR AlphaFoldDB; Q54Y32; -.
DR SMR; Q54Y32; -.
DR STRING; 44689.DDB0238874; -.
DR PaxDb; Q54Y32; -.
DR EnsemblProtists; EAL68395; EAL68395; DDB_G0278445.
DR GeneID; 8621575; -.
DR KEGG; ddi:DDB_G0278445; -.
DR dictyBase; DDB_G0278445; mpl3.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_333851_0_0_1; -.
DR InParanoid; Q54Y32; -.
DR OMA; RDTPNYD; -.
DR PRO; PR:Q54Y32; -.
DR Proteomes; UP000002195; Chromosome 3.
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; -; 2.
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; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00404; PTPc_motif; 1.
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; Lipoprotein; Myristate;
KW Protein phosphatase; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..856
FT /note="MAP kinase phosphatase with leucine-rich repeats
FT protein 3"
FT /id="PRO_0000332957"
FT REPEAT 344..365
FT /note="LRR 1"
FT REPEAT 370..391
FT /note="LRR 2"
FT REPEAT 392..413
FT /note="LRR 3"
FT REPEAT 416..437
FT /note="LRR 4"
FT REPEAT 439..461
FT /note="LRR 5"
FT REPEAT 462..484
FT /note="LRR 6"
FT REPEAT 485..506
FT /note="LRR 7"
FT REPEAT 507..528
FT /note="LRR 8"
FT DOMAIN 632..773
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 717
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 856 AA; 95418 MW; FA899072865A6CEA CRC64;
MGNSHSSENG GNSGSGGGSG GGGSGYSGVS ENMIIDLEGR YHIDYKNRNY KKLKPQMFST
FFEHYEIVQA DSLINSDFIK NKTVKKNRDN SSNNNSNNNS NNNNNNNTLN NSTIITTTTT
TTTTSTPTTT IMITPPQQQQ QQRTSLDLTN RDISESSTPN EQQIRLAQEE TENQEIVESS
FLKSSPVPSP SSSVLKSFES DFQLNTDLTT ETFDDNSAEK KRQQQQQQQQ NEDSKQSSQQ
QTQKSKDKDE SAKIVNNKSS STTNIKPILA AAQTSRSTSI PAFNRNKTKE PTKQKIKKEH
STLRKNSLSS SNIITPNNTT NTNAKDGASY FNENSLMSVK SDIKIFSLDL SINRLENITN
DILSIMARFE IQELTLSTNF FQIIPDLQLV KSLTTVNLTR NKLSKLQTSV FIELPSLTSL
ILDRNFISSI PDDIDQIKNL KYLSIKHNAL EYLPNSLSNL SQLISLDLSQ NKLKTLPPNF
DDLINLRMVW LSYNQITSLP SMRKLVNLVT FDISSNKLLS LPKDFAYLVP SRIKQSYSDI
DIDEYDENIN TCNNINSNNN DSNNSNNNNN NNNDNNNNCN KNNILEMINS TELEGGGLGC
LKELNIRDNR ELISLPVEYK QVESLMTLVT SIPSEIIPGI FLGGLDSANN APILQTLGIT
HILLAIGDCE PFFPKTFKYY SIDDARDAPQ YDISQHFEQT NCFIESGRKS GGVLVHCRAG
ISRSSTLVIS YLMKYQRMTF KQAMDLVQSK RPQIQPNPGF KDQLLKYEAK LFCTNILNIS
SHNSNNKNNN SSNNRKSINN RKSNNIIITI NNSSNSNNNN STDNSNNSST STTPNLSSLS
SDSSSSASLS KLSISK
