SDP1_YEAST
ID SDP1_YEAST Reviewed; 209 AA.
AC P40479; D6VVH4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Dual-specificity protein phosphatase SDP1;
DE EC=3.1.3.48;
DE AltName: Full=Stress-inducible MAPK phosphatase;
GN Name=SDP1; OrderedLocusNames=YIL113W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=12220658; DOI=10.1016/s0014-5793(02)03220-9;
RA Collister M., Didmon M.P., MacIsaac F., Stark M.J., MacDonald N.Q.,
RA Keyse S.M.;
RT "YIL113w encodes a functional dual-specificity protein phosphatase which
RT specifically interacts with and inactivates the Slt2/Mpk1p MAP kinase in S.
RT cerevisiae.";
RL FEBS Lett. 527:186-192(2002).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 17-198 OF WILD TYPE AND MUTANT
RP SER-142, FUNCTION, AND DISULFIDE BOND.
RX PubMed=17495930; DOI=10.1038/nature05804;
RA Fox G.C., Shafiq M., Briggs D.C., Knowles P.P., Collister M., Didmon M.J.,
RA Makrantoni V., Dickinson R.J., Hanrahan S., Totty N., Stark M.J.,
RA Keyse S.M., McDonald N.Q.;
RT "Redox-mediated substrate recognition by Sdp1 defines a new group of
RT tyrosine phosphatases.";
RL Nature 447:487-492(2007).
CC -!- FUNCTION: Mediates dephosphorylation of MAPK substrates such as SLT2,
CC acquiring enhanced catalytic activity under oxidative conditions.
CC {ECO:0000269|PubMed:12220658, ECO:0000269|PubMed:17495930}.
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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; Z38125; CAA86267.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08440.1; -; Genomic_DNA.
DR PIR; S48459; S48459.
DR RefSeq; NP_012153.1; NM_001179461.1.
DR PDB; 2J16; X-ray; 2.70 A; A/B=17-198.
DR PDB; 2J17; X-ray; 2.84 A; A/B=17-198.
DR PDBsum; 2J16; -.
DR PDBsum; 2J17; -.
DR AlphaFoldDB; P40479; -.
DR SMR; P40479; -.
DR BioGRID; 34878; 71.
DR DIP; DIP-1899N; -.
DR IntAct; P40479; 9.
DR MINT; P40479; -.
DR STRING; 4932.YIL113W; -.
DR iPTMnet; P40479; -.
DR PaxDb; P40479; -.
DR PRIDE; P40479; -.
DR EnsemblFungi; YIL113W_mRNA; YIL113W; YIL113W.
DR GeneID; 854693; -.
DR KEGG; sce:YIL113W; -.
DR SGD; S000001375; SDP1.
DR VEuPathDB; FungiDB:YIL113W; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000175236; -.
DR HOGENOM; CLU_1316327_0_0_1; -.
DR InParanoid; P40479; -.
DR OMA; SEVHIAP; -.
DR BioCyc; YEAST:G3O-31367-MON; -.
DR Reactome; R-SCE-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-SCE-202670; ERKs are inactivated.
DR Reactome; R-SCE-5675221; Negative regulation of MAPK pathway.
DR EvolutionaryTrace; P40479; -.
DR PRO; PR:P40479; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40479; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0033550; F:MAP kinase tyrosine phosphatase activity; IDA:SGD.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IDA:SGD.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0000196; P:cell wall integrity MAPK cascade; IGI:SGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
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 SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Hydrolase; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..209
FT /note="Dual-specificity protein phosphatase SDP1"
FT /id="PRO_0000094924"
FT DOMAIN 59..196
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 111
FT /ligand="4-O-phospho-L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:62338"
FT DISULFID 47..142
FT /evidence="ECO:0000269|PubMed:17495930"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:2J16"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2J16"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2J16"
FT TURN 76..81
FT /evidence="ECO:0007829|PDB:2J16"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:2J16"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2J16"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2J16"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:2J16"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:2J16"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:2J16"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:2J16"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:2J16"
FT HELIX 181..195
FT /evidence="ECO:0007829|PDB:2J16"
SQ SEQUENCE 209 AA; 23886 MW; 678371462A890A69 CRC64;
MNIYTSPTRT PNIAPKSGQR PSLPMLATDE RSTDKESPNE DREFVPCSSL DVRRIYPKGP
LLVLPEKIYL YSEPTVKELL PFDVVINVAE EANDLRMQVP AVEYHHYRWE HDSQIALDLP
SLTSIIHAAT TKREKILIHC QCGLSRSATL IIAYIMKYHN LSLRHSYDLL KSRADKINPS
IGLIFQLMEW EVALNAKTNV QANSYRKVP
