DUS29_ANOCA
ID DUS29_ANOCA Reviewed; 217 AA.
AC P0C598;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Dual specificity phosphatase 29;
DE AltName: Full=Dual specificity phosphatase DUPD1;
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:Q68J44};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q68J44};
GN Name=DUSP29; Synonyms=DUPD1;
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21881562; DOI=10.1038/nature10390;
RA Alfoeldi J., Di Palma F., Grabherr M., Williams C., Kong L., Mauceli E.,
RA Russell P., Lowe C.B., Glor R.E., Jaffe J.D., Ray D.A., Boissinot S.,
RA Shedlock A.M., Botka C., Castoe T.A., Colbourne J.K., Fujita M.K.,
RA Moreno R.G., ten Hallers B.F., Haussler D., Heger A., Heiman D.,
RA Janes D.E., Johnson J., de Jong P.J., Koriabine M.Y., Lara M., Novick P.A.,
RA Organ C.L., Peach S.E., Poe S., Pollock D.D., de Queiroz K., Sanger T.,
RA Searle S., Smith J.D., Smith Z., Swofford R., Turner-Maier J., Wade J.,
RA Young S., Zadissa A., Edwards S.V., Glenn T.C., Schneider C.J., Losos J.B.,
RA Lander E.S., Breen M., Ponting C.P., Lindblad-Toh K.;
RT "The genome of the green anole lizard and a comparative analysis with birds
RT and mammals.";
RL Nature 477:587-591(2011).
CC -!- FUNCTION: Dual specificity phosphatase able to dephosphorylate
CC phosphotyrosine, phosphoserine and phosphothreonine residues within the
CC same substrate, with a preference for phosphotyrosine as a substrate
CC (By similarity). Involved in the modulation of AMPK and MAPK1/2
CC signaling pathways (By similarity). {ECO:0000250|UniProtKB:Q68J44,
CC ECO:0000250|UniProtKB:Q8BK84}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q68J44};
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 Evidence={ECO:0000250|UniProtKB:Q68J44};
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 Evidence={ECO:0000250|UniProtKB:Q68J44};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68J44}. Nucleus
CC {ECO:0000250|UniProtKB:Q8BK84}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AAWZ01006385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAWZ01006387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0C598; -.
DR SMR; P0C598; -.
DR STRING; 28377.ENSACAP00000008506; -.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; P0C598; -.
DR Proteomes; UP000001646; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020405; Atypical_DUSP_subfamA.
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 PANTHER; PTHR45682; PTHR45682; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01909; ADSPHPHTASEA.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome.
FT CHAIN 1..217
FT /note="Dual specificity phosphatase 29"
FT /id="PRO_0000295884"
FT DOMAIN 46..194
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 139
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT BINDING 138..145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q68J44"
SQ SEQUENCE 217 AA; 24410 MW; F5A23775C2FDC3AA CRC64;
MSSTALKSGK ISAYAAVKVD PDGDYCTPGA FDLERLFWKG SPKYTHVNEV WPNLYIGDEK
TALDRYSLEK AGFTHILNAA HGRWNVDTGP EYYSDMNIEY HGVEADDLPT FNLSPFFYSA
AEFIHTALQN ETSKILVHCA MGRSRSAALV LAYLMIYKNM TVVDAIDQVL QHRCILPNRG
FLKQLRELDI KLALERRDNM NGTNSSEKTG TSTETEI
