ID L9KM31_TUPCH Unreviewed; 1024 AA.
AC L9KM31;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=TREES_T100018652 {ECO:0000313|EMBL:ELW63818.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW63818.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
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:0000256|ARBA:ARBA00001482};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000256|ARBA:ARBA00009580}.
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DR EMBL; KB320760; ELW63818.1; -; Genomic_DNA.
DR AlphaFoldDB; L9KM31; -.
DR STRING; 246437.L9KM31; -.
DR eggNOG; KOG1716; Eukaryota.
DR InParanoid; L9KM31; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin 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 GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:InterPro.
DR CDD; cd14570; DSP_slingshot_1; 1.
DR CDD; cd11652; SSH-N; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR027233; DSP_SSH1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR043587; Phosphatase_SSH-like.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR043588; SSH-N.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45864:SF5; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 1; 1.
DR PANTHER; PTHR45864; SLINGSHOT PROTEIN PHOSPHATASE HOMOLOG; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF109715; DEK C-terminal domain; 1.
DR PROSITE; PS51998; DEK_C; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518}.
FT DOMAIN 342..397
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 401..542
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 463..520
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 549..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 112922 MW; DDF6D875D94E260F CRC64;
MGTHIPSGQL APLTGTHIPS GQLAPVMGTH VLSDQLSLVM GTHIPSGQLA PVMGMHMPSI
LRKLLDLDQG LSRVEAGSDE ERKGNLREWT AGAPCDVNMA AMNLMYLSDF CIFLRPTRSF
HCSEVSSPDY LSESFFMVKG AALFLQQGSS PQGQRSLQHP HKHAGDLPQH LQVMINLLRC
EDRIKLAVRL ESAWTDRVRY MVVVYSSGRQ DTEENILLGV DFSNKESQSC TIGMVLRLWS
DTKIHLDGDG GFSVSTAGRM HIFKPVSVQA MWSALQVLHK ACEVARRHNY FPGGVALIWA
TYYESCISSE QSCINEWNAM QDLESTRPDS PALFVDKPTE GERTERLIKA KLRSIMMSQD
LENVTSKEIR NELEKQMNCN LKEFKEFIDN EMLLILGQMD KPSLIFDHLY LGSEWNASNL
EELQGSGVDY ILNVTREIDN FFPGLFAYHN IRVYDEETTD LLAHWNEAYH FINKAKRNHS
KCLVHCKMGV SRSASTVIAY AMKEFGWPLE KAYNYVKQKR SITRPNAGFM RQLSEYEGIL
DASKQRHNKL WRQQTQSSLQ QPGEDPAGPS DFLPDTLDST PETQLPCLDD ATQPGFPGSK
APGGPALPCC FRRLSDPLLH SPDEDTSSSV QLDELERDAL LEDAPPAEAH TPDRQPPESS
GLCEKEVKKK LEFGSPKARG SFLAQEEEME RETGSGAGRW GRPPAQLNRE NLNNNNSKRS
CPDDFERPFL PHVTSPPVAY ASSSVFALLQ DDAIFGILNK VKPSYQSCAG CVYPTAGGAP
EAFRERCEDP RAPAICTQPA FLPHVTSSPV AYASSRSRAL EKPACGPAES PPFLPDAAPG
VHHPAAEGRP GPQAHQRAGE AAEHAGGLGL ALQGQPSRPD HTSNFSKDFL KTICYTPTSS
SMSSNLTRSS SSDSIHSVRG KPGLVKQRTQ EIETRLRLAG LTVSSPLKRS HSLAKLGSLN
FSTEDLSSEA DVSTVTDSQD AKLSESSFLH EPQATPRNHL SATSKPSGKS APENLKNPSW
MNKS
//
