ID A0A287DED4_ICTTR Unreviewed; 1416 AA.
AC A0A287DED4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=SSH2 {ECO:0000313|Ensembl:ENSSTOP00000031871.1};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000031871.1, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000031871.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AGTP01050970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01050979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSSTOT00000039777.1; ENSSTOP00000031871.1; ENSSTOG00000023134.2.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000157430; -.
DR Proteomes; UP000005215; 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; cd14569; DSP_slingshot_2; 1.
DR CDD; cd11652; SSH-N; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR014876; DEK_C.
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:SF3; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 2; 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 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:UP000005215}.
FT DOMAIN 248..303
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 307..448
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 372..426
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1210..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1416 AA; 158421 MW; 5FE7F3B692E00D01 CRC64;
MALVTVQRSP TPSTTSSPCA SEADSGEEEC RSQPRSISES FLTVKGAALF LPRGNGSSTP
RISHRRNKHA GDLQQHLQAM FILLRPEDNI RLAVRLESTY QNRTRYMVVV STNGRQDTEE
SIVLGMDFSS NDSSTCTMGL VLPLWSDTLI HLDGDGGFSV STDNRVHIFK PVSVQAMWSA
LQSLHKACEV ARMHNYYPGS LFLTWVSYYE SHINSDQSSV NEWNAMQDVQ SHRPDSPALF
TDIPTERERT ERLIKTKLRE IMMQKDLENI TSKEIRTELE MQMVCNLREF KEFIDNEMIV
ILGQMDSPTQ IFEHVFLGSE WNASNLEDLQ NRGVRYILNV TREIDNFFPG VFEYHNIRVY
DEEATDLLAY WNDTYKFISK AKKHGSKCLV HCKMGVSRSA STVIAYAMKE YGWNLDRAYD
YVKERRTVTK PNPSFMRQLE EYQGILLASK QRHNKLWRSH SDSDLSDHHE PICKPGLELN
KKEITTSADQ IAEVKTMESH PPIPPVFVEH VIPQDTNQKG LCTKERMICL EFTSREFHAG
QIEDELNLND INGCSSGCCL NESKFPLDNC HASKVLIQPG QATEIANKFP DLTVEDLETD
ALKADMNVHL LPMEELTSRL KDLPMSPDPE SPSSQPSSQA EISDFSTDRI DFFSALEKFV
ELSQETRSRS FSHSRMEELG GGRSESCRLS VIEVAPSEVT IDDQRSSSLS NTPHASEESS
VDEEQSKAIS ELVSPDIFMQ SHPENAISVK EIVTEIESIS QGVGQIQIKG DILSNPCHTP
KKSTIYELPL EKTQAPENKP EPLEQDEGFY TTQPELAKDS GKYNPESCLR THSSTADSED
EEPVEGEHEL WGPGMQSGAK WCSGSVRRAT LEFEERLRQE QEHHGTTPAC TSLSTRKNSK
NDSSMADLAP KGKNDESTPE HSFVPEEPEM NKGKGKGSGS EAGLLSHCEQ SVVIPALELS
DYHPLPAPRE CPGSDTRTKQ EGVPKEQRTV VSYQESETQA IPLPFPKRIE IIEYTHTVTS
LDHTGSGSEI ATSEGSGEQG LRNVKVEKSV TVLCALDENL NRTLDPNQVS LHPQVLPLPC
SSSPEHDRPT NPTSMKSTPE DRDSIPSTAL ETVAPFVSCT THIPSATLDY LHPHTVVHLE
GFTEQSSTTD SEPSTEQVSW EERQEDPLSR GYEVTHMGSQ FSSEDLSVIG KLSDSIGELQ
KKTDPSPVAC RFPHSSSSED IKNLSHSPNV VKERAKEIEL RVISQAGFTK PSQMRRSASL
AKLSYLDLCK DYLPESPHLK LLQPFIRTDS GMHAMEAQEL QKKPGAPQNP EPTKYFVEQL
KTTECIAQSK PVERPLVQYA KEFGYSQQCL LPRAGLELTS SEGGLPLLQT QGLQRAGPAL
GVAVATRQQH GRTHPLRRLK RANDKKRTTN PFYNTM
//
