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Database: UniProt
Entry: A0A1U7Q4Z7_MESAU
LinkDB: A0A1U7Q4Z7_MESAU
Original site: A0A1U7Q4Z7_MESAU 
ID   A0A1U7Q4Z7_MESAU        Unreviewed;       651 AA.
AC   A0A1U7Q4Z7;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=Ssh3 {ECO:0000313|RefSeq:XP_005064123.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005064123.1};
RN   [1] {ECO:0000313|RefSeq:XP_005064123.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   RefSeq; XP_005064123.1; XM_005064066.3.
DR   AlphaFoldDB; A0A1U7Q4Z7; -.
DR   STRING; 10036.ENSMAUP00000017801; -.
DR   GeneID; 101826573; -.
DR   KEGG; maua:101826573; -.
DR   CTD; 54961; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   OrthoDB; 5490735at2759; -.
DR   Proteomes; UP000189706; Unplaced.
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; cd14571; DSP_slingshot_3; 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; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR45864:SF4; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 3; 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:UP000189706}.
FT   DOMAIN          267..322
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   DOMAIN          326..467
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          391..446
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          46..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..503
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..625
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..651
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   651 AA;  72316 MW;  EC54ED89FC5D3D4C CRC64;
     MALVTVNRSP PASGHSTPVE STQDRVVRRR SRLQRRQSFA VLRGAVLGLQ DGGDGDDAAE
     ADSEAVEDPL GEKQPPEDQT DNNGQEFQSP WKQVQRQHLH LMVELLRPQD DIRLAAQLEA
     ARPPRLRYLL VVSTGECLSQ ETILLGVDFP DSSSHSCTLG LVLPLWSDAQ VYLDGDGGFS
     VTSGGQSRIF KPVSIQTMWA TLQVLHQACE AALGSSLVPG GSALVWAMHY QEKLNSDQGC
     LNEWMAMSDL ESLRPPIAEP GQASEQEQME QAILAELWQV LDTSDLESVT SKEIRQALEL
     RLGCPLQQYR DFIDNQMLLL MAQQDRASRI FPHLYLGSEW NAANLEELQR NRVSHILNMA
     REIDNFFPER FTYHNVRVWD EESAQLLPHW KGTHRFIEHA RAQGTRVLVH CKMGVSRSAA
     TVLAYAMKQY GWSLEQALIH VQELRPIVRP NPGFLRQLQT YQGILTASRQ SHVWEQKVGV
     VSPEEPLAPE VSTPLPPLPP EPGGSGEVTV IGSEESQEVP KEELGLRPRI NLRGVMRSIS
     LLEPESTPEA GELPEVFSSH ESSDKEPLHP FPQRSAAKGG RRVHRGPWPA LKSRQSVVAL
     HSAALVASRT RAFQEQGQGQ EQGEAGMPST PRLRKVVRQA SVDDSREEGG A
//
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