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Database: UniProt
Entry: A0A3Q7TFJ9_VULVU
LinkDB: A0A3Q7TFJ9_VULVU
Original site: A0A3Q7TFJ9_VULVU 
ID   A0A3Q7TFJ9_VULVU        Unreviewed;       522 AA.
AC   A0A3Q7TFJ9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
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_025860092.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025860092.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025860092.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025860092.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025860092.1};
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_025860092.1; XM_026004307.1.
DR   AlphaFoldDB; A0A3Q7TFJ9; -.
DR   Proteomes; UP000286640; 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:UP000286640}.
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..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  58074 MW;  617E6B4B9D9D95BB CRC64;
     MALVTVSRSP PASGHSTPVG PTQGQASKRR SRLQRRQSFA VLRGAVLGLQ DGEDNGEAAE
     ASPEAVERPL GEKQPHGDQT DDGHGLQSPR KQEQSQHLHL MVELLRPQDD MRLAAQLEAA
     RPPRLRYLLV VSTREHLSQD ETVLLGVDFP DSSSSSCTLG LVLPLWSDTQ VYLDGDGGFS
     VTSGGQSRIF KPISIQTMWA TLQVLHQACE AALGSGLVPG GNALTWAAHY QEKLSSDQSC
     LNEWMAMADL ESLRPPSPGP GRPSEQEQME QAIRAELWEV LDTSDLESIT SKEIRQALEL
     RLGRPLQQYR DFIDNQMLLL MAQQDRASRI FPHLYLGSEW NAANLEELQR NRVSHILNMA
     REIDNFYPER FIYHNVRLWD EESAQLLPHW KETHRFVEAA RAQGTRVLVH CKMGVSRSAA
     TVIAYAMKQY GWSLEQALRH VQELRPIARP NPGFLRQLQT YQGILTARTR GQWGGEGCGS
     GGEPGSPERR AWATAPYQPP GGHEVHQPPG ASPRAGRHLR GQ
//
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