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Database: UniProt
Entry: A0A1S3W5Z6_ERIEU
LinkDB: A0A1S3W5Z6_ERIEU
Original site: A0A1S3W5Z6_ERIEU 
ID   A0A1S3W5Z6_ERIEU        Unreviewed;       650 AA.
AC   A0A1S3W5Z6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-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=SSH3 {ECO:0000313|RefSeq:XP_016041752.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016041752.1};
RN   [1] {ECO:0000313|RefSeq:XP_016041752.1}
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_016041752.1; XM_016186266.1.
DR   AlphaFoldDB; A0A1S3W5Z6; -.
DR   CTD; 54961; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   InParanoid; A0A1S3W5Z6; -.
DR   OrthoDB; 5490735at2759; -.
DR   Proteomes; UP000079721; 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:UP000079721}.
FT   DOMAIN          265..320
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   DOMAIN          324..465
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          389..444
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          43..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          615..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..502
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   650 AA;  71493 MW;  27575C150E94E8E5 CRC64;
     MALVTVSRSP PASGHATPVE RPDWAAKRRG RLQRRQSFAV LRGTVLGLQD SGDEGDVAEA
     GPEPAGAPLG EDQPPGAQLD SEPGEQKDEQ EQEQSRHLRL MVQLLRPQDD IRLAAQLEAA
     RPPRLRYLLV VSPSDSQDET VLLGVDFPDS RSPSCTLGLV LPLWSDTQVY LDGDGGFSVT
     SGGQSRIFKP ISIQTMWATL QVLHQACEAA LGSGLVPGGS ALTWAGHYQD QLSSNRSCLN
     EWTAMADLES LRPPSTEPGR PSEQEQMEEA IRAGLWEVLE VSDLDSVTSK EIRQALERRL
     GYPLQRSRDF IDNQMLLLMA QRDRASMIFP HLYLGSEWNA ANLEELQRNR VSHILNMARE
     IDNFFPERFI YHNVRVWDDE AAQLLPCWKE THRFVEAARA QGTRVLVHCK MGVSRSAATV
     VAYAMKQYGW SLEQAQRHVQ ERRPVVRPNP GFLRQLQTYQ GILTASRQSQ VWEQKVGAAS
     PEEPLAPEVS ALLPPPPPEP GDTGEAKAVE LEESQTAPQE EPGSRPRINL RGVMRSISLL
     EPPLELESDP EASNLPEVFS SEPSDGSPPQ TLPLPTQAKC GRQPRKGPWP ALKSRQSVVA
     LNSAALVASR TRAFREQEQG QGGAGGVSTS RLRKVVRQAG MEGGTEEGGA
//
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