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Database: UniProt
Entry: A0A1S3PEY9_SALSA
LinkDB: A0A1S3PEY9_SALSA
Original site: A0A1S3PEY9_SALSA 
ID   A0A1S3PEY9_SALSA        Unreviewed;      1047 AA.
AC   A0A1S3PEY9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=LOC106584991 {ECO:0000313|RefSeq:XP_014026181.1,
GN   ECO:0000313|RefSeq:XP_014026182.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014026182.1};
RN   [1] {ECO:0000313|RefSeq:XP_014026181.1, ECO:0000313|RefSeq:XP_014026182.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014026181.1,
RC   ECO:0000313|RefSeq:XP_014026182.1};
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_014026181.1; XM_014170706.1.
DR   RefSeq; XP_014026182.1; XM_014170707.1.
DR   GeneID; 106584991; -.
DR   CTD; 101885659; -.
DR   OrthoDB; 5490735at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa24.
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; 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; 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:UP000087266}.
FT   DOMAIN          244..299
FT                   /note="DEK-C"
FT                   /evidence="ECO:0000259|PROSITE:PS51998"
FT   DOMAIN          303..444
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50054"
FT   DOMAIN          365..422
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          680..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          852..878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          919..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1015..1047
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        920..944
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1017..1031
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1047 AA;  115688 MW;  5A75F99B86921062 CRC64;
     MHLVVESPQE AVLKMLPYFV ENAVLTQSER CCILSESFFM VKGAALFLQQ GSSPQDQKAH
     PHHKHAGDLP QHLQVMINIL RSEDRIKLAV RLESAWSDRV RYMVVVYTSG RQDTEENILL
     GIDFSDKDSK SCSVGMVLPL WSDTKIHLDG DGGFSVNTVS RNHVFKPVSV QAMWSALQIL
     HKVCEVSRRY NYFPGGMALT WMGYYESCIA SEQSCINEWN AMRDLETLRP DSPTMFVDKP
     TERERTECLI KAKLRSIMMF QDLENVTSKQ IRTELEQHMS CNLMQYKEFI DNEMLLILGQ
     MDKATLIFEH LYLGSEWNAS NLEELQDTGV GYILNVTREI DNFFPGTFSY HNIRVYDEED
     TDLLAHWNET YNFIVKAKKN HSKCLVHCKM GVSRSASTVI AYAMKEYGWS LEKAFNFVKQ
     KRSITRPNTG FMRQLAEYEG ILDASKQRHN KLWRPDRPDP DCDLHEGQQA QCCGGEDPGN
     RTPEPGMSPC YEEKGAACPL SPCRMISLEV DPAYNNYYFR RLSDSALDSD PSTPVRALPL
     LDMERVFIEI EDVERDALLD DEAFEGREGL PLPHFGLAGV GAAAQTSCRG PEPLEELRLR
     LEFSTVEEED EEEVQKDEAE MEALAHPGGR LGSAGGGDGE GEVEMVQEEE VEKEGNGLDL
     VTLNQNSNNN NHFNTLSRLN DTVPSKPAHP VKPSALSRSD NKPSHNIDSL TQDADLCLNP
     THLPSVPSVS VEVPSATLPL PLTSPDTPCS LSLLHPCGPL CDCAAPPSTP LPEAQDSPCS
     LTSEDMAGEA EGEEGKLLGV SEPLPVPELL GLSLEEKRPA VACYVTQQQE TLVQLQRSGL
     VRRRAERLER LSGLSQEGLH PLEPLDSPHS GAREGPSPVE VEFSAFPEDF PKSSTPCPVS
     LELLVVPLTN EALLGAVGSG GLTPNSSPHG STLTRSSSSD SIRSVRGKPG LVRQRAQEIE
     TRMRLAGLTV PSSLKRSNSL AKLGSLNFSA EDLCSVCSSD AGTLLLLSLS PEPGLEWECP
     STSSSAQPRA HRDQTTPERA LSGGPRS
//
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