ID A0A1S3RTV4_SALSA Unreviewed; 642 AA.
AC A0A1S3RTV4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=LOC106604772 {ECO:0000313|RefSeq:XP_014055267.1};
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_014055267.1};
RN [1] {ECO:0000313|RefSeq:XP_014055267.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014055267.1};
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_014055267.1; XM_014199792.1.
DR AlphaFoldDB; A0A1S3RTV4; -.
DR STRING; 8030.ENSSSAP00000113676; -.
DR PaxDb; 8030-ENSSSAP00000113676; -.
DR GeneID; 106604772; -.
DR KEGG; sasa:106604772; -.
DR OMA; QYWKETH; -.
DR OrthoDB; 5490735at2759; -.
DR Proteomes; UP000087266; Chromosome ssa05.
DR Bgee; ENSSSAG00000079175; Expressed in actinopterygian pyloric caecum and 13 other cell types or tissues.
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 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; 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:UP000087266}.
FT DOMAIN 242..297
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 301..442
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 366..421
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..501
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..538
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 72675 MW; C7EED87CCD283DD8 CRC64;
MALLTLHRSP SISTAPDESI PRRGRLQKRE SFALVKGAVL LLEEGEGEGP HEETSPNHSP
SPLKLGGGAS DTQHRQLHAM VSLLRPEDTI KLAVRLESVS PVRVRYLIIV STFSNKQESI
LLGMDFPDTD RCLCTIGLVV PVWSDTQVYL DGDGGFSVTS AEKTRIFKPV SIQTMWSVLQ
ALHGCCERAV KGAVIPGCGL DWAQYYYGHV ESDRLCLNEW GAMTGLESVR RDSAGQSSTE
RVSVERQIKE ELRDIMRTED LENITSKQVR SALETRIGMD MKNYKEYIDN EMMVTMAQMD
KPSKIFDYLF LGSEWNAANF EELQKNNVGY ILNVTREIDN FFPESFSYMN IRVYDVEATD
LLSHWKDTYT FINTARQSGQ AVLVHCKMGV SRSGSTVVAY AMKQQRWPLE VALSYVRERR
PIVQPNDGFM KQLHTYSGIL NASQQRHSAL WRWKSRAEKE QRKIERAQSA ASHSNEEEEE
EEEEEEESEE EEELESPDEV DEADIEMKLF EEPVHKSETD PEAPPTEPAA PPTEPSVPNP
FITVQVASHS PSRSGRMNLF SLMQSINELE DEDLRNEQIA NSHRRSPGQR RRSYRRKGLM
HQRAHVDVSP EPSRLSGLRK LEGAGPSKLE TGEGDAKTTE VR
//