ID A0A3B3Z0C6_9TELE Unreviewed; 1023 AA.
AC A0A3B3Z0C6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000032989.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000032989.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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_014843217.1; XM_014987731.1.
DR RefSeq; XP_014843224.1; XM_014987738.1.
DR AlphaFoldDB; A0A3B3Z0C6; -.
DR Ensembl; ENSPMET00000034151.1; ENSPMEP00000032989.1; ENSPMEG00000021249.1.
DR GeneID; 106918172; -.
DR CTD; 101885659; -.
DR OrthoDB; 5490735at2759; -.
DR Proteomes; UP000261480; 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; 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}.
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 574..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1023 AA; 112978 MW; DD03F8626C5FE0B2 CRC64;
MHLVVEPFQE AVMKMLPYFV ENAVLTQNEI NRILSESFFM VKGAALFLQQ GSSQQGQKAH
PPHKHAGELP QHLQVMINIL RSEDRIKLAV RLESAWSDRV RYMVVVYTSG RQDTEENILL
GIDFTNKDCK SCSIGMVLPL WSDTKIHLDG DGGFTVNTAG RTHVFKPVSV QAMWSALQVL
HKACEVSRRF NYFPGGMALT WMGYYESCIA SEQSCINEWN AMKDLETTRP DSPIMFVDKP
SERERTECLI KSKLRSIMTS QDLENVTCKQ IRTELEQHMN CNLKEYKEFI DNEMLLILGQ
MDKATLIFDH VYLGSEWNAS NLEELQETGV GYILNVTREI DNFFPGTFCY HNIRVYDEDA
TDLLAHWNDT YNFIMKAKKN DSKCLVHCKM GVSRSASTVI AYAMKEYGWS LEKAYNFVKQ
KRNITRPNAG FMRQLAEYEG ILDASKQRHN KLWHPDADCE MTEGQQGLAQ FCGGEDGGDP
TADPGMSPCC EEGSSNKGAA CSSPCRTVAL DIDPAYNNYY FRRLSDSALD SEPSTPVRGP
PLLGMEKVFI EIEDVERDAL LDDEAFHGRE GLPLPHFGPT AEGTAAQTCS RGPEPLEELR
LRLEFSTVEE ENEEDVQKEE AEMEVLMQPD DRGGGEGDGG ETQDVEVEGD AEGIGMDLAS
LNDNSNNNNH LSLLQNHKDT SSSFLLQRDA SLVSGSHQKE RSSSPSSELR LTARPPSEVQ
SASSRRSQTS TEGVSSSTGL LSPCGPQCDC ANCATSATAL PSSEAQRSAE AQDGSHLLQD
GPSESASDVL PELMRADFEG ETPAVACYLG QQQESLLQLR RSGLVRRRAE RLERLSGMSL
QECQKSKMCP SHSEEKEEFS SFTGDFAKTS TPCQVRLEPL VVPLTNEALL GVVGSGLLTP
TSSPHGSTLT RSSSSDSLRS VRGKPGLVRQ RAQEIETRLR LAGLTVPSRL KRSNSLAKLG
SLNLSSDDLC SACSSDAGTL LLLSLSPEPD QGLEWNSPTA SSLSRPGKNL LTPERALPGE
PRS
//
