ID A0A3Q2WCJ6_HAPBU Unreviewed; 1286 AA.
AC A0A3Q2WCJ6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-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};
GN Name=SSH2 {ECO:0000313|Ensembl:ENSHBUP00000022916.1};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000022916.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000022916.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_005939651.1; XM_005939589.2.
DR STRING; 8153.ENSHBUP00000022916; -.
DR Ensembl; ENSHBUT00000012419.1; ENSHBUP00000022916.1; ENSHBUG00000003458.1.
DR GeneID; 102297746; -.
DR CTD; 325085; -.
DR GeneTree; ENSGT00940000157430; -.
DR OMA; SDCADPR; -.
DR OrthoDB; 5490735at2759; -.
DR Proteomes; UP000264840; 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; cd14569; DSP_slingshot_2; 1.
DR CDD; cd11652; SSH-N; 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:SF3; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 2; 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 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:UP000264840}.
FT DOMAIN 250..305
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 309..450
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 371..428
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1286 AA; 142269 MW; 65B03A24C87CCC5E CRC64;
MALVTVQRSP TPSTTSSPCV SESGSGEDDR RFHLRSISES FLTVKGAALF LPRGNSPTQN
SAPRISQRRN KHTGDLQKHL QTMFTVLRPE DTIRLAVRLE SAYPQVTRYM VVVSTNGRQD
TEESIVLGMD FVSSDSCCTV GLVLPLWSDT MIHLDGDGGF SVSTVNRVHV FKPVSVQAMW
SALQSLHKAC EVARCHNYYP GSLFLTWVSY YQSRVSSSQL CINEWNAMQD VESHRANSPV
LFTDLPTERE RTERLIKTRL REIMMQKDLE NVTSKEIRTE LEIQMVCNLR EFKEFIDNEM
IVILGQMDSP TEIFDHVFLG SEWNASNLEE LQNSGVRYIL NVTREIDNFF PGMFEYHNIR
VYDEEATNLL EYWNDTYKFI TKAKKAGAKC LVHCKMGVSR SASTVIAYAM KEYGWNLDTA
FDYVKERRAV TKPNPSFMKQ LEEYQGILLA SKQRHNKLWR SHSDSDLSDR LDSKPSSPSL
NRADSHNNNT SSPSVHHFLG VAVLQALCPE PEDSHALSNG MCDSLVQEVR SDCADPRLLP
LPRPRAATVV PEETQGSSAS VAITVPVALP LPPPSLHILP PTPELQRAHR DTPTHLSCSV
GKPEELFLIL PDRSSSEEVS PLTLGSTDSD MINQSLSDLT NNSHTPLSPA TPTSSPPVLA
FAPSDDNNNN PSELDTRGEA DGSSTHSTDS IDFFSAREKF LGLAKDGRHR TLSEQAQQRS
SLSTDRETEV SEDEEEQRNE MSQESDDSSD KTSPDRIHHT HHDNGISVRH IVTEIEAISH
PAASLQTPSS SSSSPLPPSS HSPQVIRPEH QEEGESSEVT HTSSTPPSHP QPPTTLLCDW
PAGSVRRATK QLEQKLKQEL EMVACQRSPL HSPSSEQPPV RLSVSSEHVL LHSPMHAAEQ
RITQGENMAV SANATSKDEE KHTGSHKRPD FSGTSDLQDL SCSPKSDISQ VSGAIPVSVH
TSTDSHTVTS SLASAEQLSA SSQDTSAQSL RRGQLHSQNL QDCSNLMTLD GVTLQESDTD
ESSRVRQEGC GPVCAAQKRL ARGSQELEKI QQTLRELQAF LHEGITLETA DSRAQELGQP
QGPRDAMDTD PESYKGVSFE ESPPALKVGQ QLLERQEQRS LLEPTEWHRA TELEARIRQA
GLTPPSLMKR SASLAKLDCL ELSAHDLSSL DLRTHNRATL SHSPDSPSSP QSHPDDTWKK
QKVLAQRPCS ERTGSCSDDT SPPPLGLSPS TRGERGEREE SENSSSSNST VPASRQPGRG
HSSRRSRKAS AEKKQQRAVT LLYNTM
//
