ID A0A3B3S2S9_9TELE Unreviewed; 588 AA.
AC A0A3B3S2S9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type {ECO:0000256|PIRNR:PIRNR000929};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000929};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000025032.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000025032.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000256|ARBA:ARBA00001490,
CC ECO:0000256|PIRNR:PIRNR000929};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000929}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 2 subfamily. {ECO:0000256|ARBA:ARBA00010750,
CC ECO:0000256|PIRNR:PIRNR000929}.
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DR AlphaFoldDB; A0A3B3S2S9; -.
DR STRING; 1676925.ENSPKIP00000025032; -.
DR Ensembl; ENSPKIT00000005754.1; ENSPKIP00000025032.1; ENSPKIG00000008036.1.
DR GeneTree; ENSGT00940000159480; -.
DR OrthoDB; 2911650at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:UniProt.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR CDD; cd09931; SH2_C-SH2_SHP_like; 1.
DR CDD; cd10340; SH2_N-SH2_SHP_like; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
DR PANTHER; PTHR46257; TYROSINE-PROTEIN PHOSPHATASE CORKSCREW; 1.
DR PANTHER; PTHR46257:SF4; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 6; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000929; Tyr-Ptase_nr_6; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000929};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000929};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR000929};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}.
FT DOMAIN 4..100
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 110..211
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 249..519
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 434..510
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 538..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 457
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-1"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
FT BINDING 504
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
SQ SEQUENCE 588 AA; 66783 MW; CDD3253EB52C9F32 CRC64;
MVRWFHRNIS GLEAETLLKA RGVHGSFLAR PSKKNQGDFS LSVRVDDTVT HIRIQNTGDY
YDLYGGEKFA TLSELVDYYT TEHGVLQDKD GTLIELKYPL NSSDPTTERW YHGHLSGPNA
EKLLVGRKEP GTFLVRESLS KPGDYVLSAL TDEFGPSGER RVSHIKIICQ NDKYTVGGSE
KFDSLSDLVE HYKRKGIEEL SGTWVFLKQP YYSTRVNVSD IENRVKVLDQ TAAGTENSGD
GDKKSKAGFW EEFDALQKHE AKVKKSRNEG MRPENKSKNR YKNILPFDET RVALHSRDPT
IVGSDYINSN YVKNKLCDTG NPKVYIATQG CLATTVNDFW QMVWQECSRV IVMTTREVEK
GRNKCVPYWP ELEGSKEVGP YLVTCLSERD ASDYKIRVLE ISPLDQSDVP RRIWHYQYLS
WPDHGVPQEP GGVLSFLTQV NAKQMEFHDA GPMIIHCSAG IGRTGTILVI DMLVDIIDAK
GMDCDIDISK AILMVREQRS GMVQTEAQYK FIYLAMLQYI ETTKTKLHAS KELETEYGNL
SLQPKHQKAS RKVSNNKEDV YENLGMKGKK DVKKQKSQEK KSGSVRKK
//
