ID A0A556UFM7_BAGYA Unreviewed; 849 AA.
AC A0A556UFM7;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Tyrosine-protein phosphatase {ECO:0000256|PIRNR:PIRNR000927};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000927};
GN ORFNames=Baya_10506 {ECO:0000313|EMBL:TSO88059.1};
OS Bagarius yarrelli (Goonch) (Bagrus yarrelli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Sisoridae; Sisorinae; Bagarius.
OX NCBI_TaxID=175774 {ECO:0000313|EMBL:TSO88059.1, ECO:0000313|Proteomes:UP000319801};
RN [1] {ECO:0000313|EMBL:TSO88059.1, ECO:0000313|Proteomes:UP000319801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JWS20170419001 {ECO:0000313|EMBL:TSO88059.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TSO88059.1};
RX PubMed=31274158;
RA Jiang W., Lv Y., Cheng L., Yang K., Chao B., Wang X., Li Y., Pan X.,
RA You X., Zhang Y., Yang J., Li J., Zhang X., Liu S., Sun C., Yang J.,
RA Shi Q.;
RT "Whole-Genome Sequencing of the Giant Devil Catfish, Bagarius yarrelli.";
RL Genome Biol. Evol. 11:2071-2077(2019).
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|PIRNR:PIRNR000927};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000927}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649,
CC ECO:0000256|PIRNR:PIRNR000927}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TSO88059.1}.
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DR EMBL; VCAZ01000071; TSO88059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A556UFM7; -.
DR Proteomes; UP000319801; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014847; FA.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR041783; PTPN3/4_FERM_C.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR45706:SF7; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 4; 1.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000927; Tyr-Ptase_nr3; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
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|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000927};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR000927}; Hydrolase {ECO:0000256|PIRNR:PIRNR000927};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR000927};
KW Receptor {ECO:0000313|EMBL:TSO88059.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000319801}.
FT DOMAIN 1..253
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 579..835
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 752..826
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 320..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 776
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-1"
FT BINDING 744
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT BINDING 776..782
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT BINDING 820
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
SQ SEQUENCE 849 AA; 96742 MW; 3FBA726CCEF81E6C CRC64;
MSSRFRLPAG RSYNVRASEL ARDRQHTEVL CNIVLLDNTV QPFKVNKHDH GQVLLDAVFK
HLELTERDYF GLHLADESSD SPRWLDPNKP IRKQLKPELG DYREEENSSS YLSEFSFIPN
QPQSFEKEVA KHHQQHSGLN PAQSELNYLN TARTLELYGV ELHYARDQSN TDIFMGVMSS
GIGVYKSRVR VNYFPWLKIV KITFKCKQFF IQLRKEANET RETILGFNMV NYRSCKNLWK
TCVEHHTFFR LDQPVPAQKN FFSHYFSLGS KFRYSGRTEA QSVQYGKEKG VKDRVFARSP
SKPLARKLIG VTDWEALSRN SVSQERLETR SLPTRSPPGT PNHRNSLFVQ EATRQRPSSM
GHLVEHVIHA SPSLPVFTNH KSASSTQANS ISLDFTLSPD GFEGPPPALP PKQSRKNLSQ
LILSRSQQEL NNHIDEMYDI PVATDKPTLN GVASHDNLVL IKMKPHDNGR FGFNVTADLC
VPRLNEGDQV VMINGHDVSE HTHDQVVMSI KSSCESHTGE LVLLVRPNAI YDVVEDKLET
EPDFQYIPAK SPSDPSELDQ DAWRDSMQQL RDGLSSGALL AQFDQLYRKR PGMTMSCAKL
PYNISKNRYR DISPYDATRV ILNGTDDYIN ANYINMEIPA SSIINRYIAC QGPLPNTCTD
FWQMTWEQGS SMVVMLTTQV ERGRVKCHQY WPNPSGSGTY DGFQVSCQTE EGNSAFLVRE
MTLTRTETEE SRELTQIQYL AWPDHGVPDD STDFLDFVAL VRSKRARKDE PVVVHCSAGI
GRTGVLITME TAMCLMECSQ PVYPLDIVRT MRDQRAMMIQ TPSQFKFVCE AILKVYEENL
AKSMLYKSD
//
