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Database: UniProt
Entry: I3J9N2_ORENI
LinkDB: I3J9N2_ORENI
Original site: I3J9N2_ORENI 
ID   I3J9N2_ORENI            Unreviewed;       895 AA.
AC   I3J9N2;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Tyrosine-protein phosphatase {ECO:0000256|PIRNR:PIRNR000927};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000927};
GN   Name=ptpn4 {ECO:0000313|Ensembl:ENSONIP00000005572.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005572.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Ensembl:ENSONIP00000005572.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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|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}.
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DR   AlphaFoldDB; I3J9N2; -.
DR   STRING; 8128.ENSONIP00000056818; -.
DR   Ensembl; ENSONIT00000005576.2; ENSONIP00000005572.2; ENSONIG00000004426.2.
DR   eggNOG; KOG0792; Eukaryota.
DR   GeneTree; ENSGT00940000157211; -.
DR   HOGENOM; CLU_001645_7_0_1; -.
DR   TreeFam; TF315900; -.
DR   Proteomes; UP000005207; Unplaced.
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; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01195; FA; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SMART; SM00228; PDZ; 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; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50106; PDZ; 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   Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT   DOMAIN          1..268
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          477..549
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          615..871
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          791..862
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          334..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        812
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-1"
FT   BINDING         780
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT   BINDING         812..818
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT   BINDING         856
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
SQ   SEQUENCE   895 AA;  101498 MW;  E1DF046E7AAF7D8E CRC64;
     MTKSDNGQVL LDAVFKHLEL TERDYFGLHL TDDSSDAPRW LDPNKPVRKQ LKRGSPHNLS
     FRVKFFVTDP NKLQEEYTRY QYFLQIKQDI LTGRLPCPHN TAALLASYAV QSELGDYSEA
     EHSPGYLSEY SFIPNPPQDF HKEVAKHHQQ HSGLSPAESE FNYLNTARTL ELYGVELHYA
     RDQSNTEILI GVMSAGIVVY KNRVRINYFP WLKIVKISFK CKQFFIQLRR EATESRETLL
     GFNMVNYRAC KNLWKACVEH HTFFRLERPI PPQKNFFAYY FTLGSKFRYC GRTEVQSVQY
     GKEKGIKDRV FARSPSKPLA RKLVSGTDWE SVSRNSLSDE RLETQSLPTR SPPGTPNQNS
     LFVQEGTRLR PSSVGHLVDH VIHASPSLPV FSSNHKSASS TQANSISLDS TPSPDGVDGQ
     PPALPPKQLS RKTLSQIIQA HSQQSLLDNH LNEMYDVPVN ADKTTLNGVV PHDNLVLIKM
     RPDEHGRFGF NVKGGADQKM PIIVSRVAPG TSADLCVPRL NEGDQVVLIN GRDISDHTHD
     QVVMFIKASC ESHSGELILL VRPNAIYDVV EEKVDPEPDF QYIPEKSPQD PAQLDQHALR
     DSMVTLKEGL SGGAILAQFD QLYRKRPGMT MLCAKLPQNV SKNRYRDISP YDATRVILKS
     TDDYINANYI NMEIPASSLI NRYIACQGPL PNTCPDFWQM TWEQGSSMVV MLTTQVERGR
     VKCHQYWPNP DNSATYGDFT ITCHNEEGNS AFLVREMTLT HTPSEQQREV TQIQYVAWPD
     HGVPDDSTDF LDFVALVRTK RAGQDQPMVV HCSAGIGRTG VLITMETALC LMECGQPVYP
     LEIVKTMRDQ RAMMIQTPSQ YRFVCEAILK VYEEDLFKPL KTALYQQREK AADEK
//
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