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Database: UniProt
Entry: H3BXM3_TETNG
LinkDB: H3BXM3_TETNG
Original site: H3BXM3_TETNG 
ID   H3BXM3_TETNG            Unreviewed;      1172 AA.
AC   H3BXM3;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type {ECO:0000256|PIRNR:PIRNR000934};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000934};
GN   Name=PTPN14 {ECO:0000313|Ensembl:ENSTNIP00000000736.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000000736.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000000736.1}
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:PIRNR000934};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000934}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649,
CC       ECO:0000256|PIRNR:PIRNR000934}.
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DR   AlphaFoldDB; H3BXM3; -.
DR   Ensembl; ENSTNIT00000002579.1; ENSTNIP00000000736.1; ENSTNIG00000016380.1.
DR   GeneTree; ENSGT00940000156874; -.
DR   HOGENOM; CLU_006456_1_0_1; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13188; FERM_C_PTPN14_PTPN21; 1.
DR   CDD; cd17191; FERM_F1_PTPN14; 1.
DR   CDD; cd14599; PTPc-N14; 1.
DR   Gene3D; 1.20.80.10; -; 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; 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; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR014392; PTP_non-rcpt_14/21.
DR   InterPro; IPR041782; PTPN14/21_FERM_C.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR45706:SF6; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 14; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000934; Tyr-Ptase_nr14; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00295; B41; 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; 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; 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:PIRNR000934};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|PIRNR:PIRNR000934}; Hydrolase {ECO:0000256|PIRNR:PIRNR000934};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000934};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007303}.
FT   DOMAIN          23..310
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          894..1165
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1075..1156
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          498..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1106
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000934-1"
SQ   SEQUENCE   1172 AA;  133584 MW;  F172F0C94F38FF78 CRC64;
     RDMPFRLKLR RTRRYNVLSK NYFVTRIRLL DGNVIECTLS VESTGQECLE AVAQRLELRE
     THYFGLWFNG KTQAPAHRWV ELEKPLKKQL DKFGNEPLLF FGVMFYVPNV SQLEQEATRY
     QYYLQVKKEV LDGRLHCAVE QGIRLAGLAV QADFGDFTQF MSQDFLREYV LFPVNWPTGD
     EVLEEWTKKV AEEHKSHCRM QAAEAELLYI KEVEKLDGFG QETFPAKDNY TNDIFIGVSF
     IGVFVKHRNG RSIMLHKWKD IGTVAHNKSA ITVEITSRDD TIIFHMEDME MAKYIARLFT
     TRHKFYKQNK ICAEPTHSPA PIRRRPTWTH RISLPRPQSC NFQSMHSQYG EHYQDTQSSQ
     DSIFHDDPYY KSETSLDRCP VDFPFRNGTV PNGSMYSSPS LSSLNHSQTF VPPSPMSSNL
     SIPGSELMRP DYIPSHRHSA IIAPSYRPTP EYDAVMRQKR RMLPAHHDLH SQSLRSLNIS
     NSCAYRQPEA LVYSQPEMRD RGPYHGHGPS PGQYTPQVQI SYSKPVSHGP HQHTVSTPEL
     ANNKQQGANL GNYAATANML RNHMSRPPPP YPSSHFRPAT STPDLASHRH RCISGSSPEL
     VTRMVQLSVK TFQPDSSAVV HQSLQEVSEP LTVAAKHRST LGKRHSMEVI SSMRGGGGGV
     EGLMMKSING PLHRRNTLRE HVMRTQAQSI PQPQTSPPGP SGPYQHQKTL SNATMLIHSS
     ESEEEDEEEE ERPELDVQIP GLNEDISISA QLQAALAKLP NKPPPDYPGP PKPQNNAQIR
     THIHSHKHAH HLNHGHVLGP SISEPDLTSV KERVRKEPVK ERPVSEMFSL EDSIVEREIA
     QRVRYSLKRP LMMAALNGLY VARMPVPESP AEDGTKATDE RCKTLELKLE EERVFTEYER
     VPKKSVDCVL TTATLPENVE RNRFRDVVPY EENRVELVPN KENNTGYINA SHIKVMIRGE
     EWHYIATQGP LANTCADFWQ MVWEQGVNVI AMVTAEEEGG RSKSHRYWPK LGSKHNSATH
     GKFKVTTKFR TDSGCYATTG LKVKHLLSGQ ERTVWHLQYT DWPEQGCPEY VQGFLSYLEE
     IQSVRRHTNS MLDTSKSLNP PVVVHCSAGV GRTGVVILTE LMISCLEHNE PVEVPTMLSE
     LRQQRMLMVQ TISQYKFVYQ VLIQFLKNSR LI
//
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