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Database: UniProt
Entry: A0A3Q3LYN1_9TELE
LinkDB: A0A3Q3LYN1_9TELE
Original site: A0A3Q3LYN1_9TELE 
ID   A0A3Q3LYN1_9TELE        Unreviewed;       565 AA.
AC   A0A3Q3LYN1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000019688.2, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000019688.2}
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|ARBA:ARBA00001490};
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class 2 subfamily. {ECO:0000256|ARBA:ARBA00010750}.
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DR   AlphaFoldDB; A0A3Q3LYN1; -.
DR   STRING; 205130.ENSMAMP00000019688; -.
DR   Ensembl; ENSMAMT00000020211.2; ENSMAMP00000019688.2; ENSMAMG00000013236.2.
DR   GeneTree; ENSGT00940000153876; -.
DR   Proteomes; UP000261640; 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   CDD; cd14544; PTPc-N11_6; 1.
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; PTHR46559:SF2; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   PANTHER; PTHR46559; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11; 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   Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191}.
FT   DOMAIN          6..102
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          112..215
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          246..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          532..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..565
FT                   /note="Polar 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   565 AA;  65527 MW;  6C816E997435DAE9 CRC64;
     KLYHGWFHPN ITGIEAEQLL LTRGVHGSFL ARPSKSNPGD FTLSVRRNDE VTHIKIQNSG
     DYYDLYGGEK FATLAELVQY YTEQQDLLRE RNGHVIELKY PLNCKDPTSE RWYHGHLSGR
     DAEKLLTEKG KAGSFLVRES QSKPGDFVLS VLTNEEKHEN VDRKTKVTHV MIRYQGKYDV
     GGGERFDTLA DLVDHYKKNP MVEKSGIVVH LKQPFNATRI NAANIENRVR ELNKVADNSE
     KPKQGFWEEF EVLQQQECKL LYPRKEGQKP ENKSKNRYKN ILPFDTTRVE IRESDPDVSG
     SDYINANYIR VSVLKGRHVE EGKVFIATQG CLQNTVIDFW KMVYQENTHV IVMTTKEMER
     GRNKCVCYWP DLHATKEFGK VLVRNIDERP AQDYILRKLE VTRLDRKEPV RHIWHYQYLS
     WPDHGVPNEP GGVLWFLEEV NRTQSTIPDT GPIVVHCSAG IGRTGTIIVI DILIDIINRQ
     GLDCDIDIPK TIQRVRQQRS GMVQTEAQYK FIYMAVQQYI DTAQKRLEEE QRNKMKEREY
     SNIKYPQMTN SRSKTNMTSS RSSSV
//
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