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Database: UniProt
Entry: G3NHN6_GASAC
LinkDB: G3NHN6_GASAC
Original site: G3NHN6_GASAC 
ID   G3NHN6_GASAC            Unreviewed;       388 AA.
AC   G3NHN6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type {ECO:0000256|PIRNR:PIRNR000926};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000926};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000004845.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000004845.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000004845.1}
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:PIRNR000926};
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class 1 subfamily. {ECO:0000256|ARBA:ARBA00009701,
CC       ECO:0000256|PIRNR:PIRNR000926}.
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DR   AlphaFoldDB; G3NHN6; -.
DR   STRING; 69293.ENSGACP00000004845; -.
DR   Ensembl; ENSGACT00000004859.1; ENSGACP00000004845.1; ENSGACG00000003692.1.
DR   eggNOG; KOG0789; Eukaryota.
DR   GeneTree; ENSGT00940000154686; -.
DR   InParanoid; G3NHN6; -.
DR   OMA; QFCWKTI; -.
DR   TreeFam; TF315897; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000003692; Expressed in testis and 13 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR012265; Ptpn1/Ptpn2.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46047:SF1; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 2; 1.
DR   PANTHER; PTHR46047; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 61F; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000926; Tyr-Ptase_nr1; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000926};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000926};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        362..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..275
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          187..266
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          280..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..304
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        213
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000926-1"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000926-2"
FT   BINDING         213..219
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000926-2"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000926-2"
SQ   SEQUENCE   388 AA;  44066 MW;  B8710F69A6C2696E CRC64;
     MEEEFEDIDS SGGWQNLFNE IRNQASEFPY KVAKLPANRN LNRYRDVSPY DHSRVKLENS
     ENDYINASSV MVKEAQRAYI LCQGPLRNTC GHFWLMIWEQ CSKAIIMLNR VIEKGSEKCA
     QYWPTSEELQ MSFTDTGFVV RLLSEEDRSY YTIRVLQLQN TVMGESREIY HFHYTTWPDF
     GVPESPASFL NFLFKVRESG SLGPEHGPSV VHCSAGIGRS GTFALVDTCL VLMARRKNQS
     SVSIQKVLLD MREYRMGLIQ TPDQLRFSYM AVIEGVKLIP TSPTNSTPTA PQRQHAQRSA
     RNPSGNAGRL RGAGRPAAGR GRGVGAFRVR KRQRGERIAC TSQKVQQMKQ RLSHSERKRD
     SWLYWKPILL NVGAGAAVAV GLLVCWIF
//
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