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Database: UniProt
Entry: H0ZSS4_TAEGU
LinkDB: H0ZSS4_TAEGU
Original site: H0ZSS4_TAEGU 
ID   H0ZSS4_TAEGU            Unreviewed;       608 AA.
AC   H0ZSS4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type {ECO:0000256|PIRNR:PIRNR000929};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000929};
GN   Name=PTPN6 {ECO:0000313|Ensembl:ENSTGUP00000013670.2};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000013670.2, ECO:0000313|Proteomes:UP000007754};
RN   [1] {ECO:0000313|Ensembl:ENSTGUP00000013670.2, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA   Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA   Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA   Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA   McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA   Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA   Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA   Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA   Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA   Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA   Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000013670.2}
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         ECO:0000256|PIRNR:PIRNR000929};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000929}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class 2 subfamily. {ECO:0000256|ARBA:ARBA00010750,
CC       ECO:0000256|PIRNR:PIRNR000929}.
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DR   AlphaFoldDB; H0ZSS4; -.
DR   STRING; 59729.ENSTGUP00000031601; -.
DR   Ensembl; ENSTGUT00000013826.2; ENSTGUP00000013670.2; ENSTGUG00000013276.2.
DR   GeneTree; ENSGT00940000159480; -.
DR   HOGENOM; CLU_001645_9_10_1; -.
DR   OrthoDB; 2911650at2759; -.
DR   TreeFam; TF351632; -.
DR   Proteomes; UP000007754; Chromosome 1.
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; cd14606; PTPc-N6; 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; PTHR46257; TYROSINE-PROTEIN PHOSPHATASE CORKSCREW; 1.
DR   PANTHER; PTHR46257:SF4; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 6; 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   Cytoplasm {ECO:0000256|PIRNR:PIRNR000929};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR000929};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000929};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007754};
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..225
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          257..528
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          443..519
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          560..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..598
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        466
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000929-1"
FT   BINDING         432
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
FT   BINDING         513
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
SQ   SEQUENCE   608 AA;  68664 MW;  221D0DA2F579BFED CRC64;
     MPSRGWFHRD LSGLEAEALL KGRGVHGSFL ARPSRRNQGD FSLSVRVGDQ VTHIRIQNTG
     DFYDLYGGEK FATLSELVEY YTQQQGSLQD KDGTIIDLRY PLNCSDPTTE RWYHGHLSGP
     AAESLLQAKA TPWTFLVRES LSKPGDFVLS VLTDQPKPGS DAPAGATGAS GTRLKVTHIK
     IMCENGRYTV GGAEMFDSLT DLVEHFKKIG IEEMSGSFVY LKQPYYATRV NAADIENRVQ
     ELNKKTSLSE ETSKAGFWEE FDSLQKQEAK HLFDRHEGQR PENKSKNRYK NILPFDHSRV
     ILQGRDPNIP GSDYINANYV KNTLISPDEC TKTYIASQGC LDATVNDLWQ MVWQENTRII
     VMTTREVEKG RNKCVPYWPE LGSTKEYGPY LVQNTGEHDA LEYKLRHLCM CPKDNGNAVR
     EIWQYQYLSW PDHGVPSEPG GVLSFLDQIN QKQESIPNAG PIVVHCSAGI GRTGTIIVID
     MIVETISTKG LDCDIDIQKT IQMVRAQRSG MVQTEAQYKF IYMAICQFIE ATKKKLEVIQ
     SQKGKPNECE YGNIAYPPAA RNVHPKVSRK PSKQKEESTV YENLGKKEEK VRKQRSSEKK
     LKGSLKKK
//
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