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Database: UniProt
Entry: Q92124_XENLA
LinkDB: Q92124_XENLA
Original site: Q92124_XENLA 
ID   Q92124_XENLA            Unreviewed;       595 AA.
AC   Q92124;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type {ECO:0000256|PIRNR:PIRNR000929};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000929};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAA65731.1};
RN   [1] {ECO:0000313|EMBL:AAA65731.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Oocyte {ECO:0000313|EMBL:AAA65731.1};
RA   Freeman R.M.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAA65731.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Oocyte {ECO:0000313|EMBL:AAA65731.1};
RX   PubMed=7859288; DOI=10.1016/0092-8674(95)90498-0;
RA   Tang T.L., Freeman RM J.r., O'Reilly A.M., Neel B.G., Sokol S.Y.;
RT   "The SH2-containing protein-tyrosine phosphatase SH-PTP2 is required
RT   upstream of MAP kinase for early Xenopus development.";
RL   Cell 80:473-483(1995).
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   EMBL; U15287; AAA65731.1; -; mRNA.
DR   PIR; A55651; A55651.
DR   AlphaFoldDB; Q92124; -.
DR   STRING; 8355.Q92124; -.
DR   PaxDb; 8355-Q92124; -.
DR   OMA; VIFQQNT; -.
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; cd14605; PTPc-N11; 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; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11; 1.
DR   PANTHER; PTHR46559:SF1; 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   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR000929};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000929, ECO:0000313|EMBL:AAA65731.1};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000929};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999}.
FT   DOMAIN          6..102
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          112..216
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          247..521
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          436..512
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   ACT_SITE        459
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000929-1"
FT   BINDING         425
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
FT   BINDING         506
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000929-2"
SQ   SEQUENCE   595 AA;  68249 MW;  4F39FCF1E8F8D726 CRC64;
     MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA VTHIKIQNTG
     DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY PLNCADPTSE RWFHGHLSGK
     EAEKLLTEKG KHGSFLVRES QSHPGDFVLS VRTGDDKTES NDGKSKVTHV MIRCQDIKYD
     VGGGEKFDSL TDLVEHYKKN PMVETLGTVL QLKQPLNTTR INAAEIEIRV KELSKPAETA
     DKFKQGFWEE FETLQQQECK LLYSRKEGQR PENKNKNRYK NILPFDHTRV ELHDGDPNEQ
     VSDYINANII MPEFEIKCIN PKPKKRYIAT QGCLQNTVND FWRMVFQENS RVIVMTTKEV
     ERGKSKCVKY WPDEFALKEY GVMRVRNVKE TPAHDYILRE LKLSKVGQGN TERAVWQYHF
     KTWPDHGVPA DPGGVLDFLE EVHHKQDGIT DAGPVVVHCS AGIGRTGTFI VIDILIDVIR
     EKGVDCDIDV PKTIQMVRSQ RSGMVQTEAQ YRFIYMAVQH YIETLQRRIE EEQKSKRKGH
     EYTNIKYSLS EQGDQSPLPP CTPTPLPTPT LPEMREDAGR VYENVGLLQQ QKSFR
//
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