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
//