ID   PTN5_RAT                Reviewed;         369 AA.
AC   P35234;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 5;
DE            EC=3.1.3.48;
DE   AltName: Full=Neural-specific protein-tyrosine phosphatase;
DE   AltName: Full=Striatum-enriched protein-tyrosine phosphatase;
DE            Short=STEP;
GN   Name=Ptpn5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=1714595; DOI=10.1073/pnas.88.16.7242;
RA   Lombroso P.J., Murdoch G., Lerner M.;
RT   "Molecular characterization of a protein-tyrosine-phosphatase enriched in
RT   striatum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:7242-7246(1991).
CC   -!- FUNCTION: May regulate the activity of several effector molecules
CC       involved in synaptic plasticity and neuronal cell survival, including
CC       MAPKs, Src family kinases and NMDA receptors. {ECO:0000250}.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10044};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the central nervous system except in
CC       the cerebellum. Enriched within the striatum relative to other brain
CC       areas.
CC   -!- PTM: Phosphorylation at Ser-49 by PKA deactivates PTPN5.
CC       Phosphorylation at Thr-59 and Ser-72 by MAPKs stabilizes the
CC       phosphatase, dephosphorylation of these sites results in ubiquitin-
CC       mediated degradation of the active phosphatase (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000305}.
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DR   EMBL; S49400; AAB19491.1; -; mRNA.
DR   PIR; A41147; A41147.
DR   RefSeq; NP_062126.3; NM_019253.3.
DR   AlphaFoldDB; P35234; -.
DR   BMRB; P35234; -.
DR   SMR; P35234; -.
DR   BioGRID; 248266; 4.
DR   IntAct; P35234; 1.
DR   MINT; P35234; -.
DR   STRING; 10116.ENSRNOP00000018860; -.
DR   ChEMBL; CHEMBL2429710; -.
DR   iPTMnet; P35234; -.
DR   PhosphoSitePlus; P35234; -.
DR   PaxDb; 10116-ENSRNOP00000018860; -.
DR   DNASU; 29644; -.
DR   KEGG; rno:29644; -.
DR   UCSC; RGD:3448; rat.
DR   AGR; RGD:3448; -.
DR   CTD; 84867; -.
DR   RGD; 3448; Ptpn5.
DR   eggNOG; KOG0789; Eukaryota.
DR   InParanoid; P35234; -.
DR   OrthoDB; 2914248at2759; -.
DR   PhylomeDB; P35234; -.
DR   PRO; PR:P35234; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0043204; C:perikaryon; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:1990635; C:proximal dendrite; IDA:RGD.
DR   GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0035640; P:exploration behavior; IDA:RGD.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:RGD.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR   GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:RGD.
DR   GO; GO:0002092; P:positive regulation of receptor internalization; IMP:RGD.
DR   GO; GO:2001025; P:positive regulation of response to drug; IMP:RGD.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:RGD.
DR   GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR   GO; GO:0035902; P:response to immobilization stress; IDA:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd14613; PTPc-N5; 1.
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; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR008356; Tyr_Pase_KIM-con.
DR   PANTHER; PTHR46198; PROTEIN-TYROSINE-PHOSPHATASE; 1.
DR   PANTHER; PTHR46198:SF1; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 5; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR01778; KIMPTPASE.
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   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Phosphoprotein; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..369
FT                   /note="Tyrosine-protein phosphatase non-receptor type 5"
FT                   /id="PRO_0000094757"
FT   DOMAIN          104..359
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        300
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         300..306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         49
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P54829"
FT   MOD_RES         59
FT                   /note="Phosphothreonine; by MAPK"
FT                   /evidence="ECO:0000250|UniProtKB:P54829"
FT   MOD_RES         72
FT                   /note="Phosphoserine; by MAPK"
FT                   /evidence="ECO:0000250|UniProtKB:P54829"
SQ   SEQUENCE   369 AA;  42366 MW;  7CD8A77EE238C64B CRC64;
     MEEKVEDDFL DLDAVPETPV FDCVMDIKPE ADPTSLTVKS MGLQERRGSN VSLTLDMCTP
     GCNEEGFGYL VSPREESAHE YLLSASRVLR AEELHEKALD PFLLQAEFFE IPMNFVDPKE
     YDIPGLVRKN RYKTILPNPH SRVRLTSPDP EDPLSSYINA NYIRGYNGEE KVYIATQGPI
     VSTVVDFWRM VWQERTPIIV MITNIEEMNE KCTEYWPEEQ VVHDGVEITV QKVIHTEDYR
     LRLISLRRGT EERGLKHYWF TSWPDQKTPD RAPPLLHLVR EVEEAAQQEG PHCSPIIVHC
     SAGIGRTGCF IATSICCQQL RREGVVDILK TTCQLRQDRG GMIQTCEQYQ FVHHAMSLYE
     KQLSLQSSE
//