PTN5_RAT
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 03-AUG-2022, entry version 144.
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; P35234; -.
DR PRIDE; P35234; -.
DR DNASU; 29644; -.
DR GeneID; 29644; -.
DR KEGG; rno:29644; -.
DR UCSC; RGD:3448; rat.
DR CTD; 84867; -.
DR RGD; 3448; Ptpn5.
DR eggNOG; KOG0789; Eukaryota.
DR InParanoid; P35234; -.
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; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
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:0035254; F:glutamate receptor binding; IPI:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:RGD.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0035640; P:exploration behavior; IDA:RGD.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:RGD.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:RGD.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; 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:0006470; P:protein dephosphorylation; ISO:RGD.
DR GO; GO:1903492; P:response to acetylsalicylate; IEP: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 Gene3D; 3.90.190.10; -; 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; PTHR46198; 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; SSF52799; 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
