PTPRR_RAT
ID PTPRR_RAT Reviewed; 656 AA.
AC O08617; Q62695; Q63419;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase R;
DE Short=R-PTP-R;
DE EC=3.1.3.48;
DE AltName: Full=PC12-PTP1;
DE AltName: Full=Protein-tyrosine phosphatase PCPTP1;
DE AltName: Full=Tyrosine phosphatase CBPTP;
DE Flags: Precursor;
GN Name=Ptprr; Synonyms=Ptp;
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] (ISOFORMS 1; 3 AND 4), AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Cerebellum;
RX PubMed=7557444; DOI=10.1016/0378-1119(95)00306-q;
RA Shiozuka K., Watanabe Y., Ikeda T., Hashimoto S., Kawashima H.;
RT "Cloning and expression of PCPTP1 encoding protein tyrosine phosphatase.";
RL Gene 162:279-284(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Adrenal tumor;
RX PubMed=7814416; DOI=10.1074/jbc.270.1.49;
RA Sharma E., Lombroso P.J.;
RT "A neuronal protein tyrosine phosphatase induced by nerve growth factor.";
RL J. Biol. Chem. 270:49-53(1995).
CC -!- FUNCTION: Sequesters mitogen-activated protein kinases (MAPKs) such as
CC MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs
CC bind to a dephosphorylated kinase interacting motif, phosphorylation of
CC which by the protein kinase A complex releases the MAPKs for activation
CC and translocation into the nucleus (By similarity). {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 -!- SUBUNIT: Interacts with MAPKs. {ECO:0000250}.
CC -!- INTERACTION:
CC O08617; Q9WUD9: Src; NbExp=2; IntAct=EBI-8584374, EBI-7784541;
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000250}; Single-
CC pass type I membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=O08617-1; Sequence=Displayed;
CC Name=1;
CC IsoId=O08617-2; Sequence=VSP_005162;
CC Name=2;
CC IsoId=O08617-3; Sequence=VSP_005163;
CC Name=3;
CC IsoId=O08617-4; Sequence=VSP_005164;
CC -!- TISSUE SPECIFICITY: Widely expressed in the brain, most abundant in
CC cerebellum, midbrain, cerebral cortex and hippocampus. Also expressed
CC in heart and skeletal muscle. {ECO:0000269|PubMed:7557444,
CC ECO:0000269|PubMed:7814416}.
CC -!- INDUCTION: By nerve growth factor; isoform 2 is induced in adrenal
CC tumor cells 2 hours after exposure, levels are down-regulated 24 hours
CC after treatment. {ECO:0000269|PubMed:7814416}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 7 subfamily. {ECO:0000305}.
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DR EMBL; D64050; BAA19530.1; -; mRNA.
DR EMBL; D38292; BAA07414.1; -; mRNA.
DR EMBL; U14914; AAA64485.1; -; mRNA.
DR PIR; JC4263; JC4263.
DR RefSeq; NP_001106861.1; NM_001113390.1.
DR RefSeq; NP_446046.2; NM_053594.2.
DR AlphaFoldDB; O08617; -.
DR SMR; O08617; -.
DR BioGRID; 250182; 1.
DR IntAct; O08617; 1.
DR MINT; O08617; -.
DR STRING; 10116.ENSRNOP00000006401; -.
DR GlyGen; O08617; 1 site.
DR iPTMnet; O08617; -.
DR PhosphoSitePlus; O08617; -.
DR PaxDb; O08617; -.
DR GeneID; 94202; -.
DR KEGG; rno:94202; -.
DR UCSC; RGD:620780; rat. [O08617-1]
DR CTD; 5801; -.
DR RGD; 620780; Ptprr.
DR eggNOG; KOG0789; Eukaryota.
DR InParanoid; O08617; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; O08617; -.
DR PRO; PR:O08617; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:RGD.
DR GO; GO:0038128; P:ERBB2 signaling pathway; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IEP:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; ISO: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 InterPro; IPR016334; Tyr_Pase_rcpt_R/non-rcpt_5.
DR PANTHER; PTHR46198; PTHR46198; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF001997; PTPRR; 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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Glycoprotein; Hydrolase;
KW Membrane; Phosphoprotein; Protein phosphatase; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..656
FT /note="Receptor-type tyrosine-protein phosphatase R"
FT /id="PRO_0000025461"
FT TOPO_DOM 25..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 392..646
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 587
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 553
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 587..593
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 631
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62132"
FT MOD_RES 338
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q62132"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..287
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7557444"
FT /id="VSP_005164"
FT VAR_SEQ 1..244
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7814416"
FT /id="VSP_005163"
FT VAR_SEQ 1..121
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:7557444"
FT /id="VSP_005162"
FT CONFLICT 202
FT /note="S -> I (in Ref. 1; BAA19530)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="F -> L (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="S -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 510..511
FT /note="IY -> TH (in Ref. 2; AAA64485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 73907 MW; E929E5473B6A9DE9 CRC64;
MRRAVGFPAL CLLLNLHAAG CFSRNNDHFL AIRQKKSWKP MFIYDHSQDI KKSLDIAQEA
YKHNYPAPSE VQISKRHQIV DSAFPRPAYD PSLNLLAASG QDLEIENLPI PAANVIVVTL
QMDIDKLNIT LLRIFRQGVA AALGLLPQQV HINRLIEKKS QIELFVSPGN RKPGEPQALQ
AEEVLRSLNV DVLRQSLPQF GSIDVSPEKN VLQGQHEADK IWSKEGFYAV VIFLSIFIII
VTCLMIIYRL KERLQLSFRQ DKEKNQEIHL SPIALQQAQS EAKAAHSMVQ PDQAPKVLNV
VVDPQGQCTP EIRNTASTSV CPSPFRMKPI GLQERRGSNV SLTLDMSSLG NVEPFVAVST
PREKVAMEYL QSASRVLTSP QLRDVVASSH LLQSEFMEIP MNFVDPKEID IPRHGTKNRY
KTILPNPLSR VCLRPKNITD PLSTYINANY IRGYSGKEKA FIATQGPMIN TVNDFWQMVW
QEDSPVIVMI TKLKEKNEKC VLYWPEKRGI YGKVEVLVIG VNECDNYTIR NLVLKRGSHT
QHVKHYWYTS WPDHKTPDSA QPLLQLMLDV EEDRLASEGR GPVVVHCSAG IGRTGCFIAT
SIGCQQLKEE GVVDALSIVC QLRVDRGGMV QTSEQYEFVH HALCLFESRL SPETVQ
