Ptprr protein tyrosine phosphatase receptor type R [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ptprrprovided by MGI
Official Full Name: protein tyrosine phosphatase receptor type Rprovided by MGI
Primary source: MGI:MGI:109559
See related: Ensembl:ENSMUSG00000020151 AllianceGenome:MGI:109559
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Gmcp1; PTP-SL; PTPBR7; RPTPRR; mPTP213
Summary: Enables protein kinase binding activity and protein tyrosine phosphatase activity. Acts upstream of or within protein dephosphorylation. Predicted to be active in cell junction; cytosol; and plasma membrane. Is expressed in several structures, including central nervous system; dorsal root ganglion; and retina nuclear layer. Orthologous to human PTPRR (protein tyrosine phosphatase receptor type R). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Biased expression in cerebellum adult (RPKM 11.6), large intestine adult (RPKM 6.4) and 11 other tissues See more
Orthologs: human all
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Genomic context

Location:: 10 D2; 10 64.01 cM

Exon count:: 17

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	10	NC_000076.7 (115854093..116110837)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	10	NC_000076.6 (116018188..116274932)

Chromosome 10 - NC_000076.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

These findings indicate an important role for PTPRR in maintaining low basal mitogen-activated protein kinase activity in Purkinje cells.
Title: Protein tyrosine phosphatase receptor type R is required for Purkinje cell responsiveness in cerebellar long-term depression.
The data of this study disclosed a distinct role for PTPRR in recognition memory and exploration of a new environment.
Title: Protein tyrosine phosphatase receptor type R deficient mice exhibit increased exploration in a new environment and impaired novel object recognition memory.
Results support the suggested link between PTPRR isoforms and cerebellar calcium ion homeostasis, and suggest an additional role in the process of cell-cell adhesion
Title: PTPBR7 binding proteins in myelinating neurons of the mouse brain.
PTP-SL, like PTPBR7, is a single membrane-spanning receptor-type protein tyrosine phosphatases.
Title: Multimerisation of receptor-type protein tyrosine phosphatases PTPBR7 and PTP-SL attenuates enzymatic activity.
Ptprr-/- mice displayed ataxia characterized by defects in fine motor coordination and balance skills.
Title: Altered MAP kinase phosphorylation and impaired motor coordination in PTPRR deficient mice.
PTPBR7, was subject to N-terminal proteolytic processing, in between amino acid position 136 and 137, resulting in an additional, 65-kDa transmembrane PTPRR isoform.
Title: Proteolytic processing of the receptor-type protein tyrosine phosphatase PTPBR7.
The ERK2 docking groove is more restrictive and selective for its tyrosine phosphatase inactivators than for MEK1/2 and indicate that distinct ERK2 residues modulate the docking interactions with activating and inactivating effectors.
Title: ERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1.
Multiple isoforms through the use of distinct promoters, alternative splicing and differential translation starts.
Title: Characterization of multiple transcripts and isoforms derived from the mouse protein tyrosine phosphatase gene Ptprr.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (2)
Targeted (1) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D10Mit101 (e-PCR), detects polymorphism
- UniSTS:125997

D10Mit157.2 (e-PCR), detects polymorphism
- UniSTS:126061

AU048245 (e-PCR)
- UniSTS:109727

D31898 (e-PCR)
- UniSTS:163488

Ptprr (e-PCR), detects polymorphism
- UniSTS:536491

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables histone H2AXY142 phosphatase activity	IEA Inferred from Electronic Annotation more info
enables non-membrane spanning protein tyrosine phosphatase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein kinase binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein kinase binding	IDA Inferred from Direct Assay more info	PubMed
enables protein tyrosine phosphatase activity	IBA Inferred from Biological aspect of Ancestor more info
enables protein tyrosine phosphatase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein tyrosine phosphatase activity, metal-dependent	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in ERBB2 signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in ERBB2 signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in chromatin remodeling	IEA Inferred from Electronic Annotation more info
involved_in in utero embryonic development	ISS Inferred from Sequence or Structural Similarity more info
involved_in negative regulation of ERK1 and ERK2 cascade	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of ERK1 and ERK2 cascade	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of epithelial cell migration	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of epithelial cell migration	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within protein dephosphorylation	IDA Inferred from Direct Assay more info	PubMed
involved_in signal transduction	IBA Inferred from Biological aspect of Ancestor more info

Component	Evidence Code	Pubs
is_active_in cell junction	IBA Inferred from Biological aspect of Ancestor more info
located_in cell junction	IEA Inferred from Electronic Annotation more info
located_in cell junction	ISO Inferred from Sequence Orthology more info
is_active_in cytosol	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
is_active_in plasma membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: receptor-type tyrosine-protein phosphatase R

Names: R-PTP-R; STEP-like PTPase; phosphotyrosine phosphatase 13; protein-tyrosine-phosphatase-SL

NP_001155309.1

EC 3.1.3.48

NP_001155310.1

EC 3.1.3.48

NP_001155311.1

EC 3.1.3.48

NP_001155312.1

EC 3.1.3.48

NP_001345413.1

EC 3.1.3.48

NP_035347.1

EC 3.1.3.48

XP_006513445.1

EC 3.1.3.48

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001161837.2 → NP_001155309.1 receptor-type tyrosine-protein phosphatase R isoform b

Status: VALIDATED

Description

Transcript Variant: This variant (2) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (b) has a shorter and distinct N-terminus compared to isoform a.

Source sequence(s)

AC166836

Consensus CDS

CCDS56750.1

UniProtKB/TrEMBL

Q5U1V1

Related

ENSMUSP00000100907.3, ENSMUST00000105271.9

Conserved Domains (2) summary

smart00194
Location:284 → 536

PTPc; Protein tyrosine phosphatase, catalytic domain

cd00047
Location:309 → 536

PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
NM_001161838.2 → NP_001155310.1 receptor-type tyrosine-protein phosphatase R isoform c

Status: VALIDATED

Description

Transcript Variant: This variant (3) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (c) is shorter at the N-terminus compared to isoform a.

Source sequence(s)

AC166836

Consensus CDS

CCDS48693.1

UniProtKB/TrEMBL

Q5U1U8

Related

ENSMUSP00000114455.2, ENSMUST00000128399.2

Conserved Domains (2) summary

smart00194
Location:147 → 399

PTPc; Protein tyrosine phosphatase, catalytic domain

cd00047
Location:172 → 399

PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
NM_001161839.2 → NP_001155311.1 receptor-type tyrosine-protein phosphatase R isoform c

Status: VALIDATED

Description

Transcript Variant: This variant (4) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (c) is shorter at the N-terminus compared to isoform a.

Source sequence(s)

AC166836

Consensus CDS

CCDS48693.1

UniProtKB/TrEMBL

Q5U1U8

Related

ENSMUSP00000120965.2, ENSMUST00000148731.8

Conserved Domains (2) summary

smart00194
Location:147 → 399

PTPc; Protein tyrosine phosphatase, catalytic domain

cd00047
Location:172 → 399

PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
NM_001161840.2 → NP_001155312.1 receptor-type tyrosine-protein phosphatase R isoform c

Status: VALIDATED

Description

Transcript Variant: This variant (5) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (c) is shorter at the N-terminus compared to isoform a.

Source sequence(s)

AC166836

Consensus CDS

CCDS48693.1

UniProtKB/TrEMBL

Q5U1U8

Related

ENSMUSP00000122259.2, ENSMUST00000155606.8

Conserved Domains (2) summary

smart00194
Location:147 → 399

PTPc; Protein tyrosine phosphatase, catalytic domain

cd00047
Location:172 → 399

PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
NM_001358484.2 → NP_001345413.1 receptor-type tyrosine-protein phosphatase R isoform d

Status: VALIDATED

Description

Transcript Variant: This variant (6) differs in the 5' UTR and coding sequence compared to variant 1. The resulting isoform (d) is shorter at the N-terminus compared to isoform a.

Source sequence(s)

AC166836

UniProtKB/TrEMBL

Q5U1U5, Q5U1V1

Conserved Domains (1) summary

cd00047
Location:295 → 522

PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...
NM_001428770.1 → NP_001415699.1 receptor-type tyrosine-protein phosphatase R isoform e precursor

Status: VALIDATED

Source sequence(s)

AC124522, AC166836
NM_011217.3 → NP_035347.1 receptor-type tyrosine-protein phosphatase R isoform a precursor

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform (a).

Source sequence(s)

AC124522, AC166836

Consensus CDS

CCDS24182.1

UniProtKB/Swiss-Prot

Q62132, Q64491, Q64492, Q9QUH9

UniProtKB/TrEMBL

Q5U1U6, Q8CEI8

Related

ENSMUSP00000064392.5, ENSMUST00000063470.11

Conserved Domains (2) summary

smart00194
Location:391 → 643

PTPc; Protein tyrosine phosphatase, catalytic domain

cd00047
Location:416 → 643

PTPc; Protein tyrosine phosphatases (PTP) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr ...

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000076.7 Reference GRCm39 C57BL/6J

Range

115854093..116110837

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006513382.2 → XP_006513445.1 receptor-type tyrosine-protein phosphatase R isoform X1

Conserved Domains (1) summary

cd14611
Location:379 → 604

R-PTPc-R; catalytic domain of receptor-type tyrosine-protein phosphatase R