P18052 · PTPRA_MOUSE
- ProteinReceptor-type tyrosine-protein phosphatase alpha
- GenePtpra
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids829 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tyrosine protein phosphatase which is involved in integrin-mediated focal adhesion formation (PubMed:22801373).
Following integrin engagement, specifically recruits BCAR3, BCAR1 and CRK to focal adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and the subsequent activation of PAK and small GTPase RAC1 and CDC42 (PubMed:22801373).
Following integrin engagement, specifically recruits BCAR3, BCAR1 and CRK to focal adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and the subsequent activation of PAK and small GTPase RAC1 and CDC42 (PubMed:22801373).
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 437 | substrate | ||||
Sequence: D | ||||||
Active site | 469 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 469-475 | substrate | ||||
Sequence: CSAGVGR | ||||||
Binding site | 513 | substrate | ||||
Sequence: Q | ||||||
Active site | 759 | Phosphocysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | focal adhesion | |
Cellular Component | membrane | |
Cellular Component | receptor complex | |
Cellular Component | Schaffer collateral - CA1 synapse | |
Cellular Component | synaptic membrane | |
Molecular Function | protein tyrosine phosphatase activity | |
Molecular Function | protein-containing complex binding | |
Biological Process | insulin receptor signaling pathway | |
Biological Process | integrin-mediated signaling pathway | |
Biological Process | modulation of chemical synaptic transmission | |
Biological Process | positive regulation of oligodendrocyte differentiation | |
Biological Process | regulation of focal adhesion assembly |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReceptor-type tyrosine-protein phosphatase alpha
- EC number
- Short namesProtein-tyrosine phosphatase alpha; R-PTP-alpha
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP18052
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: Localizes to focal adhesion sites following integrin engagement.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-142 | Extracellular | ||||
Sequence: NNATTVSPSLGTTRLIKTSTTELAKEENKTSNSTSSVISLSVAPTFSPNLTLEPTYVTTVNSSHSDNGTRRAASTESGGTTISPNGSWLIENQFTDAITEPWEGNSSTAATTPETFPPADETP | ||||||
Transmembrane | 143-166 | Helical | ||||
Sequence: IIAVMVALSSLLVIVFIIIVLYML | ||||||
Topological domain | 167-829 | Cytoplasmic | ||||
Sequence: RFKKYKQAGSHSNSFRLSNGRTEDVEPQSVPLLARSPSTNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPFLSLAVSKDAVKALNKTTPLLERRFIGKSNSRGCLSDDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNVRVSVEDVTVLVDYTVRKFCIQQVGDVTNRKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKACNPQYAGAIVVHCSAGVGRTGTFVVIDAMLDMMHSERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTELEVTSLETHLQKIYNKIPGTSNNGLEEEFKKLTSIKIQNDKMRTGNLPANMKKNRVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLLHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQEYIDAFSDYANFK |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MDSWFILVLFGSGLIHVSA | ||||||
Chain | PRO_0000025434 | 20-829 | Receptor-type tyrosine-protein phosphatase alpha | |||
Sequence: NNATTVSPSLGTTRLIKTSTTELAKEENKTSNSTSSVISLSVAPTFSPNLTLEPTYVTTVNSSHSDNGTRRAASTESGGTTISPNGSWLIENQFTDAITEPWEGNSSTAATTPETFPPADETPIIAVMVALSSLLVIVFIIIVLYMLRFKKYKQAGSHSNSFRLSNGRTEDVEPQSVPLLARSPSTNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPFLSLAVSKDAVKALNKTTPLLERRFIGKSNSRGCLSDDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNVRVSVEDVTVLVDYTVRKFCIQQVGDVTNRKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKACNPQYAGAIVVHCSAGVGRTGTFVVIDAMLDMMHSERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTELEVTSLETHLQKIYNKIPGTSNNGLEEEFKKLTSIKIQNDKMRTGNLPANMKKNRVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLLHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQEYIDAFSDYANFK | ||||||
Glycosylation | 21 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 47 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 51 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 68 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 80 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 86 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 104 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 124 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 202 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 204 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 825 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Integrin binding to extracellular matrix induces phosphorylation at Tyr-825 which induces PTPRA localization and recruitment of BCAR3, BCAR1 and CRK to focal adhesions.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Highest expression in brain and kidney.
Gene expression databases
Interaction
Subunit
Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain), and SRC (PubMed:22801373).
Within the complex, interacts (when phosphorylated on Tyr-825) with BCAR3 (via SH2 domain) (PubMed:22801373).
Interacts with GRB2 (PubMed:22801373).
Within the complex, interacts (when phosphorylated on Tyr-825) with BCAR3 (via SH2 domain) (PubMed:22801373).
Interacts with GRB2 (PubMed:22801373).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P18052 | Chl1 P70232 | 4 | EBI-6597520, EBI-7703109 | |
BINARY | P18052 | Grb2 Q60631 | 4 | EBI-6597520, EBI-1688 | |
XENO | P18052 | Prkcb P68403 | 3 | EBI-6597520, EBI-397072 | |
BINARY | P18052 | Ptprn Q60673 | 3 | EBI-6597520, EBI-8328895 | |
BINARY | P18052 | Src P05480 | 2 | EBI-6597520, EBI-298680 | |
XENO | P18052 | SRC P00523 | 2 | EBI-6597520, EBI-848039 | |
XENO | P18052 | SRC P12931 | 3 | EBI-6597520, EBI-621482 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 79-106 | Disordered | ||||
Sequence: VNSSHSDNGTRRAASTESGGTTISPNGS | ||||||
Domain | 232-528 | Tyrosine-protein phosphatase 1 | ||||
Sequence: FREEFNALPACPIQATCEAASKEENKEKNRYVNILPFLSLAVSKDAVKALNKTTPLLERRFIGKSNSRGCLSDDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNVRVSVEDVTVLVDYTVRKFCIQQVGDVTNRKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKACNPQYAGAIVVHCSAGVGRTGTFVVIDAMLDMMHSERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEH | ||||||
Domain | 560-818 | Tyrosine-protein phosphatase 2 | ||||
Sequence: LEEEFKKLTSIKIQNDKMRTGNLPANMKKNRVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLLHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQEY |
Sequence similarities
Belongs to the protein-tyrosine phosphatase family. Receptor class 4 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P18052-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsLong
- Length829
- Mass (Da)93,698
- Last updated2011-07-27 v3
- Checksum4724A0F477D304B5
P18052-2
- Name2
- SynonymsShort
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8VHH6 | A0A2R8VHH6_MOUSE | Ptpra | 374 | ||
Q91V35 | Q91V35_MOUSE | Ptpra | 793 |
Features
Showing features for sequence conflict, alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M36033 EMBL· GenBank· DDBJ | AAA39448.1 EMBL· GenBank· DDBJ | mRNA | ||
M36034 EMBL· GenBank· DDBJ | AAA39449.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
L13607 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL731707 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466519 EMBL· GenBank· DDBJ | EDL28272.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z23054 EMBL· GenBank· DDBJ | CAA80589.1 EMBL· GenBank· DDBJ | mRNA | ||
Z23055 EMBL· GenBank· DDBJ | CAA80590.1 EMBL· GenBank· DDBJ | mRNA |