P35822 · PTPRK_MOUSE
- ProteinReceptor-type tyrosine-protein phosphatase kappa
- GenePtprk
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1457 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa.
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 | 1068 | substrate | ||||
Sequence: D | ||||||
Active site | 1100 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 1100-1106 | substrate | ||||
Sequence: CSAGAGR | ||||||
Binding site | 1144 | substrate | ||||
Sequence: Q | ||||||
Active site | 1394 | Phosphocysteine intermediate | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | dendrite | |
Cellular Component | membrane | |
Cellular Component | neuronal cell body | |
Cellular Component | photoreceptor outer segment | |
Molecular Function | protein tyrosine phosphatase activity | |
Biological Process | cell adhesion | |
Biological Process | neuron projection development |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReceptor-type tyrosine-protein phosphatase kappa
- EC number
- Short namesProtein-tyrosine phosphatase kappa; R-PTP-kappa
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP35822
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 26-752 | Extracellular | ||||
Sequence: ALGQFSAGGCTFDDGPGACDYHQDLYDDFEWVHVSAQEPHYLPPEMPQGSYMVVDSSNHDPGEKARLQLPTMKENDTHCIDFSYLLYSQKGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTFWPNEYQVIFEAEVSGGRSGYIAIDDIQVLSYPCDKSPHFLRLGDVEVNAGQNATFQCIATGRDAVHNKLWLQRRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCVTQSERGSGVSNFAQLIVREPPRPIAPPQLLGVGPTYLLIQLNANSIIGDGPIILKEVEYRMTSGSWTETHAVNAPTYKLWHLDPDTEYEIRVLLTRPGEGGTGLPGPPLITRTKCAEPMRTPKTLKIAEIQARRIAVDWESLGYNITRCHTFNVTICYHYFRGHNESRADCLDMDPKAPQHVVNHLPPYTNVSLKMILTNPEGRKESEETIIQTDEDVPGPVPVKSLQGTSFENKIFLNWKEPLEPNGIITQYEVSYSSIRSFDPAVPVAGPPQTVSNLWNSTHHVFMHLHPGTTYQFFIRASTVKGFGPATAINVTTNISAPSLPDYEGVDASLNETATTITVLLRPAQAKGAPISAYQIVVEQLHPHRTKREAGAMECYQVPVTYQNALSGGAPYYFAAELPPGNLPEPAPFTVGDNRTYKGFWNPPLAPRKGYNIYFQAMSSVEKETKTQCVRIATKAAATEEPEVIPDPAKQTDRVVK | ||||||
Transmembrane | 753-774 | Helical | ||||
Sequence: IAGISAGILVFILLLLVVIVIV | ||||||
Topological domain | 775-1457 | Cytoplasmic | ||||
Sequence: KKSKLAKKRKDAMGNTRQEMTHMVNAMDRSYADQSTLHAEDPLSLTFMDQHNFSPRLPNDPLVPTAVLDENHSATAESSRLLDVPRYLCEGTESPYQTGQLHPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDIWLYRDGYQRPSHYIATQGPVHETVYDFWRMVWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLCGETAIPVCEFKAAYFDMIRIDSQTNSSHLKDEFQTLNSVTPRLQAEDCSIACLPRNHDKNRFMDMLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYLESS |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MDVAAAALPAFVALWLLYPWPLLGS | ||||||
Chain | PRO_0000025447 | 26-1457 | Receptor-type tyrosine-protein phosphatase kappa | |||
Sequence: ALGQFSAGGCTFDDGPGACDYHQDLYDDFEWVHVSAQEPHYLPPEMPQGSYMVVDSSNHDPGEKARLQLPTMKENDTHCIDFSYLLYSQKGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTFWPNEYQVIFEAEVSGGRSGYIAIDDIQVLSYPCDKSPHFLRLGDVEVNAGQNATFQCIATGRDAVHNKLWLQRRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCVTQSERGSGVSNFAQLIVREPPRPIAPPQLLGVGPTYLLIQLNANSIIGDGPIILKEVEYRMTSGSWTETHAVNAPTYKLWHLDPDTEYEIRVLLTRPGEGGTGLPGPPLITRTKCAEPMRTPKTLKIAEIQARRIAVDWESLGYNITRCHTFNVTICYHYFRGHNESRADCLDMDPKAPQHVVNHLPPYTNVSLKMILTNPEGRKESEETIIQTDEDVPGPVPVKSLQGTSFENKIFLNWKEPLEPNGIITQYEVSYSSIRSFDPAVPVAGPPQTVSNLWNSTHHVFMHLHPGTTYQFFIRASTVKGFGPATAINVTTNISAPSLPDYEGVDASLNETATTITVLLRPAQAKGAPISAYQIVVEQLHPHRTKREAGAMECYQVPVTYQNALSGGAPYYFAAELPPGNLPEPAPFTVGDNRTYKGFWNPPLAPRKGYNIYFQAMSSVEKETKTQCVRIATKAAATEEPEVIPDPAKQTDRVVKIAGISAGILVFILLLLVVIVIVKKSKLAKKRKDAMGNTRQEMTHMVNAMDRSYADQSTLHAEDPLSLTFMDQHNFSPRLPNDPLVPTAVLDENHSATAESSRLLDVPRYLCEGTESPYQTGQLHPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDIWLYRDGYQRPSHYIATQGPVHETVYDFWRMVWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLCGETAIPVCEFKAAYFDMIRIDSQTNSSHLKDEFQTLNSVTPRLQAEDCSIACLPRNHDKNRFMDMLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYLESS | ||||||
Glycosylation | 100 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 139 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 210 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 215↔269 | |||||
Sequence: CIATGRDAVHNKLWLQRRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRC | ||||||
Glycosylation | 415 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 423 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 435 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 461 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 551 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 585 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 589 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 606 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 689 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 868 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
This protein undergoes proteolytic processing.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
High levels in liver and kidney. Lower levels in lung, brain and heart. Not seen in spleen and testis.
Developmental stage
Developmentally regulated with highest expression found in developing areas or in areas capable of developmental plasticity.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-193 | MAM | ||||
Sequence: FSAGGCTFDDGPGACDYHQDLYDDFEWVHVSAQEPHYLPPEMPQGSYMVVDSSNHDPGEKARLQLPTMKENDTHCIDFSYLLYSQKGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTFWPNEYQVIFEAEVSGGRSGYIAIDDIQVLSYPCDK | ||||||
Domain | 195-280 | Ig-like C2-type | ||||
Sequence: PHFLRLGDVEVNAGQNATFQCIATGRDAVHNKLWLQRRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCVTQSERGSGVS | ||||||
Domain | 293-388 | Fibronectin type-III 1 | ||||
Sequence: PIAPPQLLGVGPTYLLIQLNANSIIGDGPIILKEVEYRMTSGSWTETHAVNAPTYKLWHLDPDTEYEIRVLLTRPGEGGTGLPGPPLITRTKCAEP | ||||||
Domain | 391-487 | Fibronectin type-III 2 | ||||
Sequence: TPKTLKIAEIQARRIAVDWESLGYNITRCHTFNVTICYHYFRGHNESRADCLDMDPKAPQHVVNHLPPYTNVSLKMILTNPEGRKESEETIIQTDED | ||||||
Domain | 490-594 | Fibronectin type-III 3 | ||||
Sequence: GPVPVKSLQGTSFENKIFLNWKEPLEPNGIITQYEVSYSSIRSFDPAVPVAGPPQTVSNLWNSTHHVFMHLHPGTTYQFFIRASTVKGFGPATAINVTTNISAPS | ||||||
Domain | 595-688 | Fibronectin type-III 4 | ||||
Sequence: LPDYEGVDASLNETATTITVLLRPAQAKGAPISAYQIVVEQLHPHRTKREAGAMECYQVPVTYQNALSGGAPYYFAAELPPGNLPEPAPFTVGD | ||||||
Domain | 899-1159 | Tyrosine-protein phosphatase 1 | ||||
Sequence: FKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDIWLYRDGYQRPSHYIATQGPVHETVYDFWRMVWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEA | ||||||
Domain | 1191-1453 | Tyrosine-protein phosphatase 2 | ||||
Sequence: LKDEFQTLNSVTPRLQAEDCSIACLPRNHDKNRFMDMLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEY |
Sequence similarities
Belongs to the protein-tyrosine phosphatase family. Receptor class 2B subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,457
- Mass (Da)164,186
- Last updated1994-06-01 v1
- Checksum19D4B99B7ECE8605
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1W2P6K2 | A0A1W2P6K2_MOUSE | Ptprk | 36 | ||
A0A1W2P706 | A0A1W2P706_MOUSE | Ptprk | 282 | ||
A0A1W2P7Y1 | A0A1W2P7Y1_MOUSE | Ptprk | 1471 | ||
B2RRF0 | B2RRF0_MOUSE | Ptprk | 1445 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L10106 EMBL· GenBank· DDBJ | AAA40021.1 EMBL· GenBank· DDBJ | mRNA |