UniProt:Q92932 PTPRN2

chain
  • signal peptide:1-21
  • chain:22-1015
  • chain:502-1015
checksum 950C15CA89DBC029
comment
  • FUNCTION Plays a role in vesicle-mediated secretory processes. Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets. Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation. Plays a role in insulin secretion in response to glucose stimuli. Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain. In females, but not in males, required for normal accumulation and secretion of pituitary hormones, such as luteinizing hormone (LH) and follicle-stimulating hormone (FSH) (By similarity). Required to maintain normal levels of renin expression and renin release (By similarity). May regulate catalytic active protein-tyrosine phosphatases such as PTPRA through dimerization (By similarity). Has phosphatidylinositol phosphatase activity; the PIPase activity is involved in its ability to regulate insulin secretion. Can dephosphorylate phosphatidylinositol 4,5-biphosphate (PI(4,5)P2), phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate (By similarity). Regulates PI(4,5)P2 level in the plasma membrane and localization of cofilin at the plasma membrane and thus is indirectly involved in regulation of actin dynamics related to cell migration and metastasis; upon hydrolysis of PI(4,5)P2 cofilin is released from the plasma membrane and acts in the cytoplasm in severing F-actin filaments (PubMed:26620550).CATALYTIC ACTIVITY O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] + phosphateBIOPHYSICOCHEMICAL PROPERTIES Optimum pH is 4.5.SUBUNIT Self-associates. Interacts (via cytoplasmic domain) with PTPRN (via cytoplasmic domain). Interacts (precursor form) with CPE. Interacts with HAP1. Interacts with AP2A1 or AP2A2 and AP1G1; indicative for an association with adaptor protein complex 2 (AP-2) and adaptor protein complex 1 (AP-1) (By similarity). Interacts with AP2M1; indicative for an association with adaptor protein complex 2 (AP-2). Interacts with MYO5A (By similarity).SUBCELLULAR LOCATION Predominantly found on dense-core secretory granules. Sorting to secretory granules in part is dependent of the N-terminal propeptide domain of the precursor and its interaction with CPE (By similarity). Transiently found at the cell membrane, when secretory vesicles fuse with the cell membrane to release their cargo. Is then endocytosed and recycled to secretory vesicles involving clathrin-dependent AP2-mediated endocytosis. Recycled via STX6- but not TTTGN1/TGN38-containing compartments (By similarity).SUBCELLULAR LOCATION Highest levels in brain and pancreas (PubMed:8798755, PubMed:8954911). Lower levels in trachea, prostate, stomach and spinal cord (PubMed:8798755).DOMAIN The cytoplasmic domain appears to contain the autoantigenic epitopes.DOMAIN The leucine-based sorting signal is proposed to function in trafficking at the plasma membrane.DOMAIN The tyrosine-based internalization signal is proposed to function at the level of clathrin-mediated endocytosis and recycling.PTM Subject to proteolytic cleavage at multiple sites.DISEASE Autoantigen in insulin-dependent diabetes mellitus (IDDM).SIMILARITY Belongs to the protein-tyrosine phosphatase family. Receptor class 8 subfamily.CAUTION Has no tyrosine-protein phosphatase activity at mild acidic conditions (pH 5.5). The in vivo relevance of the low PPase activity at acidic conditions (pH 4.5) is questioned. This catalytic activity seems to be affected by the replacement of a highly conserved residue in the tyrosine-protein phosphatase domain.
crossReference
databaseName UniProt
dbId 62481
description
  • recommendedName: Receptor-type tyrosine-protein phosphatase N2 shortName: R-PTP-N2 ecNumber: 3.1.3.- ecNumber evidence="25"3.1.3.48 alternativeName: fullName evidence="19"Islet cell autoantigen-related protein shortName evidence="19"IAR shortName evidence="21"ICAAR alternativeName: fullName evidence="18 20"Phogrin component recommendedName: IA-2beta60 /component
displayName UniProt:Q92932 PTPRN2
geneName
  • PTPRN2
  • KIAA0387
identifier Q92932
isSequenceChanged false
keyword
  • 3D-structure
  • Acetylation
  • Alternative splicing
  • Cytoplasmic vesicle
  • Diabetes mellitus
  • Glycoprotein
  • Hydrolase
  • Lipid metabolism
  • Membrane
  • Phospholipid metabolism
  • Phosphoprotein
  • Protein phosphatase
  • Proteomics identification
  • Receptor
  • Reference proteome
  • Signal
  • Synapse
  • Transmembrane
  • Transmembrane helix
modified [InstanceEdit:9939033] Weiser, Joel, 2025-02-21
moleculeType Protein
name
  • PTPRN2
otherIdentifier
  • 11729975_a_at
  • 11729976_a_at
  • 11754309_s_at
  • 17064907
  • 203029_PM_s_at
  • 203029_s_at
  • 203030_PM_s_at
  • 203030_s_at
  • 211534_PM_x_at
  • 211534_x_at
  • 3081895
  • 3081896
  • 3081897
  • 3081898
  • 3081902
  • 3081913
  • 3081916
  • 3081918
  • 3081919
  • 3081926
  • 3081932
  • 3081940
  • 3081960
  • 3081961
  • 3081970
  • 3081997
  • 3082011
  • 3082023
  • 3082027
  • 3082028
  • 3082030
  • 3082031
  • 3082043
  • 3082044
  • 3082048
  • 3082050
  • 3082067
  • 3082086
  • 3082096
  • 3082097
  • 36160_s_at
  • 5799
  • 8144121
  • A_32_P66804
  • A_32_P79434
  • GE59343
  • GO:0003824
  • GO:0004721
  • GO:0004725
  • GO:0005001
  • GO:0005886
  • GO:0006470
  • GO:0006629
  • GO:0007269
  • GO:0016020
  • GO:0016311
  • GO:0016787
  • GO:0030141
  • GO:0030658
  • GO:0030659
  • GO:0030667
  • GO:0030672
  • GO:0031410
  • GO:0035773
  • GO:0043235
  • GO:0045202
  • GO:0051046
  • GO:0101003
  • GO:0140096
  • HMNXSV003022897
  • ILMN_1728844
  • PH_hs_0004259
  • TC07002077.hg
  • U66702_at
  • g11386148_3p_a_at
  • g2262074_3p_a_at
  • g2281288_3p_a_at
physicalEntity
referenceDatabase [ReferenceDatabase:2] UniProt
referenceGene
referenceTranscript
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • PTPR2_HUMAN
  • E9PC57
  • Q8N4I5
  • Q92662
  • Q9Y4F8
  • Q9Y4I6
sequenceLength 1015
species [Species:48887] Homo sapiens
stId uniprot:Q92932
url http://purl.uniprot.org/uniprot/Q92932
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