Ptprn
entrez
116660
canonical
uniprot
Q63259
canonical
ensembl
ENSRNOG00000019587
resolver
ensp
ENSRNOP00000026654
resolver
genesymbol
Ptprn
resolver
uniprot
Q62883
resolver
uniprot
Q63795
resolver
uniprot
Q64643
resolver
uniprot_entry
PTPRN_RAT
resolver
uniprot_sec
Q62883
resolver
uniprot_sec
Q63795
resolver
uniprot_sec
Q64643
resolver
amino_acid_sequence
MRRPRRPGGPAGCGGSEGSGGLRLLVCLLLLSGRPGGCSAISAHGCLFDRRLCSHLEVCIQDGLFGQCQAGVGQARPLLQVTSPVLQRLQGVLRQLMSQGLSWHDDLTQYVISQEMERIPRLRPPEPHPRDRSGSVPRRAGPAGELLSQGNPTGSSPAVQGLSRPPGDGNGAGVGSPLSSLQAELLPPLLEHLLMPPQPPHPSLTYEPALLQPYLFQQFGSRDGSRGSESASGVVGHLAKAEDPVLFSRSLSKAILGTHSGHSFGDLTGPSPAQLFQDSGLLYMAQELPVPGRARAPRLPEEGGSSRAEDSSEGHEEEVLGGHGEKSPPQAVQADVSLQRLAAVLAGYGVELRQLTPEQLSTLLTLLQLLPKGTGRHLGGAVNGGADVKKTIEEQMQRGDTADARPPTPLLPGHPTASSTSIKVRQVLSPGFPEPPKTSSPLGISAVLLEKKSPLGQSQPTVVGQPSARPSAEEYGYIVTDQKPLSLVAGVKLLEILAEHVHMTSGSFINISVVGPAVTFRIRHNEQNLSLADVTQQAGLVKSELEAQTGLQILQTGVGQREESAAVLPRQAHGISPMRSLLLTLVALAGVAGLLVALAVALCMRHHSKQRDKERLAALGPEGAHGDTTFEYQDLCRQHMATKSLFNRAEGQPEPSRVSSVSSQFSDAAQASPSSHSSTPSWCEEPAQANMDISTGHMILAYMEDHLRNRDRLAKEWQALCAYQAEPNTCATAQGEGNIKKNRHPDFLPYDHARIKLKVESSPSRSDYINASPIIEHDPRMPAYIATQGPLSHTIADFWQMVWESGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHVYEVNLVSEHIWCEDFLVRSFYLKNVQTQETRTLTQFHFLSWPAEGTPASTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATLEHVRDQRPGLVRSKDQFEFALTAVAEEVNAILKALPQ
uniprot
proteins
function
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). Required to maintain normal levels of renin expression and renin release. Seems to lack intrinsic enzyme activity. {ECO:0000250|UniProtKB:Q16849, ECO:0000250|UniProtKB:Q60673}.; FUNCTION: [ICA512-transmembrane fragment]: ICA512-TMF regulates dynamics and exocytosis of insulin secretory granules (SGs); binding of ICA512-TMF to SNTB2/beta-2-syntrophin is proposed to restrain SGs mobility and exocytosis by tethering them to the actin cytoskeleton depending on UTRN; the function is inhibited by cytoplasmic ICA512-CFF dimerizing with ICA512-TMF and displacing SNTB2 (By similarity). {ECO:0000250|UniProtKB:Q16849}.; FUNCTION: [ICA512-cleaved cytosolic fragment]: ICA512-CCF translocated to the nucleus promotes expression of insulin and other granule-related genes; the function implicates binding to and regulating activity of STAT5B probably by preventing its dephosphorylation and potentially by inducing its sumoylation by recruiting PIAS4 (By similarity). Enhances pancreatic beta-cell proliferation by converging with signaling by STAT5B and STAT3 (PubMed:18178618). ICA512-CCF located in the cytoplasm regulates dynamics and exocytosis of insulin secretory granules (SGs) by dimerizing with ICA512-TMF and displacing SNTB2 thus enhancing SGs mobility and exocytosis (By similarity). {ECO:0000250|UniProtKB:Q16849, ECO:0000269|PubMed:18178618}.
uniprot
proteins
mass_dalton
106228
uniprot
proteins
post_translational_modification
PTM: Subject to proteolytic cleavage at multiple sites (PubMed:7568143). Subject to cleavage on a pair of basic residues (By similarity). Following exocytosis of secretory granules in pancreatic beta-cells ICA512-TMF located in the plasma-membrane is cleaved by mu-type calpain CPN1 to yield ICA512-CCF (PubMed:15596545). {ECO:0000250|UniProtKB:P56722, ECO:0000269|PubMed:15596545, ECO:0000269|PubMed:7568143}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q16849}.; PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q16849}.; PTM: Sumoylated at two sites including Lys-758. Sumoylation decreases interaction with STAT5. {ECO:0000250|UniProtKB:Q16849}.
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
protein_family
Receptor class 8 subfamily
uniprot
proteins
pubmed
10457160
uniprot
proteins
pubmed
11483505
uniprot
proteins
pubmed
15596545
uniprot
proteins
pubmed
18178618
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
7568143
uniprot
proteins
pubmed
7657822
uniprot
proteins
pubmed
7887886
uniprot
proteins
pubmed
8641276
uniprot
proteins
sequence_length
983
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:7568143, ECO:0000305|PubMed:7657822}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:11483505, ECO:0000269|PubMed:8641276}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:8641276}. Cell projection, axon {ECO:0000269|PubMed:8641276}. Synapse {ECO:0000269|PubMed:8641276}. Cell membrane {ECO:0000269|PubMed:8641276}; Single-pass type I membrane protein {ECO:0000305}. Endosome {ECO:0000269|PubMed:8641276}. Note=Detected on neuronal secretory vesicles, but not on synaptic vesicles. Colocalizes with insulin-containing secretory granules. Primarily detected on secretory vesicle membranes. 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 via the Golgi apparatus membranes. {ECO:0000269|PubMed:8641276}.; SUBCELLULAR LOCATION: [ICA512-transmembrane fragment]: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:11483505, ECO:0000269|PubMed:8641276}.; SUBCELLULAR LOCATION: [ICA512-cleaved cytosolic fragment]: Nucleus {ECO:0000250|UniProtKB:Q16849}.
uniprot
proteins
transmembrane_region
TRANSMEM 580..604; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins