Ptprn2
entrez
19276
canonical
uniprot
P80560
canonical
ensembl
ENSMUSG00000056553
resolver
ensp
ENSMUSP00000064046
resolver
ensp
ENSMUSP00000139978
resolver
enst
ENSMUST00000070733
resolver
enst
ENSMUST00000190247
resolver
genesymbol
Ptprn2
resolver
uniprot
A0A087WPZ5
resolver
uniprot
A3KN68
resolver
uniprot
O09134
resolver
uniprot
P70328
resolver
uniprot
Q1RLJ1
resolver
uniprot
Q3UU93
resolver
uniprot_entry
A0A087WPZ5_MOUSE
resolver
uniprot_entry
A3KN68_MOUSE
resolver
uniprot_entry
PTPR2_MOUSE
resolver
uniprot_entry
Q3UU93_MOUSE
resolver
uniprot_sec
O09134
resolver
uniprot_sec
P70328
resolver
uniprot_sec
Q1RLJ1
resolver
amino_acid_sequence
MGPPLPLLLLLLLPPPLPRALPAPASARGRQLPGRLGCLFEDGLCGSLETCVNDGVFGRCQKVPVMDTYRYEVPPGALLHLKVTLQKLSRTGFTWQDDYTQRVIAQELANLPKAYLWHGEASGPARSLQQNADNEKWFSLEREVALAKTLRRYLPYLELLSQTPTANAHSRIDHETRPAKGEDSSPENILTYVAHTSALTYPPATRAKYPDNLLRPFSRLQPDELSPKVDGDIDKQKLIAALGAYTAQRLPGENDPEPRYLVHGSARAPRPFSATALSQRWPPPPGDAKDSPSMDDDTLLQSLLKDLQQNSEVDRLGPLKEEKADSVAGAIQSDPAEGSQESHGRGAEGQPREQTDAPETMLQDHRLSEVDDPVYKEVNRLSFQLGDLLKDYGSPLLPEGPLLEKSSREEIKKSEQPEEVLSSEEETAGVEHVRSRTYSKDLFERKPNSEPQPRRLEDQFQNRAPELWEDEESLKLAAQGPPSGGLQLEVQPSEEQQGYILTGNNPLSPEKGKQLMDQVAHILRVPSSFFADIKVLGPAVTFKVSANIQNMTTADVIKAAADNKDQLEKATGLTILQSGIRPKGKLKLLPHQEEQEDSTKFILLTFLSIACILGVLLASSLAYCLRHNSHYKLKDKLSGLGADPSADATEAYQELCRQRMAIRPQDRSEGPHTSRINSVSSQFSDGPMPSPSARSSTSSWSEEPVQSNMDISTGHMILAYMEDHLKNKNRLEKEWEALCAYQAEPNSSLVAQREENAPKNRSLAVLTYDHSRILLKSQNSHGSSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCAVIVMLTPLSENGVRQCHHYWPDEGSNLYHVYEVNLVSEHIWCQDFLVRSFYLKNLQTNETRTVTQFHFLSWYDQGVPSSTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYVLIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAILKALPQ
uniprot
proteins
ec_number
3.1.3.-
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
FUNCTION: Plays a role in vesicle-mediated secretory processes (PubMed:21732083). 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 (PubMed:21732083). Plays a role in insulin secretion in response to glucose stimuli (PubMed:15220191, PubMed:16418280, PubMed:21732083). 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) (PubMed:16269463). Required to maintain normal levels of renin expression and renin release (PubMed:19019914). May regulate catalytic active protein-tyrosine phosphatases such as PTPRA through dimerization (PubMed:12364328). 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 (By similarity). {ECO:0000250|UniProtKB:Q63475, ECO:0000250|UniProtKB:Q92932, ECO:0000269|PubMed:12364328, ECO:0000269|PubMed:15220191, ECO:0000269|PubMed:16269463, ECO:0000269|PubMed:16418280, ECO:0000269|PubMed:19019914, ECO:0000269|PubMed:21732083}.
uniprot
proteins
mass_dalton
111497
uniprot
proteins
mutagenesis
MUTAGEN 990..991; /note="EE->AA: Impairs localization to secretory granules, promotes location at the TGN, decreases interaction with alpha- and gamma-type adaptin subunits."; /evidence="ECO:0000269|PubMed:16262730, ECO:0000269|PubMed:21210912"; MUTAGEN 995..996; /note="IL->AA: Impairs localization to secretory granules, promotes location at the plasma membrane, defective ind gamma endocytosis, highly decreases interaction with alpha- and gamma-type adaptin subunits."; /evidence="ECO:0000269|PubMed:16262730
uniprot
proteins
post_translational_modification
PTM: Subject to proteolytic cleavage at multiple sites during maturation of secretory granules. In the brain at least IA-2beta71, IA-2beta64 and IA-2beta60 have been detected, in the pancreas and a pancreatic beta cell line only IA-2beta60 has been detected. {ECO:0000269|PubMed:17611635, ECO:0000269|PubMed:8637868}.
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
pubmed
12364328
uniprot
proteins
pubmed
15220191
uniprot
proteins
pubmed
15485654
uniprot
proteins
pubmed
16262730
uniprot
proteins
pubmed
16269463
uniprot
proteins
pubmed
16418280
uniprot
proteins
pubmed
17611635
uniprot
proteins
pubmed
19019914
uniprot
proteins
pubmed
19361477
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21210912
uniprot
proteins
pubmed
21544547
uniprot
proteins
pubmed
21732083
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
8637868
uniprot
proteins
pubmed
8681804
uniprot
proteins
sequence_length
1001
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:19361477}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:19361477}; Single-pass type I membrane protein {ECO:0000305}. Note=Predominantly found on dense-core secretory granules. Sorting to secretory granules in part is dependent of the N-terminal pro domain of the precursor and its interaction with CPE. 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. {ECO:0000250|UniProtKB:Q63475, ECO:0000269|PubMed:15485654, ECO:0000269|PubMed:21210912, ECO:0000305}.; SUBCELLULAR LOCATION: [IA-2beta60]: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 601..621; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins