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Protein

Receptor-type tyrosine-protein phosphatase N2

Gene

PTPRN2

Organism
Macaca nemestrina (Pig-tailed macaque)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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. May regulate catalytic active protein-tyrosine phosphatases such as PTPRA through dimerization. Has phosphatidylinositol phosphatase activity; the PIPase activity is involved in its ability to regulate insulin secretion. Can dephosphorylate phosphatidylinositol 4,5-biphosphate, phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate. 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 hydrolyzation of PI(4,5)P2 cofilin is released from the plasma membrane and acts in the cytoplasm in severing F-actin filaments.By similarity

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei911SubstrateBy similarity1
Active sitei943Phosphocysteine intermediatePROSITE-ProRule annotation1
Binding sitei988SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase, Receptor

Keywords - Biological processi

Lipid metabolism, Phospholipid metabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase N2 (EC:3.1.3.-, EC:3.1.3.48)
Short name:
R-PTP-N2
Alternative name(s):
M1851
Cleaved into the following chain:
Gene namesi
Name:PTPRN2
OrganismiMacaca nemestrina (Pig-tailed macaque)
Taxonomic identifieri9545 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Subcellular locationi

  • Cytoplasmic vesiclesecretory vesicle membrane By similarity; Single-pass type I membrane protein By similarity
  • Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane By similarity; Single-pass type I membrane protein By similarity

  • Note: 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. 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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 613ExtracellularSequence analysisAdd BLAST594
Transmembranei614 – 634HelicalSequence analysisAdd BLAST21
Topological domaini635 – 1013CytoplasmicSequence analysisAdd BLAST379

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000002545520 – 1013Receptor-type tyrosine-protein phosphatase N2Add BLAST994
ChainiPRO_0000438069500 – 1013IA-2beta60By similarityAdd BLAST514

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei434PhosphoserineBy similarity1
Modified residuei435PhosphoserineBy similarity1
Glycosylationi562N-linked (GlcNAc...)Sequence analysis1
Modified residuei690PhosphoserineBy similarity1
Modified residuei696PhosphoserineBy similarity1
Modified residuei968N6-acetyllysineBy similarity1

Post-translational modificationi

Subject to proteolytic cleavage at multiple sites.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei425 – 426CleavageBy similarity2

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiO02695.

Expressioni

Tissue specificityi

Detected in pancreatic islets and adrenal medulla.1 Publication

Interactioni

Subunit structurei

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). Interacts with AP2M1; indicative for an association with adaptor protein complex 2 (AP-2). Interacts with MYO5A.By similarity

Structurei

3D structure databases

ProteinModelPortaliO02695.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini743 – 1003Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST261

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 419Involved in localization to secretory granules; interaction with CPEBy similarityAdd BLAST419
Regioni943 – 949Substrate bindingBy similarity7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi664 – 673Tyrosine-based internalization motifBy similarity10
Motifi1002 – 1008Leucine-based sorting signalBy similarity7

Domaini

The tyrosine-based internalization signal is proposed to function in clathrin-mediated endocytosis and recycling.By similarity
The leucine-based sorting signal is proposed to function in trafficking at the plasma membrane.By similarity

Sequence similaritiesi

Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG105788.
OrthoDBiEOG091G0LUR.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR021613. Receptor_IA-2_dom.
IPR029403. RESP18_dom.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF11548. Receptor_IA-2. 1 hit.
PF14948. RESP18. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O02695-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPLLLLLL LLLPPRVLPA APSSVPHGRQ LPGRLGCLLE EGLCGASEAC
60 70 80 90 100
VNDGVFGRCQ KVPAMDFYRY EVSPVALQRL RVALQKLSGT GFTWQDDYTQ
110 120 130 140 150
YVMDQELADL PKTYLRHPEA SGPARPSKHS IGSERRYSQE GGAALAKAFR
160 170 180 190 200
RHLPFLEALS QAPASDALAR TRMAQDRPRA EGDDRFSKSI LTYVAHTSVL
210 220 230 240 250
TYPPGPQAQL PEDLLPRTLS QLQPDELSPK VDSSVERHHL MAALSAYAAQ
260 270 280 290 300
RPPAPPGKGS LEPQYLLRAP SRMPRPLLSP AVPQKWPSPL GDPEDPPSTG
310 320 330 340 350
EGARIHTLLK DLQRQPAEAR GLSDLELDSM AELMAGLMQG MDHRGALGGP
360 370 380 390 400
GKAALGESGE QADGPKAALR GESFPDDGVQ DDDDRLYQEV HRLSATLGGL
410 420 430 440 450
LQDHGSRLSP GALPFAKPLK MERKKSERPE ASLSSEEETA GVENVKSQTY
460 470 480 490 500
SKDLLGQQPH SEPGAGAFGE LQNQMPGPSE EEQSLPAGAQ EALGDGLQLE
510 520 530 540 550
VKPSEEEARG YIVTDRDPLR PEEGRQLVED VARLLQMPSS TFADVEVLGP
560 570 580 590 600
AVTFKVGANV QNVTTADVEK ATVDNKDKLE ETSGLKILQT GVGSKSKLKF
610 620 630 640 650
LPPQAEQEDS TKFIALTLVS LACILGVLLA SGLIYCLRHS SQHRLKEKLS
660 670 680 690 700
GLGRDPGADA TAAYQELCRQ RMATRPPDRP EGPHTSRISS VSSQFSDGPM
710 720 730 740 750
PSPSARSSAS SWSEEPVQSN MDISTGHMIL SYMEDHLKNK NRLEKEWEAL
760 770 780 790 800
CAYQAEPNSS LVAQKEENVP KNRSLAVLTY DHSRVLLKAE NSHSHSDYIN
810 820 830 840 850
ASPIMDHDPR NPAYIATQGP LPATVADFWQ MVWESGCVVI VMLTPLTENG
860 870 880 890 900
VRQCYHYWPD EGSNLYHIYE VNLVSEHIWC EDFLVRSFYL KNLQTNETRT
910 920 930 940 950
VTQFHFLSWY DRGVPSSSRS LLDFRRKVNK CYRGRSCPII VHCSDGAGRS
960 970 980 990 1000
GTYVLIDMVL NKMAKGAKEI DIAATLEHLR DQRPGMVQTK EQFEFALTAV
1010
AEEVNAILKA LPQ
Length:1,013
Mass (Da):111,191
Last modified:July 1, 1997 - v1
Checksum:i4808D43937A2EF59
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91574 mRNA. Translation: AAC51186.1.
RefSeqiNP_001292849.1. NM_001305920.1.

Genome annotation databases

GeneIDi105474981.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91574 mRNA. Translation: AAC51186.1.
RefSeqiNP_001292849.1. NM_001305920.1.

3D structure databases

ProteinModelPortaliO02695.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO02695.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi105474981.

Organism-specific databases

CTDi5799.

Phylogenomic databases

HOVERGENiHBG105788.
OrthoDBiEOG091G0LUR.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR021613. Receptor_IA-2_dom.
IPR029403. RESP18_dom.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF11548. Receptor_IA-2. 1 hit.
PF14948. RESP18. 1 hit.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPTPR2_MACNE
AccessioniPrimary (citable) accession number: O02695
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: November 30, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Has no tyrosine-protein phosphatase activity at mild acidic conditions (pH 5.5). The in vivo relevance of the low PPase activity for the human protein 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.Curated

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.