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Protein

Receptor-type tyrosine-protein phosphatase-like N

Gene

Ptprn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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). Seems to lack intrinsic enzyme activity.By similarity

GO - Molecular functioni

  • GTPase binding Source: RGD

GO - Biological processi

  • cytokine-mediated signaling pathway Source: RGD
  • dense core granule maturation Source: Ensembl
  • insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • luteinization Source: UniProtKB
  • response to cAMP Source: RGD
  • response to estrogen Source: RGD
  • response to glucose Source: RGD
  • response to insulin Source: RGD
  • response to reactive oxygen species Source: UniProtKB
  • second-messenger-mediated signaling Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase-like N
Short name:
R-PTP-N
Alternative name(s):
105 kDa islet cell antigen
BEM-3
Brain-enriched membrane-associated protein tyrosine phosphatase
ICA1051 Publication
ICA5121 Publication
PTP IA-21 Publication
PTPLP
Gene namesi
Name:Ptprn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi620777. Ptprn.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini41 – 579539ExtracellularSequence analysisAdd
BLAST
Transmembranei580 – 60425HelicalSequence analysisAdd
BLAST
Topological domaini605 – 983379CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon terminus Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • endosome Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: RGD
  • neuronal cell body Source: UniProtKB
  • perikaryon Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
  • secretory granule Source: UniProtKB
  • synapse Source: UniProtKB
  • transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasmic vesicle, Endosome, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4040By similarityAdd
BLAST
Chaini41 – 983943Receptor-type tyrosine-protein phosphatase-like NPRO_0000025453Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei311 – 3111PhosphoserineCombined sources
Modified residuei312 – 3121PhosphoserineCombined sources
Glycosylationi510 – 5101N-linked (GlcNAc...)Sequence analysis
Glycosylationi528 – 5281N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Subject to proteolytic cleavage at multiple sites (PubMed:7568143). Subject to cleavage on a pair of basic residues (By similarity).By similarity1 Publication
N-glycosylated.By similarity
O-glycosylated.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei452 – 4532CleavageBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ63259.
PRIDEiQ63259.

PTM databases

iPTMnetiQ63259.
PhosphoSiteiQ63259.

Expressioni

Tissue specificityi

Detected in pancreas islets (PubMed:7657822, PubMed:10457160). Detected in pancreas alpha, beta and delta cells, and in chromaffin cells in the adrenal medulla (PubMed:8641276). Detected in amygdala, hypothalamus, autonomous nerve fibers and ganglia, especially at synaptic contacts (PubMed:8641276). Detected in pituitary (at protein level) (PubMed:8641276, PubMed:10457160). Detected in brain, specifically in cerebral cortex, diencephalon and brain stem (PubMed:7887886).4 Publications

Gene expression databases

GenevisibleiQ63259. RN.

Interactioni

Subunit structurei

Homodimer. Interacts with phosphorylated SNTB2; this protects PTPRN against cleavage by CAPN1. Dephosphorylation of SNTB2 upon insulin stimulation disrupts the interaction and results in PTPRN cleavage. Interacts with SNX19.By similarity

GO - Molecular functioni

  • GTPase binding Source: RGD

Protein-protein interaction databases

IntActiQ63259. 2 interactions.
MINTiMINT-4566117.
STRINGi10116.ENSRNOP00000026654.

Structurei

3D structure databases

ProteinModelPortaliQ63259.
SMRiQ63259. Positions 472-562, 691-980.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini713 – 973261Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0793. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00820000127032.
HOGENOMiHOG000243992.
HOVERGENiHBG053762.
InParanoidiQ63259.
KOiK07817.
OMAiFLPYDHA.
OrthoDBiEOG7K9K30.
PhylomeDBiQ63259.
TreeFamiTF351976.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR033522. PTPRN.
IPR021613. Receptor_IA-2_dom.
IPR029403. RESP18_dom.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PANTHERiPTHR19134:SF2. PTHR19134:SF2. 1 hit.
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.

Q63259-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRPRRPGGP AGCGGSEGSG GLRLLVCLLL LSGRPGGCSA ISAHGCLFDR
60 70 80 90 100
RLCSHLEVCI QDGLFGQCQA GVGQARPLLQ VTSPVLQRLQ GVLRQLMSQG
110 120 130 140 150
LSWHDDLTQY VISQEMERIP RLRPPEPHPR DRSGSVPRRA GPAGELLSQG
160 170 180 190 200
NPTGSSPAVQ GLSRPPGDGN GAGVGSPLSS LQAELLPPLL EHLLMPPQPP
210 220 230 240 250
HPSLTYEPAL LQPYLFQQFG SRDGSRGSES ASGVVGHLAK AEDPVLFSRS
260 270 280 290 300
LSKAILGTHS GHSFGDLTGP SPAQLFQDSG LLYMAQELPV PGRARAPRLP
310 320 330 340 350
EEGGSSRAED SSEGHEEEVL GGHGEKSPPQ AVQADVSLQR LAAVLAGYGV
360 370 380 390 400
ELRQLTPEQL STLLTLLQLL PKGTGRHLGG AVNGGADVKK TIEEQMQRGD
410 420 430 440 450
TADARPPTPL LPGHPTASST SIKVRQVLSP GFPEPPKTSS PLGISAVLLE
460 470 480 490 500
KKSPLGQSQP TVVGQPSARP SAEEYGYIVT DQKPLSLVAG VKLLEILAEH
510 520 530 540 550
VHMTSGSFIN ISVVGPAVTF RIRHNEQNLS LADVTQQAGL VKSELEAQTG
560 570 580 590 600
LQILQTGVGQ REESAAVLPR QAHGISPMRS LLLTLVALAG VAGLLVALAV
610 620 630 640 650
ALCMRHHSKQ RDKERLAALG PEGAHGDTTF EYQDLCRQHM ATKSLFNRAE
660 670 680 690 700
GQPEPSRVSS VSSQFSDAAQ ASPSSHSSTP SWCEEPAQAN MDISTGHMIL
710 720 730 740 750
AYMEDHLRNR DRLAKEWQAL CAYQAEPNTC ATAQGEGNIK KNRHPDFLPY
760 770 780 790 800
DHARIKLKVE SSPSRSDYIN ASPIIEHDPR MPAYIATQGP LSHTIADFWQ
810 820 830 840 850
MVWESGCTVI VMLTPLVEDG VKQCDRYWPD EGSSLYHVYE VNLVSEHIWC
860 870 880 890 900
EDFLVRSFYL KNVQTQETRT LTQFHFLSWP AEGTPASTRP LLDFRRKVNK
910 920 930 940 950
CYRGRSCPII VHCSDGAGRT GTYILIDMVL NRMAKGVKEI DIAATLEHVR
960 970 980
DQRPGLVRSK DQFEFALTAV AEEVNAILKA LPQ
Length:983
Mass (Da):106,228
Last modified:July 15, 1998 - v2
Checksum:iBCD567DAFFFE2A2B
GO

Sequence cautioni

The sequence BAA07397.1 differs from that shown. Reason: Frameshift at positions 33 and 102. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti466 – 4661P → T in AAA83235 (PubMed:7657822).Curated
Sequence conflicti507 – 5071S → R in AAA83235 (PubMed:7657822).Curated
Sequence conflicti517 – 5171A → V in AAA83235 (PubMed:7657822).Curated
Sequence conflicti520 – 5201F → S in AAA83235 (PubMed:7657822).Curated
Sequence conflicti564 – 5641S → A in AAA83235 (PubMed:7657822).Curated
Sequence conflicti566 – 5661A → E in AAA83235 (PubMed:7657822).Curated
Sequence conflicti574 – 5741G → R in BAA07397 (PubMed:7887886).Curated
Sequence conflicti581 – 5811L → V in AAA83235 (PubMed:7657822).Curated
Sequence conflicti599 – 5991A → V in BAA08254 (Ref. 4) Curated
Sequence conflicti609 – 6091K → R in AAA83235 (PubMed:7657822).Curated
Sequence conflicti664 – 6641Q → K in AAA83235 (PubMed:7657822).Curated
Sequence conflicti672 – 6721S → N in AAA83235 (PubMed:7657822).Curated
Sequence conflicti714 – 7141A → P in AAA83235 (PubMed:7657822).Curated
Sequence conflicti716 – 7161E → K in CAA63313 (PubMed:7568143).Curated
Sequence conflicti731 – 7311A → S in AAA83235 (PubMed:7657822).Curated
Sequence conflicti953 – 9553RPG → PTC in AAA83235 (PubMed:7657822).Curated
Sequence conflicti962 – 9621Q → K in AAA83235 (PubMed:7657822).Curated
Sequence conflicti966 – 9661A → P in AAA83235 (PubMed:7657822).Curated
Sequence conflicti969 – 9691A → P in AAA83235 (PubMed:7657822).Curated
Sequence conflicti971 – 9711A → G in AAA83235 (PubMed:7657822).Curated
Sequence conflicti976 – 9761A → P in AAA83235 (PubMed:7657822).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92563 mRNA. Translation: CAA63313.1.
D38222 mRNA. Translation: BAA07397.1. Frameshift.
U40652 mRNA. Translation: AAA83235.1.
D45414 mRNA. Translation: BAA08254.1.
PIRiS54342.
RefSeqiNP_446333.1. NM_053881.1.
UniGeneiRn.11097.

Genome annotation databases

EnsembliENSRNOT00000026654; ENSRNOP00000026654; ENSRNOG00000019587.
GeneIDi116660.
KEGGirno:116660.
UCSCiRGD:620777. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92563 mRNA. Translation: CAA63313.1.
D38222 mRNA. Translation: BAA07397.1. Frameshift.
U40652 mRNA. Translation: AAA83235.1.
D45414 mRNA. Translation: BAA08254.1.
PIRiS54342.
RefSeqiNP_446333.1. NM_053881.1.
UniGeneiRn.11097.

3D structure databases

ProteinModelPortaliQ63259.
SMRiQ63259. Positions 472-562, 691-980.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ63259. 2 interactions.
MINTiMINT-4566117.
STRINGi10116.ENSRNOP00000026654.

PTM databases

iPTMnetiQ63259.
PhosphoSiteiQ63259.

Proteomic databases

PaxDbiQ63259.
PRIDEiQ63259.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026654; ENSRNOP00000026654; ENSRNOG00000019587.
GeneIDi116660.
KEGGirno:116660.
UCSCiRGD:620777. rat.

Organism-specific databases

CTDi5798.
RGDi620777. Ptprn.

Phylogenomic databases

eggNOGiKOG0793. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00820000127032.
HOGENOMiHOG000243992.
HOVERGENiHBG053762.
InParanoidiQ63259.
KOiK07817.
OMAiFLPYDHA.
OrthoDBiEOG7K9K30.
PhylomeDBiQ63259.
TreeFamiTF351976.

Miscellaneous databases

PROiQ63259.

Gene expression databases

GenevisibleiQ63259. RN.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR033522. PTPRN.
IPR021613. Receptor_IA-2_dom.
IPR029403. RESP18_dom.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PANTHERiPTHR19134:SF2. PTHR19134:SF2. 1 hit.
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...

Publicationsi

« Hide 'large scale' publications
  1. "The 37/40-kilodalton autoantigen in insulin-dependent diabetes mellitus is the putative tyrosine phosphatase IA-2."
    Passini N., Larigan J.D., Genovese S., Appella E., Sinigaglia F., Rogge L.
    Proc. Natl. Acad. Sci. U.S.A. 92:9412-9416(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION.
  2. "Cloning and expression of protein tyrosine phosphatase-like protein derived from a rat pheochromocytoma cell line."
    Kambayashi Y., Takahashi K., Bardhan S., Inagami T.
    Biochem. J. 306:331-335(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "Relationship of the 37,000- and 40,000-M(r) tryptic fragments of islet antigens in insulin-dependent diabetes to the protein tyrosine phosphatase-like molecule IA-2 (ICA512)."
    Payton M.A., Hawkes C.J., Christie M.R.
    J. Clin. Invest. 96:1506-1511(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-983, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. Itoh S., Okada M., Nakagawa H.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 396-983.
    Strain: Wistar.
    Tissue: Brain.
  5. "ICA 512, an autoantigen of type I diabetes, is an intrinsic membrane protein of neurosecretory granules."
    Solimena M., Dirkx R. Jr., Hermel J.-M., Pleasic-Williams S., Shapiro J.A., Caron L., Rabin D.U.
    EMBO J. 15:2102-2114(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Post-translational modifications of ICA512, a receptor tyrosine phosphatase-like protein of secretory granules."
    Hermel J.-M., Dirkx R., Solimena M.
    Eur. J. Neurosci. 11:2609-2620(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Dephosphorylation of beta2-syntrophin and Ca2+/mu-calpain-mediated cleavage of ICA512 upon stimulation of insulin secretion."
    Ort T., Voronov S., Guo J., Zawalich K., Froehner S.C., Zawalich W., Solimena M.
    EMBO J. 20:4013-4023(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPTPRN_RAT
AccessioniPrimary (citable) accession number: Q63259
Secondary accession number(s): Q62883, Q63795, Q64643
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: July 6, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Does not possess catalytic activity due to replacement of highly conserved residues in tyrosine-protein phosphatase domain.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

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.