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UniProtKB - Q63259 (PTPRN_RAT)

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Protein

Receptor-type tyrosine-protein phosphatase-like N

Gene

Ptprn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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). Required to maintain normal levels of renin expression and renin release. Seems to lack intrinsic enzyme activity.By similarity
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).By similarity
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).By similarity1 Publication

Caution

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

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

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
  • positive regulation of transcription by RNA polymerase II Source: Ensembl
  • positive regulation of type B pancreatic cell proliferation 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
  • transcription, DNA-templated Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionReceptor
Biological processTranscription, Transcription regulation

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
Cleaved into the following 3 chains:
ICA512-N-terminal fragment
Short name:
ICA512-NTF
ICA512-transmembrane fragment
Short name:
ICA512-TMF
ICA512-cleaved cytosolic fragment
Short name:
ICA512-CCF
Gene namesi
Name:Ptprn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi620777 Ptprn

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini41 – 579LumenalSequence analysisAdd BLAST539
Transmembranei580 – 604HelicalSequence analysisAdd BLAST25
Topological domaini605 – 983CytoplasmicSequence analysisAdd BLAST379

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 40By similarityAdd BLAST40
ChainiPRO_000002545341 – 983Receptor-type tyrosine-protein phosphatase-like NAdd BLAST943
ChainiPRO_000043808541 – 452ICA512-N-terminal fragmentBy similarityAdd BLAST412
ChainiPRO_0000438086453 – 983ICA512-transmembrane fragmentBy similarityAdd BLAST531
ChainiPRO_0000438087663 – 983ICA512-cleaved cytosolic fragmentBy similarityAdd BLAST321

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi46Interchain (with C-46 or C-53); in multimeric formBy similarity
Disulfide bondi53Interchain (with C-46 or C-53); in multimeric formBy similarity
Disulfide bondi59 ↔ 68By similarity
Modified residuei311PhosphoserineCombined sources1
Modified residuei312PhosphoserineCombined sources1
Glycosylationi510N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi528N-linked (GlcNAc...) asparagineSequence analysis1
Cross-linki758Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

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).By similarity2 Publications
N-glycosylated.By similarity
O-glycosylated.By similarity
Sumoylated at two sites including Lys-758. Sumoylation decreases interaction with STAT5.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei452 – 453CleavageBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ63259
PRIDEiQ63259

PTM databases

iPTMnetiQ63259
PhosphoSitePlusiQ63259

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

BgeeiENSRNOG00000019587
GenevisibleiQ63259 RN

Interactioni

Subunit structurei

Homodimer; shown for the unprocessed protein (proICA512) in the endoplasmic reticulum and resolved during protein maturation as ICA512-TMF seems to be predominantly monomeric in secretory granules; however, ICA512-CCF interacts with ICA512-TMF disrupting the ICA512-TMF:SNTB2 complex. The isolated lumenal RESP18 homology domain has been shown to form disulfide-linked homooligomers. Interacts (via cytoplasmic domain) with phosphorylated SNTB2; this protects PTPRN against cleavage by CAPN1 to produce ICA512-CCF. Dephosphorylation of SNTB2 upon insulin stimulation disrupts the interaction and results in PTPRN cleavage. Interacts with SNX19. ICA512-CCF interacts with PIAS4; in the nucleus. Interacts with STAT5B (phosphorylated); down-regulated by ICA512-CCF sumoylation; ICA512-CCF prevents STAT5B dephosphorylation; ICA512-CCF mediates interaction of STAT5B with PIAS4. Interacts (via RESP18 homology domain) with insulin and proinsulin. Interacts with PTPRN2, PTPRA and PTPRE.By similarity

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

IntActiQ63259, 2 interactors
STRINGi10116.ENSRNOP00000026654

Structurei

3D structure databases

ProteinModelPortaliQ63259
SMRiQ63259
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini713 – 973Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST261

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni41 – 137RESP18 homology domainBy similarityAdd BLAST97
Regioni453 – 579Sufficient for dimerization of proICA512By similarityAdd BLAST127
Regioni605 – 736Sufficient for dimerization of proICA512By similarityAdd BLAST132

Domaini

The RESP18 homology domain is sufficient for targeting proICA512 to secretory granules.By similarity

Sequence similaritiesi

Belongs to the protein-tyrosine phosphatase family. Receptor class 8 subfamily.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0793 Eukaryota
COG5599 LUCA
GeneTreeiENSGT00920000148980
HOGENOMiHOG000243992
HOVERGENiHBG053762
InParanoidiQ63259
KOiK07817
OMAiFLPYDHA
OrthoDBiEOG091G0LUR
PhylomeDBiQ63259
TreeFamiTF351976

Family and domain databases

Gene3Di3.30.70.2470, 1 hit
3.90.190.10, 1 hit
InterProiView protein in InterPro
IPR033522 IA-2/IA-2_beta
IPR029021 Prot-tyrosine_phosphatase-like
IPR000242 PTPase_domain
IPR021613 Receptor_IA-2_dom
IPR038112 Receptor_IA-2_ectodomain_sf
IPR029403 RESP18_dom
IPR016130 Tyr_Pase_AS
IPR003595 Tyr_Pase_cat
IPR000387 TYR_PHOSPHATASE_dom
PANTHERiPTHR19134:SF2 PTHR19134:SF2, 1 hit
PfamiView protein in Pfam
PF11548 Receptor_IA-2, 1 hit
PF14948 RESP18, 1 hit
PF00102 Y_phosphatase, 1 hit
PRINTSiPR00700 PRTYPHPHTASE
SMARTiView protein in SMART
SM00194 PTPc, 1 hit
SM00404 PTPc_motif, 1 hit
SUPFAMiSSF52799 SSF52799, 1 hit
PROSITEiView protein in PROSITE
PS00383 TYR_PHOSPHATASE_1, 1 hit
PS50056 TYR_PHOSPHATASE_2, 1 hit
PS50055 TYR_PHOSPHATASE_PTP, 1 hit

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 differs from that shown. Reason: Frameshift at positions 33 and 102.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti466P → T in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti507S → R in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti517A → V in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti520F → S in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti564S → A in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti566A → E in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti574G → R in BAA07397 (PubMed:7887886).Curated1
Sequence conflicti581L → V in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti599A → V in BAA08254 (Ref. 4) Curated1
Sequence conflicti609K → R in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti664Q → K in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti672S → N in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti714A → P in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti716E → K in CAA63313 (PubMed:7568143).Curated1
Sequence conflicti731A → S in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti953 – 955RPG → PTC in AAA83235 (PubMed:7657822).Curated3
Sequence conflicti962Q → K in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti966A → P in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti969A → P in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti971A → G in AAA83235 (PubMed:7657822).Curated1
Sequence conflicti976A → P in AAA83235 (PubMed:7657822).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiPTPRN_RAT
AccessioniPrimary (citable) accession number: Q63259
Secondary accession number(s): Q62883, Q63795, Q64643
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: June 20, 2018
This is version 137 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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