PTPRS
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPTPRS, PTPSIGMA, protein tyrosine phosphatase, receptor type S, R-PTP-S, R-PTP-sigma, protein tyrosine phosphatase receptor type S
External IDsOMIM: 601576 MGI: 97815 HomoloGene: 20626 GeneCards: PTPRS
Orthologs
SpeciesHumanMouse
Entrez

5802

19280

Ensembl

ENSG00000105426

ENSMUSG00000013236

UniProt

Q13332

B0V2N1

RefSeq (mRNA)

NM_001252453
NM_001252455
NM_001252456
NM_011218

RefSeq (protein)

NP_002841
NP_570923
NP_570924
NP_570925

NP_001239382
NP_001239384
NP_001239385
NP_035348

Location (UCSC)Chr 19: 5.16 – 5.34 MbChr 17: 56.72 – 56.78 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Receptor-type tyrosine-protein phosphatase S, also known as R-PTP-S, R-PTP-sigma, or PTPσ, is an enzyme that in humans is encoded by the PTPRS gene.[5][6][7]

Function

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an extracellular region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains (D1 and D2), and thus represents a receptor-type PTP. D1 is catalytically active, while D2 is catalytically inactive. The extracellular region of this protein is composed of multiple Ig-like and fibronectin type III-like domains. Rem2 signaling affects neuronal structure and function in part by regulation of gene expression. Molecular and Cellular NeuroscienceStudies of the similar gene in mice suggested that this PTP may be involved in cell-cell interaction, primary axonogenesis, and axon guidance during embryogenesis. This PTP has been also implicated in the molecular control of adult nerve repair. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported.[7]

Clinical significance

A PTPRS protein mimetic may improve muscular and bladder control in rats with spinal cord injuries.[8][9]

Interactions

PTPRS has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000105426 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000013236 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Wagner J, Gordon LA, Heng HH, Tremblay ML, Olsen AS (Mar 1997). "Physical mapping of receptor type protein tyrosine phosphatase sigma (PTPRS) to human chromosome 19p13.3". Genomics. 38 (1): 76–8. doi:10.1006/geno.1996.0594. PMID 8954782.
  6. ^ a b Pulido R, Serra-Pagès C, Tang M, Streuli M (Jan 1996). "The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1". Proc Natl Acad Sci U S A. 92 (25): 11686–90. doi:10.1073/pnas.92.25.11686. PMC 40467. PMID 8524829.
  7. ^ a b "Entrez Gene: PTPRS protein tyrosine phosphatase, receptor type, S".
  8. ^ a b Lang BT, Cregg JM, DePaul MA, Tran AP, Xu K, Dyck SM, Madalena KM, Brown BP, Weng Y, Li S, Karimi-Abdolrezaee S, Busch SA, Shen Y, Silver J (2014). "Modulation of the proteoglycan receptor PTPσ promotes recovery after spinal cord injury". Nature. 518 (7539): 404–8. doi:10.1038/nature13974. PMC 4336236. PMID 25470046.
  9. ^ Maggie Fox (3 December 2014). "'Unprecedented': Drug May Help Heal Damaged Spine". NBC. Retrieved December 8, 2014.
  10. ^ Wallace MJ, Fladd C, Batt J, Rotin D (May 1998). "The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma". Mol. Cell. Biol. 18 (5): 2608–16. doi:10.1128/MCB.18.5.2608. PMC 110640. PMID 9566880.
  11. ^ Serra-Pagès C, Medley QG, Tang M, Hart A, Streuli M (Jun 1998). "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins". J. Biol. Chem. 273 (25): 15611–20. doi:10.1074/jbc.273.25.15611. PMID 9624153.
  12. ^ Hamasaki H, Fujitani M, Yamashita T (March 2016). "NME2 associates with PTPσ to transduce signals from chondroitin sulfate proteoglycans". Biochemical and Biophysical Research Communications. 471 (4): 522–7. doi:10.1016/j.bbrc.2016.02.042. PMID 26896769.

Further reading


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