Difference between revisions of "Phosphatase Subfamily PTPRC"

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(Domain)
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===Domain ===
 
===Domain ===
 
PTPRC has twin intracellular PTP phosphatase domains, and extracellular FN3 domains, plus a CD45-specific and a PTP-N-terminal domain found specifically in PTPRC, as annotated by InterPro. CD45 is extensively alternatively spliced.
 
PTPRC has twin intracellular PTP phosphatase domains, and extracellular FN3 domains, plus a CD45-specific and a PTP-N-terminal domain found specifically in PTPRC, as annotated by InterPro. CD45 is extensively alternatively spliced.
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==== Second phosphatase domain (D2) is inactive ====
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The functional role of the D2 domain has not yet been defined although possible roles in regulating RPTP stability, specificity, and dimerization have been suggested <cite> Barr09</cite>.
  
 
===Functions===
 
===Functions===

Revision as of 21:42, 1 October 2015


Phosphatase Classification: Fold CC1: Superfamily CC1: Family PTP: Subfamily PTPRC


PTPRC (CD45) is a vertebrate-specific receptor PTP involved in immune signaling.

Evolution

PTPRC is found as a single-copy gene in all vertebrates, including the lamprey, but not in any invertebrate.

Domain

PTPRC has twin intracellular PTP phosphatase domains, and extracellular FN3 domains, plus a CD45-specific and a PTP-N-terminal domain found specifically in PTPRC, as annotated by InterPro. CD45 is extensively alternatively spliced.

Second phosphatase domain (D2) is inactive

The functional role of the D2 domain has not yet been defined although possible roles in regulating RPTP stability, specificity, and dimerization have been suggested [1].

Functions

CD45 modulates immune function [2]. It is selectively expressed on lymphocytes and dephosphorylates and activates the src family tyrosine kinases lck, fyn and lyn in B and T cells.

Miscellaneous

PTPRC (CD45) is used in CellSearch system to detect circulating tumor cell.

References

  1. Furlan G, Minowa T, Hanagata N, Kataoka-Hamai C, and Kaizuka Y. Phosphatase CD45 both positively and negatively regulates T cell receptor phosphorylation in reconstituted membrane protein clusters. J Biol Chem. 2014 Oct 10;289(41):28514-25. DOI:10.1074/jbc.M114.574319 | PubMed ID:25128530 | HubMed [furlan14]