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Sequence homology: Cow: 92%; Dog: 100%; Guinea Pig: 79%; Horse: 93%; Human: 100%; Mouse: 85%; Pig: 93%; Rabbit: 93%; Rat: 92%
GRAIL is a type I transmembrane protein that localizes to the endocytic pathway and contains a PA (protease associated) domain and a RING-type zinc finger domain. It is a ubiquitin-protein isopeptide ligase (E3) necessary for the induction of CD4(+) T cell anergy in vivo and induced expression of this protein was observed in anergic CD4 (+) T cells, which suggested a role in the induction of anergic phenotype. It is differentially expressed in naturally occurring and peripherally induced CD25 (+) T regulatory cells and the expression is linked to the conversion of these cells to a regulatory phenotype. Expression of GRAIL in retrovirally transduced T cell hybridomas limits activation-induced IL-2 and IL-4 cytokine production. It also functions in the patterning of the dorsal ectoderm and sensitizes ectoderm to respond to neural-inducing signals.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: E3 ubiquitin-protein ligase RNF128; Gene related to anergy in lymphocytes protein; GRAIL; RING finger protein 128; RING-type E3 ubiquitin transferase RNF128; RP11-150F24.1
Gene Aliases: GRAIL; RNF128
UniProt ID: (Human) Q8TEB7
Entrez Gene ID: (Human) 79589
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